ID Q6P452_HUMAN Unreviewed; 299 AA. AC Q6P452; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540}; GN Name=ANXA4 {ECO:0000313|EMBL:AAH63672.1, GN ECO:0000313|Ensembl:ENSP00000386756.1}; 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 {ECO:0000313|EMBL:AAH63672.1}; RN [1] {ECO:0000313|EMBL:AAH63672.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus {ECO:0000313|EMBL:AAH63672.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [2] {ECO:0000313|Ensembl:ENSP00000386756.1, ECO:0000313|Proteomes:UP000005640} 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 [4] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [5] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [6] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0000313|Ensembl:ENSP00000386756.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an CC indirect inhibitor of the thromboplastin-specific complex, which is CC involved in the blood coagulation cascade. CC {ECO:0000256|ARBA:ARBA00002758}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. {ECO:0000256|RuleBase:RU003540}. CC -!- SIMILARITY: Belongs to the annexin family. CC {ECO:0000256|ARBA:ARBA00007831, ECO:0000256|RuleBase:RU003540}. 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; AC019206; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092431; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063672; AAH63672.1; -; mRNA. DR RefSeq; NP_001144.1; NM_001153.4. DR RefSeq; NP_001307629.1; NM_001320700.1. DR RefSeq; NP_001307631.1; NM_001320702.1. DR IntAct; Q6P452; 1. DR ProteomicsDB; 66944; -. DR Antibodypedia; 1552; 578 antibodies from 42 providers. DR DNASU; 307; -. DR Ensembl; ENST00000409920.5; ENSP00000386756.1; ENSG00000196975.16. DR GeneID; 307; -. DR KEGG; hsa:307; -. DR UCSC; uc002sfs.5; human. DR CTD; 307; -. DR HGNC; HGNC:542; ANXA4. DR VEuPathDB; HostDB:ENSG00000196975; -. DR GeneTree; ENSGT00940000156575; -. DR HOGENOM; CLU_025300_0_0_1; -. DR OrthoDB; 1500773at2759; -. DR BioGRID-ORCS; 307; 4 hits in 1156 CRISPR screens. DR ChiTaRS; ANXA4; human. DR GenomeRNAi; 307; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000196975; Expressed in pancreatic ductal cell and 207 other cell types or tissues. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW. DR GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro. DR Gene3D; 1.10.220.10; Annexin; 4. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR002392; ANX5. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF28; ANNEXIN A4; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00201; ANNEXINV. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 2. DR PROSITE; PS51897; ANNEXIN_2; 3. PE 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Annexin {ECO:0000256|ARBA:ARBA00023216, ECO:0000256|RuleBase:RU003540}; KW Calcium {ECO:0000256|RuleBase:RU003540}; KW Calcium/phospholipid-binding {ECO:0000256|RuleBase:RU003540}; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Proteomics identification {ECO:0007829|EPD:Q6P452, KW ECO:0007829|MaxQB:Q6P452}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU003540}. SQ SEQUENCE 299 AA; 33552 MW; CB81FAA4E951DA56 CRC64; MAMATKGGTV KAASGFNAME DAQTLRKAMK GLGTDEDAII SVLAYRNTAQ RQEIRTAYKS TIGRDLIDDL KSELSGNFEQ GAGTDEGCLI EILASRTPEE IRRISQTYQQ QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DEGNYLDDAL VRQDAQDLYE AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV KCMRNKSAYF AEKLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRAHFKRL YGKSLYSFIK GDTSGDYRKV LLVLCGGDD //