MASCOT Search Results
Protein View: ANXA5_HUMAN
Annexin A5 OS=Homo sapiens GN=ANXA5 PE=1 SV=2
AC P08758; D3DNW7; Q6FHB3; Q6FI16; Q8WV69; Q9UDH9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 09-DEC-2015, entry version 185.
DE RecName: Full=Annexin A5;
DE AltName: Full=Anchorin CII;
DE AltName: Full=Annexin V;
DE AltName: Full=Annexin-5;
DE AltName: Full=Calphobindin I;
DE Short=CBP-I;
DE AltName: Full=Endonexin II;
DE AltName: Full=Lipocortin V;
DE AltName: Full=Placental anticoagulant protein 4;
DE Short=PP4;
DE AltName: Full=Placental anticoagulant protein I;
DE Short=PAP-I;
DE AltName: Full=Thromboplastin inhibitor;
DE AltName: Full=Vascular anticoagulant-alpha;
DE Short=VAC-alpha;
GN Name=ANXA5; Synonyms=ANX5, ENX2, PP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2964863; DOI=10.1021/bi00399a011;
RA Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.;
RT "Primary structure of human placental anticoagulant protein.";
RL Biochemistry 26:8087-8092(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-320.
RX PubMed=2963810;
RA Iwasaki A., Suda M., Nakao H., Nagoya T., Saino Y., Arai K.,
RA Mizoguchi T., Sato F., Yoshizaki H., Hirata M., Miyata T., Shidara Y.,
RA Murata M., Maki M.;
RT "Structure and expression of cDNA for an inhibitor of blood
RT coagulation isolated from human placenta: a new lipocortin-like
RT protein.";
RL J. Biochem. 102:1261-1273(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2455636; DOI=10.1111/j.1432-1033.1988.tb14139.x;
RA Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G.,
RA Stratowa C., Hauptmann R.;
RT "Cloning and expression of cDNA for human vascular anticoagulant, a
RT Ca2+-dependent phospholipid-binding protein.";
RL Eur. J. Biochem. 174:585-592(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2967291;
RA Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T.;
RT "Cloning and expression of cDNA for human endonexin II, a Ca2+ and
RT phospholipid binding protein.";
RL J. Biol. Chem. 263:8037-8043(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2968983;
RA Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA Hession C., Frey A.Z., Wallner B.P.;
RT "Five distinct calcium and phospholipid binding proteins share
RT homology with lipocortin I.";
RL J. Biol. Chem. 263:10799-10811(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2967495; DOI=10.1073/pnas.85.11.3708;
RA Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F.,
RA Kuepper H.;
RT "Characterization of cDNA encoding human placental anticoagulant
RT protein (PP4): homology with the lipocortin family.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=7958998; DOI=10.1016/0378-1119(94)90157-0;
RA Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T.;
RT "The gene encoding human annexin V has a TATA-less promoter with a
RT high G+C content.";
RL Gene 149:253-260(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8034319; DOI=10.1006/geno.1994.1201;
RA Cookson B.T., Engelhardt S., Smith C., Bamford H.A., Prochazka M.,
RA Tait J.F.;
RT "Organization of the human annexin V (ANX5) gene.";
RL Genomics 20:463-467(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [14]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2532007;
RA Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H.,
RA Cavadore J.-C., Conard J., Russo-Marie F., Lederer F.;
RT "A 32 kDa lipocortin from human mononuclear cells appears to be
RT identical with the placental inhibitor of blood coagulation.";
RL Biochem. J. 263:929-935(1989).
RN [15]
RP PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
RL Submitted (JAN-2005) to UniProtKB.
RN [16]
RP PROTEIN SEQUENCE OF 21-31; 93-108; 176-188 AND 304-319, AND
RP INTERACTION WITH HBV.
RX PubMed=8249278; DOI=10.1006/viro.1993.1628;
RA Hertogs K., Leenders W.P., Depla E., De Bruin W.C., Meheus L.,
RA Raymackers J., Moshage H., Yap S.H.;
RT "Endonexin II, present on human liver plasma membranes, is a specific
RT binding protein of small hepatitis B virus (HBV) envelope protein.";
RL Virology 197:549-557(1993).
RN [17]
RP PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
RX PubMed=2957692; DOI=10.1073/pnas.84.17.6078;
RA Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T.;
RT "Structural and functional characterization of endonexin II, a
RT calcium- and phospholipid-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987).
RN [18]
RP PROTEIN SEQUENCE OF 85-93.
