ID ANXA1_HUMAN Reviewed; 346 AA. AC P04083; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-SEP-2015, entry version 200. DE RecName: Full=Annexin A1; DE AltName: Full=Annexin I; DE AltName: Full=Annexin-1; DE AltName: Full=Calpactin II; DE AltName: Full=Calpactin-2; DE AltName: Full=Chromobindin-9; DE AltName: Full=Lipocortin I; DE AltName: Full=Phospholipase A2 inhibitory protein; DE AltName: Full=p35; GN Name=ANXA1; Synonyms=ANX1, LPC1; 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=2936963; DOI=10.1038/320077a0; RA Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R., RA Sinclair L.K., Foeller C., Chow E.P., Browning J.L., RA Ramachandran K.L., Pepinsky R.B.; RT "Cloning and expression of human lipocortin, a phospholipase A2 RT inhibitor with potential anti-inflammatory activity."; RL Nature 320:77-81(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1832554; DOI=10.1021/bi00101a015; RA Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.; RT "Correlation of gene and protein structure of rat and human lipocortin RT I."; RL Biochemistry 30:9015-9021(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8425544; DOI=10.1111/j.1432-1033.1993.tb19904.x; RA Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G., RA Ialenti A., di Rosa M., Ciliberto G.; RT "Structural characterization of a biologically active human lipocortin RT 1 expressed in Escherichia coli."; RL Eur. J. Biochem. 211:347-355(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix, and Lung; 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 [5] RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT TYR-21 BY EGFR AND RP SER-27 BY PKC. RX PubMed=2457390; DOI=10.1021/bi00410a024; RA Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D., RA Chow E.P., Sinclair L.K., Pepinsky R.B.; RT "Location of sites in human lipocortin I that are phosphorylated by RT protein tyrosine kinases and protein kinases A and C."; RL Biochemistry 27:3682-3690(1988). RN [6] RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=3303336; DOI=10.1126/science.3303336; RA Biemann K., Scoble H.A.; RT "Characterization by tandem mass spectrometry of structural RT modifications in proteins."; RL Science 237:992-998(1987). RN [7] RP DIMERIZATION. RX PubMed=2532504; RA Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B.; RT "A dimeric form of lipocortin-1 in human placenta."; RL Biochem. J. 263:97-103(1989). RN [8] RP PHOSPHORYLATION AT SER-5 BY TRPM7. RX PubMed=15485879; DOI=10.1074/jbc.C400441200; RA Dorovkov M.V., Ryazanov A.G.; RT "Phosphorylation of annexin I by TRPM7 channel-kinase."; RL J. Biol. Chem. 279:50643-50646(2004). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-312, AND 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., 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION RP 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 [14] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8453382; DOI=10.1002/pro.5560020317; RA Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R.; RT "Crystal structure of human annexin I at 2.5-A resolution."; RL Protein Sci. 2:448-458(1993). RN [15] RP STRUCTURE BY NMR OF 41-113. RX PubMed=9915835; DOI=10.1074/jbc.274.5.2971; RA Gao J., Li Y., Yan H.; RT "NMR solution structure of domain 1 of human annexin I shows an RT autonomous folding unit."; RL J. Biol. Chem. 274:2971-2977(1999). CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes CC membrane fusion and is involved in exocytosis. This protein CC regulates phospholipase A2 activity. It seems to bind from two to CC four calcium ions with high affinity. CC -!- SUBUNIT: Homodimer in placenta (20%); linked by CC transglutamylation. Interacts with DYSF (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-354007, EBI-81279; CC Q13546:RIPK1; NbExp=5; IntAct=EBI-354007, EBI-358507; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm CC {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Basolateral CC cell membrane {ECO:0000250}. Note=Found in the cilium, nucleus and CC basolateral cell membrane of ciliated cells in the tracheal CC endothelium. Found in the cytoplasm of type II pneumocytes and CC alveolar macrophages. {ECO:0000250}. CC -!- DOMAIN: A pair of annexin repeats may form one binding site for CC calcium and phospholipid. CC -!- PTM: Phosphorylated by protein kinase C, epidermal growth factor CC receptor/kinase and TRPM7. Phosphorylation results in loss of the CC inhibitory activity. {ECO:0000269|PubMed:15485879, CC ECO:0000269|PubMed:2457390}. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 4 annexin repeats. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ANXA1ID653ch9q21.html"; 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; X05908; CAA29338.1; -; mRNA. DR EMBL; BC001275; AAH01275.1; -; mRNA. DR EMBL; BC035993; AAH35993.1; -; mRNA. DR CCDS; CCDS6645.1; -. DR PIR; A03080; LUHU. DR RefSeq; NP_000691.1; NM_000700.2. DR RefSeq; XP_011516911.1; XM_011518609.1. DR UniGene; Hs.494173; -. DR PDB; 1AIN; X-ray; 2.50 A; A=33-346. DR PDB; 1BO9; NMR; -; A=41-113. DR PDB; 1QLS; X-ray; 2.30 A; D=2-12. DR PDBsum; 1AIN; -. DR PDBsum; 1BO9; -. DR PDBsum; 1QLS; -. DR ProteinModelPortal; P04083; -. DR SMR; P04083; 2-344. DR BioGrid; 106798; 61. DR DIP; DIP-32875N; -. DR IntAct; P04083; 60. DR MINT; MINT-1212274; -. DR STRING; 9606.ENSP00000257497; -. DR DrugBank; DB00288; Amcinonide. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB00741; Hydrocortisone. DR TCDB; 1.A.31.1.3; the annexin (annexin) family. DR PhosphoSite; P04083; -. DR BioMuta; ANXA1; -. DR DMDM; 113944; -. DR DOSAC-COBS-2DPAGE; P04083; -. DR REPRODUCTION-2DPAGE; IPI00218918; -. DR REPRODUCTION-2DPAGE; P04083; -. DR UCD-2DPAGE; P04083; -. DR MaxQB; P04083; -. DR PaxDb; P04083; -. DR PeptideAtlas; P04083; -. DR PRIDE; P04083; -. DR DNASU; 301; -. DR Ensembl; ENST00000257497; ENSP00000257497; ENSG00000135046. DR Ensembl; ENST00000376911; ENSP00000366109; ENSG00000135046. DR GeneID; 301; -. DR KEGG; hsa:301; -. DR UCSC; uc004ajf.1; human. DR CTD; 301; -. DR GeneCards; GC09P073151; -. DR HGNC; HGNC:533; ANXA1. DR HPA; CAB013023; -. DR HPA; CAB035987; -. DR HPA; CAB058693; -. DR HPA; HPA011271; -. DR HPA; HPA011272; -. DR MIM; 151690; gene. DR neXtProt; NX_P04083; -. DR PharmGKB; PA24823; -. DR eggNOG; NOG282829; -. DR HOGENOM; HOG000158803; -. DR HOVERGEN; HBG061815; -. DR InParanoid; P04083; -. DR KO; K17091; -. DR OMA; IMVSRHE; -. DR OrthoDB; EOG74XS72; -. DR PhylomeDB; P04083; -. DR TreeFam; TF105452; -. DR Reactome; R-HSA-397014; Muscle contraction. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands. DR SignaLink; P04083; -. DR ChiTaRS; ANXA1; human. DR EvolutionaryTrace; P04083; -. DR GeneWiki; Annexin_A1; -. DR GenomeRNAi; 301; -. DR NextBio; 1213; -. DR PRO; PR:P04083; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; P04083; -. DR CleanEx; HS_ANXA1; -. DR ExpressionAtlas; P04083; baseline and differential. DR Genevisible; P04083; HS. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell. DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0042629; C:mast cell granule; IEA:Ensembl. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0043234; C:protein complex; IEA:Ensembl. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0036310; F:annealing helicase activity; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase. DR GO; GO:0033676; F:double-stranded DNA-dependent ATPase activity; IEA:Ensembl. DR GO; GO:0004386; F:helicase activity; IEA:Ensembl. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc. DR GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB. DR GO; GO:0005102; F:receptor binding; TAS:ProtInc. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl. DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl. DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB. DR GO; GO:0046632; P:alpha-beta T cell differentiation; ISS:BHF-UCL. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:BHF-UCL. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0032508; P:DNA duplex unwinding; IEA:Ensembl. DR GO; GO:0036292; P:DNA rewinding; IEA:Ensembl. DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0042063; P:gliogenesis; IEA:Ensembl. DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB. DR GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc. DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IMP:BHF-UCL. DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IEA:Ensembl. DR GO; GO:0097350; P:neutrophil clearance; IMP:BHF-UCL. DR GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL. DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl. DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl. DR GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB. DR GO; GO:0070459; P:prolactin secretion; IEA:Ensembl. DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl. DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB. DR Gene3D; 1.10.220.10; -; 4. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR002388; AnnexinI. DR PANTHER; PTHR10502:SF17; PTHR10502:SF17; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00197; ANNEXINI. DR SMART; SM00335; ANX; 4. DR PROSITE; PS00223; ANNEXIN; 4. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Annexin; Calcium; KW Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Membrane; Nucleus; Phospholipase A2 inhibitor; KW Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3303336}. FT CHAIN 2 346 Annexin A1. FT /FTId=PRO_0000067460. FT REPEAT 51 111 Annexin 1. FT REPEAT 123 183 Annexin 2. FT REPEAT 207 267 Annexin 3. FT REPEAT 282 342 Annexin 4. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000269|PubMed:3303336}. FT MOD_RES 5 5 Phosphoserine; by TRPM7. FT {ECO:0000269|PubMed:15485879}. FT MOD_RES 21 21 Phosphotyrosine; by EGFR. FT {ECO:0000269|PubMed:2457390}. FT MOD_RES 27 27 Phosphoserine; by PKC. FT {ECO:0000269|PubMed:2457390}. FT MOD_RES 34 34 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 37 37 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 58 58 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P10107}. FT MOD_RES 239 239 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 312 312 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT CROSSLNK 19 19 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-?). FT HELIX 3 10 {ECO:0000244|PDB:1QLS}. FT HELIX 46 55 {ECO:0000244|PDB:1BO9}. FT STRAND 62 64 {ECO:0000244|PDB:1BO9}. FT HELIX 65 71 {ECO:0000244|PDB:1BO9}. FT HELIX 77 87 {ECO:0000244|PDB:1BO9}. FT HELIX 94 99 {ECO:0000244|PDB:1BO9}. FT HELIX 106 109 {ECO:0000244|PDB:1BO9}. FT HELIX 110 112 {ECO:0000244|PDB:1BO9}. SQ SEQUENCE 346 AA; 38714 MW; 14B42E1FA4178EC0 CRC64; MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN //