ID ANXA2_HUMAN Reviewed; 339 AA. AC P07355; Q567R4; Q6N0B3; Q8TBV2; Q96DD5; Q9UDH8; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 259. DE RecName: Full=Annexin A2; DE AltName: Full=Annexin II; DE AltName: Full=Annexin-2; DE AltName: Full=Calpactin I heavy chain; DE AltName: Full=Calpactin-1 heavy chain; DE AltName: Full=Chromobindin-8; DE AltName: Full=Lipocortin II; DE AltName: Full=Placental anticoagulant protein IV; DE Short=PAP-IV; DE AltName: Full=Protein I; DE AltName: Full=p36; GN Name=ANXA2; Synonyms=ANX2, ANX2L4, CAL1H, LPC2D; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=3013422; DOI=10.1016/0092-8674(86)90736-1; RA Huang K.-S., Wallner B.P., Mattaliano R.J., Tizard R., Burne C., Frey A., RA Hession C., McGray P., Sinclair L.K., Chow E.P., Browning J.L., RA Ramachandran K.L., Tang J., Smart J.E., Pepinsky R.B.; RT "Two human 35 kd inhibitors of phospholipase A2 are related to substrates RT of pp60v-src and of the epidermal growth factor receptor/kinase."; RL Cell 46:191-199(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2174397; DOI=10.1016/0378-1119(90)90367-z; RA Spano F., Raugei G., Palla E., Colella C., Melli M.; RT "Characterization of the human lipocortin-2-encoding multigene family: its RT structure suggests the existence of a short amino acid unit undergoing RT duplication."; RL Gene 95:243-251(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-98. RC TISSUE=Brain, Colon, Pancreas, Prostate, Skin, Testis, and Urinary RC bladder; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 2-10; 38-47; 50-63; 69-77; 89-115; 153-169 AND 213-220, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Colon adenocarcinoma, and Osteosarcoma; RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Bensaad K., RA Vousden K.H.; RL Submitted (FEB-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339. RX PubMed=1825830; DOI=10.1016/s0021-9258(19)67770-7; RA Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K.; RT "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is RT part of the primer recognition protein complex that interacts with DNA RT polymerase alpha."; RL J. Biol. Chem. 266:5169-5176(1991). RN [9] RP PROTEIN SEQUENCE OF 15-40 AND 50-63. RX PubMed=8110754; DOI=10.1021/bi00171a023; RA Hyatt S.L., Liao L., Chapline C., Jaken S.; RT "Identification and characterization of alpha-protein kinase C binding RT proteins in normal and transformed REF52 cells."; RL Biochemistry 33:1223-1228(1994). RN [10] RP PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307, AND INTERACTION RP WITH HCMV (MICROBIAL INFECTION). RC TISSUE=Umbilical vein endothelial cell; RX PubMed=8117306; DOI=10.1006/bbrc.1994.1140; RA Wright J.F., Kurosky A., Wasi S.; RT "An endothelial cell-surface form of annexin II binds human RT cytomegalovirus."; RL Biochem. Biophys. Res. Commun. 198:983-989(1994). RN [11] RP PROTEIN SEQUENCE OF 234-241 AND 252-261. RX PubMed=8449982; DOI=10.1083/jcb.120.6.1357; RA Emans N., Gorvel J.P., Walter C., Gerke V., Kellner R., Griffiths G., RA Gruenberg J.; RT "Annexin II is a major component of fusogenic endosomal vesicles."; RL J. Cell Biol. 120:1357-1369(1993). RN [12] RP PHOSPHORYLATION AT SER-26. RX PubMed=2946940; DOI=10.1128/mcb.6.7.2738-2744.1986; RA Gould K.L., Woodgett J.R., Isacke C.M., Hunter T.; RT "The protein-tyrosine kinase substrate p36 is also a substrate for protein RT kinase C in vitro and in vivo."; RL Mol. Cell. Biol. 6:2738-2744(1986). RN [13] RP INTERACTION WITH CEACAM1. RX PubMed=14522961; DOI=10.1074/jbc.m309115200; RA Kirshner J., Schumann D., Shively J.E.; RT "CEACAM1, a cell-cell adhesion molecule, directly associates with annexin RT II in a three-dimensional model of mammary morphogenesis."; RL J. Biol. Chem. 278:50338-50345(2003). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [15] RP PHOSPHORYLATION AT TYR-24, AND MUTAGENESIS OF TYR-24. RX PubMed=15302870; DOI=10.1074/jbc.m408078200; RA Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A.; RT "An annexin 2 phosphorylation switch mediates p11-dependent translocation RT of annexin 2 to the cell surface."; RL J. Biol. Chem. 279:43411-43418(2004). RN [16] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [17] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [18] RP FUNCTION, INTERACTION WITH PCSK9, AND MUTAGENESIS OF 77-ARG--LYS-81; RP 80-LYS--ALA-84 AND LYS-88. RX PubMed=18799458; DOI=10.1074/jbc.m805971200; RA Mayer G., Poirier S., Seidah N.G.; RT "Annexin A2 is a C-terminal PCSK9-binding protein that regulates endogenous RT low density lipoprotein receptor levels."; RL J. Biol. Chem. 283:31791-31801(2008). RN [19] 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., Buerckstuemmer T., RA 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 [20] RP INTERACTION WITH COCH. RX PubMed=21886777; DOI=10.1371/journal.pone.0023070; RA Goel M., Sienkiewicz A.E., Picciani R., Lee R.K., Bhattacharya S.K.; RT "Cochlin induced TREK-1 co-expression and annexin A2 secretion: role in RT trabecular meshwork cell elongation and motility."; RL PLoS ONE 6:E23070-E23070(2011). RN [21] RP FUNCTION, VARIANT LEU-98, CHARACTERIZATION OF VARIANT LEU-98, AND RP MUTAGENESIS OF 28-LYS--GLU-36; 37-ARG--LYS-47; 77-ARG--LYS-80 AND RP 77-ARG--LYS-81. RX PubMed=22848640; DOI=10.1371/journal.pone.0041865; RA Seidah N.G., Poirier S., Denis M., Parker R., Miao B., Mapelli C., Prat A., RA Wassef H., Davignon J., Hajjar K.A., Mayer G.; RT "Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL RT receptor degradation."; RL PLoS ONE 7:E41865-E41865(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP FUNCTION, INTERACTION WITH PCSK9, AND RNA-BINDING. RX PubMed=24808179; DOI=10.1074/jbc.m113.541094; RA Ly K., Saavedra Y.G., Canuel M., Routhier S., Desjardins R., Hamelin J., RA Mayne J., Lazure C., Seidah N.G., Day R.; RT "Annexin A2 reduces PCSK9 protein levels via a translational mechanism and RT interacts with the M1 and M2 domains of PCSK9."; RL J. Biol. Chem. 289:17732-17746(2014). RN [24] 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [26] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH M.PNEUMONIAE CARDS RP TOXIN. RX PubMed=25139904; DOI=10.1128/mbio.01497-14; RA Somarajan S.R., Al-Asadi F., Ramasamy K., Pandranki L., Baseman J.B., RA Kannan T.R.; RT "Annexin A2 mediates Mycoplasma pneumoniae community-acquired respiratory RT distress syndrome toxin binding to eukaryotic cells."; RL MBio 5:0-0(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., Ayoub D., RA 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 INTERACTION WITH UBAP2, IDENTIFICATION BY MASS SPECTROMETRY, AND RP INVOLVEMENT IN HEPATOCELLULAR CARCINOMA. RX PubMed=27121050; DOI=10.18632/oncotarget.8783; RA Bai D.S., Wu C., Yang L.X., Zhang C., Zhang P.F., He Y.Z., Cai J.B., RA Song Z.J., Dong Z.R., Huang X.Y., Ke A.W., Shi G.M.; RT "UBAP2 negatively regulates the invasion of hepatocellular carcinoma cell RT by ubiquitinating and degradating Annexin A2."; RL Oncotarget 7:32946-32955(2016). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=8636985; DOI=10.1006/jmbi.1996.0205; RA Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Goettig P., RA Huber R., Gerke V., Tiel C., Roemisch J., Weber K.; RT "The crystal structure and ion channel activity of human annexin II, a RT peripheral membrane protein."; RL J. Mol. Biol. 257:839-847(1996). RN [31] {ECO:0007744|PDB:5LPU, ECO:0007744|PDB:5LPX, ECO:0007744|PDB:5LQ0, ECO:0007744|PDB:5LQ2} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-339, INTERACTION WITH S100A4, RP PHOSPHORYLATION AT TYR-24 AND SER-26, AND MUTAGENESIS OF SER-26. RX PubMed=28669632; DOI=10.1016/j.str.2017.06.001; RA Ecsedi P., Kiss B., Gogl G., Radnai L., Buday L., Koprivanacz K., RA Liliom K., Leveles I., Vertessy B., Jeszenoi N., Hetenyi C., Schlosser G., RA Katona G., Nyitray L.; RT "Regulation of the Equilibrium between Closed and Open Conformations of RT Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding."; RL Structure 25:1195-1207.e5(2017). CC -!