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   01-OCT-2000 (Rel. 40, Last annotation update)
DE   ANNEXIN I (LIPOCORTIN I) (CALPACTIN II) (CHROMOBINDIN 9) (P35)
DE   (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, 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   [5]
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   [6]
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   [7]
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   [8]
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: IN PLACENTA 20% OF THE PROTEIN IS FOUND AS A COVALENTLY
CC       CROSS-LINKED DIMER WHICH IS GENERATED BY A TRANSGLUTAMINASE.
CC   -!- DOMAIN: CONTAINS FOUR HOMOLOGOUS REPEATS WITH A CONSENSUS
CC       SEQUENCE COMMON TO ALL ANNEXIN PROTEINS. A PAIR OF THESE REPEATS
CC       MAY FORM ONE BINDING SITE FOR 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.
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DR   EMBL; X05908; CAA29338.1; -.
DR   PIR; A03080; LUHU.
DR   PIR; S28846; S28846.
DR   PDB; 1AIN; 15-JUL-93.
DR   PDB; 1BO9; 19-AUG-98.
DR   MIM; 151690; -.
DR   InterPro; IPR001464; Annexin.
DR   Pfam; PF00191; annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00197; ANNEXINI.
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   MOD_RES       1      1       ACETYLATION.
FT   MOD_RES      18     18       INTERCHAIN CROSS-LINK.
FT   MOD_RES      20     20       PHOSPHORYLATION (BY EGFR).
FT   MOD_RES      23     23       PHOSPHORYLATION.
FT   MOD_RES      26     26       PHOSPHORYLATION (BY PKC) (BY SIMILARITY).
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
//