RC TISSUE=Placenta;
RX PubMed=2974032;
RA Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
RA de Haen C.;
RT "Sedimentation equilibrium analysis of five lipocortin-related
RT phospholipase A2 inhibitors from human placenta. Evidence against a
RT mechanistically relevant association between enzyme and inhibitor.";
RL J. Biol. Chem. 263:18657-18663(1988).
RN [19]
RP PROTEIN SEQUENCE OF 152-161 AND 246-260.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by
RT a proteomics survey.";
RL Mol. Cell 23:607-618(2006).
RN [21]
RP INVOLVEMENT IN RPRGL3.
RX PubMed=17339269; DOI=10.1093/hmg/ddm017;
RA Bogdanova N., Horst J., Chlystun M., Croucher P.J., Nebel A.,
RA Bohring A., Todorova A., Schreiber S., Gerke V., Krawczak M.,
RA Markoff A.;
RT "A common haplotype of the annexin A5 (ANXA5) gene promoter is
RT associated with recurrent pregnancy loss.";
RL Hum. Mol. Genet. 16:573-578(2007).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-79 AND
RP LYS-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP S-NITROSYLATION, AND DOMAIN.
RX PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
RA Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
RA Fox P.L.;
RT "Target-selective protein S-nitrosylation by sequence motif
RT recognition.";
RL Cell 159:623-634(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=2147412;
RA Huber R., Roemisch J., Paques E.-P.;
RT "The crystal and molecular structure of human annexin V, an
RT anticoagulant protein that binds to calcium and membranes.";
RL EMBO J. 9:3867-3874(1990).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2148156; DOI=10.1016/0014-5793(90)81428-Q;
RA Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P.;
RT "The calcium binding sites in human annexin V by crystal structure
RT analysis at 2.0-A resolution. Implications for membrane binding and
RT calcium channel activity.";
RL FEBS Lett. 275:15-21(1990).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1311770; DOI=10.1016/0022-2836(92)90984-R;
RA Huber R., Berendes R., Burger A., Schneider M., Karshikov A.,
RA Luecke H., Roemisch J., Paques E.-P.;
RT "Crystal and molecular structure of human annexin V after refinement.
RT Implications for structure, membrane binding and ion channel formation
RT of the annexin family of proteins.";
RL J. Mol. Biol. 223:683-704(1992).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9398511; DOI=10.1006/jmbi.1997.1375;
RA Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M.;
RT "Crystal structure of annexin V with its ligand K-201 as a calcium
RT channel activity inhibitor.";
RL J. Mol. Biol. 274:16-20(1997).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9435213; DOI=10.1073/pnas.95.2.455;
RA Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L.;
RT "Residue-specific bioincorporation of non-natural, biologically active
RT amino acids into proteins as possible drug carriers: structure and
RT stability of the per-thiaproline mutant of annexin V.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998).
CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC indirect inhibitor of the thromboplastin-specific complex, which
CC is involved in the blood coagulation cascade.
CC -!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity). Interacts
CC with hepatitis B virus (HBV). {ECO:0000250,
CC ECO:0000269|PubMed:8249278}.
CC -!- INTERACTION:
CC Q9BSI4:TINF2; NbExp=2; IntAct=EBI-296601, EBI-717399;
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC calcium and phospholipid.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and
CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
CC implicating the iNOS-S100A8/9 transnitrosylase complex.
CC {ECO:0000305|PubMed:25417112}.
CC -!- DISEASE: Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: A
CC common complication of pregnancy, resulting in spontaneous
CC abortion before the fetus has reached viability. The term includes
CC all miscarriages from the time of conception until 24 weeks of
CC gestation. Recurrent pregnancy loss is defined as 3 or more
CC consecutive spontaneous abortions. {ECO:0000269|PubMed:17339269}.
CC Note=Disease susceptibility is associated with variations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 4 annexin repeats. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=R&D Systems' cytokine source book: Annexin V;
CC URL="http://www.rndsystems.com/molecule_detail.aspx?m=1063";
DR EMBL; M18366; AAA35570.1; -; mRNA.
DR EMBL; D00172; BAA00122.1; -; mRNA.
DR EMBL; X12454; CAA30985.1; -; mRNA.
DR EMBL; J03745; AAA52386.1; -; mRNA.
DR EMBL; M21731; AAA36166.1; -; mRNA.
DR EMBL; M19384; AAB59545.1; -; mRNA.
DR EMBL; U01691; AAB40047.1; -; Genomic_DNA.