- FUNCTION: Calcium-regulated membrane-binding protein whose affinity for CC calcium is greatly enhanced by anionic phospholipids. It binds two CC calcium ions with high affinity. May be involved in heat-stress CC response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces CC PCSK9 protein levels via a translational mechanism but also competes CC with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, CC PubMed:22848640). {ECO:0000269|PubMed:18799458, CC ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}. CC -!- FUNCTION: (Microbial infection) Binds M.pneumoniae CARDS toxin, CC probably serves as one receptor for this pathogen. When ANXA2 is down- CC regulated by siRNA, less toxin binds to human cells and less CC vacuolization (a symptom of M.pneumoniae infection) is seen. CC {ECO:0000269|PubMed:25139904}. CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2 CC heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By CC similarity). Interacts with DYSF (By similarity). Interacts with COCH CC (PubMed:21886777). Interacts (via repeat Annexin 1) with PCSK9 (via the CC C-terminal domain); the interaction inhibits the degradation of LDLR CC (PubMed:18799458). Interacts with CEACAM1 (via the cytoplasmic domain); CC this interaction is regulated by phosphorylation of CEACAM1 CC (PubMed:14522961). Interacts with APPL2 and APPL1; targets APPL2 to CC endosomes and acting in parallel to RAB5A (By similarity). Interacts CC with S100A4 (PubMed:28669632). May interact with UBAP2 CC (PubMed:27121050). {ECO:0000250|UniProtKB:A2SW69, CC ECO:0000250|UniProtKB:P07356, ECO:0000250|UniProtKB:Q6TEQ7, CC ECO:0000269|PubMed:14522961, ECO:0000269|PubMed:18799458, CC ECO:0000269|PubMed:21886777, ECO:0000269|PubMed:27121050}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC (HCMV). {ECO:0000269|PubMed:8117306}. CC -!- SUBUNIT: (Microbial infection) Interacts with M.pneumoniae CARDS toxin; CC CARDS probably uses this protein as a receptor. A portion of CC internalized CARDS remains associated with intracellular annexin 2. CC {ECO:0000269|PubMed:25139904}. CC -!- INTERACTION: CC P07355; P07355: ANXA2; NbExp=5; IntAct=EBI-352622, EBI-352622; CC P07355; P00533: EGFR; NbExp=4; IntAct=EBI-352622, EBI-297353; CC P07355; Q92556: ELMO1; NbExp=3; IntAct=EBI-352622, EBI-346417; CC P07355; Q15811-1: ITSN1; NbExp=2; IntAct=EBI-352622, EBI-8052560; CC P07355; P10636-8: MAPT; NbExp=10; IntAct=EBI-352622, EBI-366233; CC P07355; P40692: MLH1; NbExp=7; IntAct=EBI-352622, EBI-744248; CC P07355; Q15599: NHERF2; NbExp=6; IntAct=EBI-352622, EBI-1149760; CC P07355; P12004: PCNA; NbExp=2; IntAct=EBI-352622, EBI-358311; CC P07355; Q8NBP7: PCSK9; NbExp=7; IntAct=EBI-352622, EBI-7539251; CC P07355; Q9NUX5: POT1; NbExp=2; IntAct=EBI-352622, EBI-752420; CC P07355; P60903: S100A10; NbExp=4; IntAct=EBI-352622, EBI-717048; CC P07355; Q14508: WFDC2; NbExp=36; IntAct=EBI-352622, EBI-723529; CC P07355; P75409: cards; Xeno; NbExp=6; IntAct=EBI-352622, EBI-2259548; CC P07355; P15363: p37; Xeno; NbExp=24; IntAct=EBI-352622, EBI-12740262; CC P07355; B7UM99: tir; Xeno; NbExp=3; IntAct=EBI-352622, EBI-2504426; CC P07355; Q7DB77: tir; Xeno; NbExp=2; IntAct=EBI-352622, EBI-6480811; CC P07355; PRO_0000045602 [Q99IB8]; Xeno; NbExp=5; IntAct=EBI-352622, EBI-6927873; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane {ECO:0000269|PubMed:17081065}. Melanosome CC {ECO:0000269|PubMed:17081065}. Note=In the lamina beneath the plasma CC membrane. Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. Translocated from the cytoplasm to the cell CC surface through a Golgi-independent mechanism. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P07355-1; Sequence=Displayed; CC Name=2; CC IsoId=P07355-2; Sequence=VSP_038091; CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. CC -!- PTM: Phosphorylation of Tyr-24 enhances heat stress-induced CC translocation to the cell surface. {ECO:0000269|PubMed:15302870, CC ECO:0000269|PubMed:2946940}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- DISEASE: Note=Increased expression of ANXA2 is associated with CC hepatocellular carcinoma tumor progression. CC {ECO:0000269|PubMed:27121050}. CC -!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids with CC actin and the cytoskeleton and be involved with exocytosis. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH66955.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86 of CC September 2007; CC URL="https://web.expasy.org/spotlight/back_issues/086"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D00017; BAA00013.1; -; mRNA. DR EMBL; BT007432; AAP36100.1; -; mRNA. DR EMBL; BX640598; CAE45704.1; -; mRNA. DR EMBL; AC087385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001388; AAH01388.1; -; mRNA. DR EMBL; BC009564; AAH09564.1; -; mRNA. DR EMBL; BC015834; AAH15834.1; -; mRNA. DR EMBL; BC016774; AAH16774.1; -; mRNA. DR EMBL; BC021114; AAH21114.1; -; mRNA. DR EMBL; BC023990; AAH23990.1; -; mRNA. DR EMBL; BC052558; AAH52558.1; -; mRNA. DR EMBL; BC052567; AAH52567.1; -; mRNA. DR EMBL; BC066955; AAH66955.2; ALT_INIT; mRNA. DR EMBL; BC068065; AAH68065.1; -; mRNA. DR EMBL; BC093056; AAH93056.1; -; mRNA. DR CCDS; CCDS10175.1; -. [P07355-1] DR CCDS; CCDS32256.1; -. [P07355-2] DR PIR; A23942; LUHU36. DR RefSeq; NP_001002857.1; NM_001002857.1. [P07355-1] DR RefSeq; NP_001002858.1; NM_001002858.2. [P07355-2] DR RefSeq; NP_001129487.1; NM_001136015.2. [P07355-1] DR RefSeq; NP_004030.1; NM_004039.2. [P07355-1] DR RefSeq; XP_016877579.1; XM_017022090.1. DR RefSeq; XP_016877580.1; XM_017022091.1. DR PDB; 1W7B; X-ray; 1.52 A; A=1-339. DR PDB; 1XJL; X-ray; 2.59 A; A/B=21-339. DR PDB; 2HYU; X-ray; 1.86 A; A=32-339. DR PDB; 2HYV; X-ray; 1.42 A; A=32-339. DR PDB; 2HYW; X-ray; 2.10 A; A/B=32-339. DR PDB; 4DRW; X-ray; 3.50 A; A/B/C/D=2-16. DR PDB; 4FTG; X-ray; 2.51 A; C/D=2-16. DR PDB; 4HRH; X-ray; 3.00 A; A/B=2-16. DR PDB; 5LPU; X-ray; 2.10 A; A/B=2-339. DR PDB; 5LPX; X-ray; 1.90 A; A=2-339. DR PDB; 5LQ0; X-ray; 2.90 A; A/B=2-339. DR PDB; 5LQ2; X-ray; 3.40 A; A/B=2-339. DR PDB; 5N7D; X-ray; 2.30 A; A/B=22-339. DR PDB; 5N7F; X-ray; 2.30 A; A/B=22-339. DR PDB; 5N7G; X-ray; 2.95 A; A/B=22-339. DR PDB; 6TWQ; X-ray; 2.65 A; A/B=22-339. DR PDB; 6TWU; X-ray; 2.40 A; A/B=22-339. DR PDB; 6TWX; X-ray; 2.30 A; A/B=22-339. DR PDB; 6TWY; X-ray; 2.30 A; A/B=22-339. DR PDB; 7DTO; X-ray; 2.80 A; A=31-339. DR PDB; 7EQ7; X-ray; 2.11 A; A=1-339. DR PDB; 7NMI; X-ray; 2.10 A; B=29-339. DR PDB; 7P70; X-ray; 2.00 A; A=22-339. DR PDB; 7P71; X-ray; 2.60 A; A/B=22-339. DR PDB; 7P72; X-ray; 2.15 A; A=22-339. DR PDB; 7P73; X-ray; 1.85 A; A=23-339. DR PDB; 7P74; X-ray; 1.90 A; A=22-339. DR PDB; 7PC3; X-ray; 1.95 A; A=29-339. DR PDB; 7PC4; X-ray; 2.30 A; A=22-339. DR PDB; 7PC5; X-ray; 1.70 A; A=22-339. DR PDB; 7PC7; X-ray; 2.10 A; A/B=22-339. DR PDB; 7PC8; X-ray; 2.50 A; A/B=22-339. DR PDB; 7PC9; X-ray; 2.40 A; A/B=29-339. DR PDB; 7PCB; X-ray; 2.00 A; A=29-339. DR PDB; 7QQL; X-ray; 2.44 A; A/B/C=29-339. DR PDB; 7QQM; X-ray; 1.60 A; A=23-339. DR PDB; 7QQN; X-ray; 2.45 A; A/C=22-339. DR PDB; 7ZVN; X-ray; 1.87 A; A=34-339. DR PDB; 7ZVX; X-ray; 2.40 A; A/B=34-339. DR PDB; 8AEL; X-ray; 2.20 A; A=22-339. DR PDBsum; 1W7B; -. DR PDBsum; 1XJL; -. DR PDBsum; 2HYU; -. DR PDBsum; 2HYV; -. DR PDBsum; 