ID   ANX1_HUMAN     STANDARD;      PRT;   345 AA.
AC   P04083;
DT   01-NOV-1986 (Rel. 03, Created)
DT   01-NOV-1986 (Rel. 03, Last sequence update)
DT   15-SEP-2003 (Rel. 42, Last annotation update)
DE   Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9)
DE   (P35) (Phospholipase A2 inhibitory protein).
GN   ANXA1 OR ANX1 OR LPC1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=86146879; PubMed=2936963;
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   SEQUENCE FROM N.A.
RX   MEDLINE=91369906; PubMed=1832554;
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
RT   lipocortin I.";
RL   Biochemistry 30:9015-9021(1991).
RN   [3]
RP   SEQUENCE FROM N.A.
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
RT   lipocortin 1 expressed in Escherichia coli.";
RL   Eur. J. Biochem. 211:347-355(1993).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Cervix;
RX   MEDLINE=22388257; PubMed=12477932;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length
RT   human and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [5]
RP   PARTIAL SEQUENCE, AND PHOSPHORYLATION SITES.
RX   MEDLINE=88309771; PubMed=2457390;
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   DIMERIC FORM.
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   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   [9]
RP   STRUCTURE BY NMR OF 40-112.
RX   MEDLINE=99115644; PubMed=9915835;
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 AND EPIDERMAL GROWTH
CC       FACTOR RECEPTOR/KINASE. PHOSPHORYLATION RESULTS IN LOSS OF THE
CC       INHIBITORY ACTIVITY.
CC   -!- SIMILARITY: Belongs to the annexin family.
CC   -!- SIMILARITY: Contains 4 annexin repeats.
CC   -!- DATABASE: NAME=Annexin I home page;
CC       WWW="http://www.mds.qmw.ac.uk/biopharm/annI.html".
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DR   EMBL; X05908; CAA29338.1; -.
DR   EMBL; BC001275; AAH01275.1; -.
DR   PIR; A03080; LUHU.
DR   PDB; 1AIN; 15-JUL-93.
DR   PDB; 1BO9; 19-AUG-98.
DR   PDB; 1QLS; 25-FEB-00.
DR   PHCI-2DPAGE; P04083; -.
DR   Genew; HGNC:533; ANXA1.
DR   MIM; 151690; -.
DR   GO; GO:0005509; F:calcium ion binding activity; TAS.
DR   GO; GO:0005102; F:receptor binding activity; 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:0006629; P:lipid metabolism; TAS.
DR   InterPro; IPR001464; Annexin.
DR   Pfam; PF00191; annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   ProDom; PD000143; Annexin; 4.
DR   SMART; SM00335; ANX; 4.
DR   PROSITE; PS00223; ANNEXIN; 4.
KW   Annexin; Calcium/phospholipid-binding; Repeat; 3D-structure;
KW   Phospholipase A2 inhibitor; Phosphorylation; Acetylation.
FT   INIT_MET      0      0
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   CROSSLNK     18     18       Isoglutamyl lysine isopeptide (Gln)
FT                                (Interchain to Lys).
FT   MOD_RES       1      1       ACETYLATION.
FT   MOD_RES      20     20       PHOSPHORYLATION (BY EGFR).
FT   MOD_RES      23     23       PHOSPHORYLATION.
FT   MOD_RES      26     26       PHOSPHORYLATION (BY PKC) (BY SIMILARITY).
FT   TURN         43     44
FT   HELIX        45     54
FT   TURN         55     56
FT   HELIX        64     70
FT   TURN         74     75
FT   HELIX        76     86
FT   TURN         87     87
FT   HELIX        93     98
FT   TURN        101    102
FT   TURN        104    104
FT   HELIX       105    108
FT   HELIX       109    111
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
//