DR EMBL; U01681; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01682; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01683; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01685; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01686; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01687; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01689; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01690; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U05770; AAB60648.1; -; Genomic_DNA.
DR EMBL; U05760; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05761; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05762; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05764; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05765; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05766; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05767; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05768; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05769; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; AK312644; BAG35528.1; -; mRNA.
DR EMBL; CR536522; CAG38759.1; -; mRNA.
DR EMBL; CR541842; CAG46640.1; -; mRNA.
DR EMBL; AC096730; AAY40954.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05257.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05258.1; -; Genomic_DNA.
DR EMBL; BC001429; AAH01429.1; -; mRNA.
DR EMBL; BC004993; AAH04993.1; -; mRNA.
DR EMBL; BC012804; AAH12804.1; -; mRNA.
DR EMBL; BC012822; AAH12822.1; -; mRNA.
DR EMBL; BC018671; AAH18671.1; -; mRNA.
DR CCDS; CCDS3720.1; -.
DR PIR; D29250; AQHUP.
DR RefSeq; NP_001145.1; NM_001154.3.
DR UniGene; Hs.480653; -.
DR PDB; 1ANW; X-ray; 2.40 A; A/B=2-320.
DR PDB; 1ANX; X-ray; 1.90 A; A/B/C=2-320.
DR PDB; 1AVH; X-ray; 2.30 A; A/B=1-320.
DR PDB; 1AVR; X-ray; 2.30 A; A=1-320.
DR PDB; 1HAK; X-ray; 3.00 A; A/B=1-320.
DR PDB; 1HVD; X-ray; 2.00 A; A=2-320.
DR PDB; 1HVE; X-ray; 2.30 A; A=2-320.
DR PDB; 1HVF; X-ray; 2.00 A; A=2-320.
DR PDB; 1HVG; X-ray; 3.00 A; A=2-320.
DR PDB; 1SAV; X-ray; 2.50 A; A=1-320.
DR PDB; 2XO2; X-ray; 2.80 A; A=1-320.
DR PDB; 2XO3; X-ray; 2.30 A; A=1-320.
DR PDBsum; 1ANW; -.
DR PDBsum; 1ANX; -.
DR PDBsum; 1AVH; -.
DR PDBsum; 1AVR; -.
DR PDBsum; 1HAK; -.
DR PDBsum; 1HVD; -.
DR PDBsum; 1HVE; -.
DR PDBsum; 1HVF; -.
DR PDBsum; 1HVG; -.
DR PDBsum; 1SAV; -.
DR PDBsum; 2XO2; -.
DR PDBsum; 2XO3; -.
DR ProteinModelPortal; P08758; -.
DR SMR; P08758; 3-318.
DR BioGrid; 106805; 41.
DR IntAct; P08758; 20.
DR MINT; MINT-1382250; -.
DR STRING; 9606.ENSP00000296511; -.
DR PhosphoSite; P08758; -.
DR BioMuta; ANXA5; -.
DR DMDM; 113960; -.
DR OGP; P08758; -.
DR REPRODUCTION-2DPAGE; IPI00329801; -.
DR REPRODUCTION-2DPAGE; P08758; -.
DR PaxDb; P08758; -.
DR PeptideAtlas; P08758; -.
DR PRIDE; P08758; -.
DR DNASU; 308; -.
DR Ensembl; ENST00000296511; ENSP00000296511; ENSG00000164111.
DR GeneID; 308; -.
DR KEGG; hsa:308; -.
DR UCSC; uc003idu.4; human.
DR CTD; 308; -.
DR GeneCards; ANXA5; -.
DR HGNC; HGNC:543; ANXA5.
DR HPA; CAB003677; -.
DR HPA; HPA035330; -.
DR MalaCards; ANXA5; -.
DR MIM; 131230; gene.
DR MIM; 614391; phenotype.
DR neXtProt; NX_P08758; -.
DR PharmGKB; PA24833; -.
DR eggNOG; KOG0819; Eukaryota.
DR eggNOG; ENOG410XPUN; LUCA.
DR HOGENOM; HOG000158803; -.
DR HOVERGEN; HBG061815; -.
DR InParanoid; P08758; -.
DR KO; K16646; -.
DR OMA; KCIRSVP; -.
DR OrthoDB; EOG74XS72; -.
DR PhylomeDB; P08758; -.
DR TreeFam; TF105452; -.
DR SignaLink; P08758; -.
DR ChiTaRS; ANXA5; human.
DR EvolutionaryTrace; P08758; -.
DR GeneWiki; Annexin_A5; -.
DR GenomeRNAi; 308; -.
DR NextBio; 1243; -.
DR PRO; PR:P08758; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; P08758; -.
DR CleanEx; HS_ANXA5; -.
DR ExpressionAtlas; P08758; baseline and differential.
DR Genevisible; P08758; HS.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0072563; C:endothelial microparticle; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0098779; P:mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0043086; P:negative regulation of catalytic activity; TAS:GOC.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:1901317; P:regulation of sperm motility; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0098792; P:xenophagy; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR015473; Annexins_V.
DR InterPro; IPR002392; AnnexinV.
DR PANTHER; PTHR10502:SF26; PTHR10502:SF26; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00201; ANNEXINV.
DR SMART; SM00335; ANX; 4.
DR PROSITE; PS00223; ANNEXIN; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Blood coagulation; Calcium;
KW Calcium/phospholipid-binding; Complete proteome;
KW Direct protein sequencing; Hemostasis; Phosphoprotein;
KW Reference proteome; Repeat; S-nitrosylation.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
FT ECO:0000269|PubMed:2963810}.
FT CHAIN 2 320 Annexin A5.
FT /FTId=PRO_0000067487.
FT REPEAT 24 84 Annexin 1.
FT REPEAT 96 156 Annexin 2.
FT REPEAT 180 240 Annexin 3.
FT REPEAT 255 315 Annexin 4.
FT MOTIF 314 319 [IL]-x-C-x-x-[DE] motif.
FT {ECO:0000305|PubMed:25417112}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:19413330}.
FT MOD_RES 37 37 Phosphoserine.
FT {ECO:0000250|UniProtKB:P48036}.
FT MOD_RES 70 70 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 76 76 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 79 79 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 97 97 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 101 101 N6-acetyllysine.
FT {ECO:0000244|PubMed:16916647}.
FT MOD_RES 290 290 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P48036}.
FT CONFLICT 135 135 S -> L (in Ref. 10; CAG38759).
FT {ECO:0000305}.
FT CONFLICT 279 279 I -> T (in Ref. 13; AAH18671).
FT {ECO:0000305}.
FT HELIX 17 28 {ECO:0000244|PDB:1ANX}.
FT STRAND 29 32 {ECO:0000244|PDB:1ANX}.
FT HELIX 35 43 {ECO:0000244|PDB:1ANX}.
FT HELIX 47 61 {ECO:0000244|PDB:1ANX}.
FT HELIX 65 72 {ECO:0000244|PDB:1ANX}.
FT HELIX 75 85 {ECO:0000244|PDB:1ANX}.
FT HELIX 88 100 {ECO:0000244|PDB:1ANX}.
FT STRAND 102 104 {ECO:0000244|PDB:1ANX}.
FT HELIX 107 116 {ECO:0000244|PDB:1ANX}.
FT HELIX 119 133 {ECO:0000244|PDB:1ANX}.
FT HELIX 137 144 {ECO:0000244|PDB:1ANX}.
FT HELIX 147 157 {ECO:0000244|PDB:1ANX}.
FT HELIX 169 182 {ECO:0000244|PDB:1ANX}.
FT TURN 183 185 {ECO:0000244|PDB:1ANX}.
FT STRAND 186 188 {ECO:0000244|PDB:1ANX}.
FT HELIX 191 200 {ECO:0000244|PDB:1ANX}.
FT HELIX 203 217 {ECO:0000244|PDB:1ANX}.
FT HELIX 221 228 {ECO:0000244|PDB:1ANX}.
FT HELIX 231 245 {ECO:0000244|PDB:1ANX}.
FT HELIX 247 256 {ECO:0000244|PDB:1ANX}.
FT HELIX 257 259 {ECO:0000244|PDB:1ANX}.
FT STRAND 260 263 {ECO:0000244|PDB:1ANX}.
FT HELIX 266 276 {ECO:0000244|PDB:1ANX}.
FT TURN 277 280 {ECO:0000244|PDB:1ANX}.
FT HELIX 281 290 {ECO:0000244|PDB:1ANX}.
FT STRAND 292 294 {ECO:0000244|PDB:1HVG}.
FT HELIX 296 303 {ECO:0000244|PDB:1ANX}.
FT HELIX 306 316 {ECO:0000244|PDB:1ANX}.
SQ SEQUENCE 320 AA; 35937 MW; 45E14E3964BA4D1A CRC64;
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE
ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF
QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI
KGDTSGDYKK ALLLLCGEDD