2HYW; -. DR PDBsum; 4DRW; -. DR PDBsum; 4FTG; -. DR PDBsum; 4HRH; -. DR PDBsum; 5LPU; -. DR PDBsum; 5LPX; -. DR PDBsum; 5LQ0; -. DR PDBsum; 5LQ2; -. DR PDBsum; 5N7D; -. DR PDBsum; 5N7F; -. DR PDBsum; 5N7G; -. DR PDBsum; 6TWQ; -. DR PDBsum; 6TWU; -. DR PDBsum; 6TWX; -. DR PDBsum; 6TWY; -. DR PDBsum; 7DTO; -. DR PDBsum; 7EQ7; -. DR PDBsum; 7NMI; -. DR PDBsum; 7P70; -. DR PDBsum; 7P71; -. DR PDBsum; 7P72; -. DR PDBsum; 7P73; -. DR PDBsum; 7P74; -. DR PDBsum; 7PC3; -. DR PDBsum; 7PC4; -. DR PDBsum; 7PC5; -. DR PDBsum; 7PC7; -. DR PDBsum; 7PC8; -. DR PDBsum; 7PC9; -. DR PDBsum; 7PCB; -. DR PDBsum; 7QQL; -. DR PDBsum; 7QQM; -. DR PDBsum; 7QQN; -. DR PDBsum; 7ZVN; -. DR PDBsum; 7ZVX; -. DR PDBsum; 8AEL; -. DR AlphaFoldDB; P07355; -. DR SMR; P07355; -. DR BioGRID; 106799; 372. DR ComplexPortal; CPX-130; ANXA2-PCSK9 complex. DR ComplexPortal; CPX-850; AHNAK - Annexin A2 - S100-A10 complex. DR ComplexPortal; CPX-853; Annexin A2 - S100-A10 complex. DR ComplexPortal; CPX-856; SMARCA3 - Annexin A2 - S100-A10 complex. DR CORUM; P07355; -. DR IntAct; P07355; 124. DR MINT; P07355; -. DR STRING; 9606.ENSP00000346032; -. DR ChEMBL; CHEMBL1764938; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB00591; Fluocinolone acetonide. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB00031; Tenecteplase. DR TCDB; 1.A.31.1.4; the annexin (annexin) family. DR GlyCosmos; P07355; 1 site, 2 glycans. DR GlyGen; P07355; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P07355; -. DR MetOSite; P07355; -. DR PhosphoSitePlus; P07355; -. DR SwissPalm; P07355; -. DR BioMuta; ANXA2; -. DR DMDM; 113950; -. DR DOSAC-COBS-2DPAGE; P07355; -. DR REPRODUCTION-2DPAGE; IPI00455315; -. DR REPRODUCTION-2DPAGE; P07355; -. DR CPTAC; CPTAC-462; -. DR EPD; P07355; -. DR jPOST; P07355; -. DR MassIVE; P07355; -. DR MaxQB; P07355; -. DR PaxDb; 9606-ENSP00000346032; -. DR PeptideAtlas; P07355; -. DR PRIDE; P07355; -. DR ProteomicsDB; 51995; -. [P07355-1] DR ProteomicsDB; 51996; -. [P07355-2] DR TopDownProteomics; P07355-1; -. [P07355-1] DR Antibodypedia; 3808; 964 antibodies from 46 providers. DR DNASU; 302; -. DR Ensembl; ENST00000332680.8; ENSP00000346032.3; ENSG00000182718.18. [P07355-2] DR Ensembl; ENST00000396024.7; ENSP00000379342.3; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000421017.6; ENSP00000411352.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000451270.7; ENSP00000387545.3; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000557906.6; ENSP00000452895.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000558558.6; ENSP00000452981.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000559818.6; ENSP00000453859.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000559956.6; ENSP00000453694.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000560468.6; ENSP00000452858.2; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000677968.1; ENSP00000503447.1; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000678061.1; ENSP00000503855.1; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000678450.1; ENSP00000504164.1; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000678870.1; ENSP00000503757.1; ENSG00000182718.18. [P07355-1] DR Ensembl; ENST00000679109.1; ENSP00000504035.1; ENSG00000182718.18. [P07355-1] DR GeneID; 302; -. DR KEGG; hsa:302; -. DR MANE-Select; ENST00000451270.7; ENSP00000387545.3; NM_004039.3; NP_004030.1. DR UCSC; uc002agk.4; human. [P07355-1] DR AGR; HGNC:537; -. DR CTD; 302; -. DR DisGeNET; 302; -. DR GeneCards; ANXA2; -. DR HGNC; HGNC:537; ANXA2. DR HPA; ENSG00000182718; Tissue enhanced (esophagus). DR MIM; 151740; gene. DR neXtProt; NX_P07355; -. DR OpenTargets; ENSG00000182718; -. DR PharmGKB; PA24827; -. DR VEuPathDB; HostDB:ENSG00000182718; -. DR eggNOG; KOG0819; Eukaryota. DR GeneTree; ENSGT00940000154257; -. DR HOGENOM; CLU_025300_0_0_1; -. DR InParanoid; P07355; -. DR OMA; DLMRIRT; -. DR OrthoDB; 1500773at2759; -. DR TreeFam; TF105452; -. DR PathwayCommons; P07355; -. