ID   ANXA1_HUMAN    STANDARD;      PRT;   345 AA.
AC   P04083;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-OCT-2006, entry version 94.
DE   Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin-9)
DE   (p35) (Phospholipase A2 inhibitory protein).
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   MEDLINE=86146879; 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.
RX   MEDLINE=91369906; 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.
RX   MEDLINE=93145967; PubMed=8425544;
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-20 AND SER-26.
RX   MEDLINE=88309771; 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   DIMERIZATION.
RX   MEDLINE=90104259; 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   [7]
RP   ACETYLATION.
RX   MEDLINE=87292145; PubMed=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   [8]
RP   PHOSPHORYLATION AT SER-4 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=93200922; PubMed=8453382;
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   [11]
RP   STRUCTURE BY NMR OF 40-112.
RX   MEDLINE=99115644; 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.
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.
CC   -!- SIMILARITY: Belongs to the annexin family.
CC   -!- SIMILARITY: Contains 4 annexin repeats.
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DR   EMBL; X05908; CAA29338.1; -; Other_RNA.
DR   EMBL; BC001275; AAH01275.1; -; mRNA.
DR   EMBL; BC035993; AAH35993.1; -; mRNA.
DR   PIR; A03080; LUHU.
DR   UniGene; Hs.494173; -.
DR   PDB; 1AIN; X-ray; @=32-345.
DR   PDB; 1BO9; NMR; A=40-112.
DR   PDB; 1QLS; X-ray; D=1-11.
DR   SMR; P04083; 1-343.
DR   PHCI-2DPAGE; P04083; -.
DR   Ensembl; ENSG00000135046; Homo sapiens.
DR   KEGG; hsa:301; -.
DR   H-InvDB; HIX0008100; -.
DR   HGNC; HGNC:533; ANXA1.
DR   MIM; 151690; gene.
DR   LinkHub; P04083; -.
DR   ArrayExpress; P04083; -.
DR   RZPD-ProtExp; C0232; -.
DR   RZPD-ProtExp; IOH3222; -.
DR   RZPD-ProtExp; RZPDo834D053; -.
DR   RZPD-ProtExp; RZPDo839A0648; -.
DR   GO; GO:0001533; C:cornified envelope; IDA.
DR   GO; GO:0005737; C:cytoplasm; TAS.
DR   GO; GO:0005509; F:calcium ion binding; TAS.
DR   GO; GO:0004859; F:phospholipase inhibitor activity; TAS.
DR   GO; GO:0005543; F:phospholipid binding; TAS.
DR   GO; GO:0030674; F:protein binding, bridging; IDA.
DR   GO; GO:0005102; F:receptor binding; TAS.
DR   GO; GO:0005198; F:structural molecule activity; IDA.
DR   GO; GO:0006916; P:anti-apoptosis; TAS.
DR   GO; GO:0006928; P:cell motility; TAS.
DR   GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS.
DR   GO; GO:0006954; P:inflammatory response; TAS.
DR   GO; GO:0030216; P:keratinocyte differentiation; IDA.
DR   GO; GO:0006629; P:lipid metabolism; TAS.
DR   GO; GO:0018149; P:peptide cross-linking; IDA.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR002388; AnnexinI.
DR   PANTHER; PTHR10502; Annexin; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00197; ANNEXINI.
DR   ProDom; PD000143; Annexin; 4.
DR   SMART; SM00335; ANX; 4.
DR   PROSITE; PS00223; ANNEXIN; 4.
KW   3D-structure; Acetylation; Annexin; Calcium;
KW   Calcium/phospholipid-binding; Direct protein sequencing;
KW   Phospholipase A2 inhibitor; Phosphorylation; Repeat.
FT   INIT_MET      0      0
FT   CHAIN         1    345       Annexin A1.
FT                                /FTId=PRO_0000067460.
FT   REPEAT       50    110       Annexin 1.
FT   REPEAT      122    182       Annexin 2.
FT   REPEAT      206    266       Annexin 3.
FT   REPEAT      281    341       Annexin 4.
FT   MOD_RES       1      1       N-acetylalanine.
FT   MOD_RES       4      4       Phosphoserine (by TRPM7).
FT   MOD_RES      20     20       Phosphotyrosine (by EGFR).
FT   MOD_RES      23     23       Phosphothreonine.
FT   MOD_RES      26     26       Phosphoserine (by PKC).
FT   MOD_RES     206    206       Phosphotyrosine.
FT   CROSSLNK     18     18       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT   HELIX         2      9
SQ   SEQUENCE   345 AA;  38583 MW;  90A245C9E69F5011 CRC64;
     AMVSEFLKQA WFIENEEQEY VQTVKSSKGG PGSAVSPYPT FNPSSDVAAL HKAIMVKGVD
     EATIIDILTK RNNAQRQQIK AAYLQETGKP LDETLKKALT GHLEEVVLAL LKTPAQFDAD
     ELRAAMKGLG TDEDTLIEIL ASRTNKEIRD INRVYREELK RDLAKDITSD TSGDFRNALL
     SLAKGDRSED FGVNEDLADS DARALYEAGE RRKGTDVNVF NTILTTRSYP QLRRVFQKYT
     KYSKHDMNKV LDLELKGDIE KCLTAIVKCA TSKPAFFAEK LHQAMKGVGT RHKALIRIMV
     SRSEIDMNDI KAFYQKMYGI SLCQAILDET KGDYEKILVA LCGGN
//