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; P07355; -. DR SIGNOR; P07355; -. DR BioGRID-ORCS; 302; 14 hits in 1160 CRISPR screens. DR ChiTaRS; ANXA2; human. DR EvolutionaryTrace; P07355; -. DR GeneWiki; Annexin_A2; -. DR GenomeRNAi; 302; -. DR Pharos; P07355; Tbio. DR PRO; PR:P07355; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P07355; Protein. DR Bgee; ENSG00000182718; Expressed in bronchial epithelial cell and 205 other cell types or tissues. DR ExpressionAtlas; P07355; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:1990665; C:AnxA2-p11 complex; IDA:UniProtKB. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:1990667; C:PCSK9-AnxA2 complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; EXP:ComplexPortal. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL. DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:UniProtKB. DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL. DR GO; GO:0046790; F:virion binding; IBA:GO_Central. DR GO; GO:0001525; P:angiogenesis; IEP:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl. DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl. DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0001765; P:membrane raft assembly; IMP:UniProtKB. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:ComplexPortal. DR GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:BHF-UCL. DR GO; GO:0002091; P:negative regulation of receptor internalization; IDA:ComplexPortal. DR GO; GO:0036035; P:osteoclast development; IDA:UniProtKB. DR GO; GO:0045921; P:positive regulation of exocytosis; NAS:ComplexPortal. DR GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IDA:BHF-UCL. DR GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IDA:BHF-UCL. DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL. DR GO; GO:1905686; P:positive regulation of plasma membrane repair; NAS:ComplexPortal. DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:ComplexPortal. DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:BHF-UCL. DR GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:ComplexPortal. DR GO; GO:0044090; P:positive regulation of vacuole organization; IMP:AgBase. DR GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB. DR GO; GO:0050767; P:regulation of neurogenesis; ISO:ComplexPortal. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0006900; P:vesicle budding from membrane; IMP:UniProtKB. DR DisProt; DP02735; -. DR Gene3D; 1.10.220.10; Annexin; 4. DR IDEAL; IID00700; -. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR002389; ANX2. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF18; ANNEXIN A2-RELATED; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00198; ANNEXINII. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 4. DR PROSITE; PS51897; ANNEXIN_2; 4. DR UCD-2DPAGE; P07355; -. DR Genevisible; P07355; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Annexin; KW Basement membrane; Calcium; Calcium/phospholipid-binding; KW Direct protein sequencing; Extracellular matrix; Host-virus interaction; KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; RNA-binding; KW Secreted; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..339 FT /note="Annexin A2" FT /id="PRO_0000067470" FT REPEAT 33..104 FT /note="Annexin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 105..176 FT /note="Annexin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 189..261 FT /note="Annexin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 265..336 FT /note="Annexin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REGION 2..24 FT /note="S100A10-binding site" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 24 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000269|PubMed:15302870, FT ECO:0000269|PubMed:28669632" FT MOD_RES 26 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:28669632, FT ECO:0000269|PubMed:2946940" FT MOD_RES 49 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 152 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 199 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 227 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MGRQLAGCGDAGKKASFKM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038091" FT VARIANT 98 FT /note="V -> L (does not affect interaction with PCSK9; FT dbSNP:rs17845226)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:22848640" FT /id="VAR_012982" FT MUTAGEN 24 FT /note="Y->A: Abolishes heat stress-induced cell surface FT localization." FT /evidence="ECO:0000269|PubMed:15302870" FT MUTAGEN 26 FT /note="S->E: Stronger interaction with S100A4." FT /evidence="ECO:0000269|PubMed:28669632" FT MUTAGEN 28..36 FT /note="KAYTNFDAE->SAYTNFNAS: No effect on interaction with FT PCSK9." FT /evidence="ECO:0000269|PubMed:22848640" FT MUTAGEN 37..47 FT /note="RDALNIETAIK->SDALNIHTAIM: Slightly decreases FT interaction with PCSK9." FT /evidence="ECO:0000269|PubMed:22848640" FT MUTAGEN 77..81 FT /note="RRTKK->AATAA: Strongly decreases interaction with FT PCSK9." FT /evidence="ECO:0000269|PubMed:18799458, FT ECO:0000269|PubMed:22848640" FT MUTAGEN 77..80 FT /note="RRTK->AATA: Decreases interaction with PCSK9. FT Strongly decreases interaction with PCSK9; when associated FT with K-88." FT /evidence="ECO:0000269|PubMed:18799458" FT MUTAGEN 80..84 FT /note="KKELA->GKPLD: No effect on interaction with PCSK9." FT /evidence="ECO:0000269|PubMed:18799458" FT MUTAGEN 88 FT /note="K->A: Strongly decreases interaction with PCSK9; FT when associated with 77-A--A-80." FT /evidence="ECO:0000269|PubMed:18799458" FT CONFLICT 29 FT /note="A -> P (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="D -> G (in Ref. 4; CAE45704)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="V -> A (in Ref. 6; AAH23990)" FT /evidence="ECO:0000305" FT HELIX 4..12 FT /evidence="ECO:0007829|PDB:5LPU" FT TURN 24..27 FT /evidence="ECO:0007829|PDB:7QQM" FT HELIX 35..47 FT /evidence="ECO:0007829|PDB:2HYV" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:5N7D" FT HELIX 53..60 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 65..79 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 83..90 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 106..117 FT /evidence="ECO:0007829|PDB:2HYV" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:1W7B" FT HELIX 125..134 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 137..151 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 155..161 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 165..175 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 188..200 FT /evidence="ECO:0007829|PDB:2HYV" FT TURN 201..204 FT /evidence="ECO:0007829|PDB:2HYV" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 210..219 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:2HYV" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:2HYV" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:7DTO" FT HELIX 240..247 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 250..264 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 266..278 FT /evidence="ECO:0007829|PDB:2HYV" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 285..295 FT /evidence="ECO:0007829|PDB:2HYV" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 300..311 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 315..322 FT /evidence="ECO:0007829|PDB:2HYV" FT HELIX 325..335 FT /evidence="ECO:0007829|PDB:2HYV" SQ SEQUENCE 339 AA; 38604 MW; 5126E1337A0CBEA1 CRC64; MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD //