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-1994 (REL. 30, LAST ANNOTATION UPDATE)
DE   ANNEXIN I (LIPOCORTIN I) (CALPACTIN II) (CHROMOBINDIN 9) (P35)
DE   (PHOSPHOLIPASE A2 INHIBITORY PROTEIN).
GN   ANX1 OR LPC1.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86146879.
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.;
RL   NATURE 320:77-81(1986).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91369906.
RA   KOVACIC R.T., TIZARD R., CATE R.L., FREY A.Z., WALLNER B.P.;
RL   BIOCHEMISTRY 30:9015-9021(1991).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 93145967.
RA   ARCONE R., ARPAIA G., RUOPPOLO M., MALORNI A., PUCCI P., MARINO G.,
RA   IALENTI A., DI ROSA M., CILIBERTO G.;
RL   EUR. J. BIOCHEM. 211:347-355(1993).
RN   [4]
RP   SEQUENCE, AND PHOSPHORYLATION SITES.
RX   MEDLINE; 88309771.
RA   VARTICOVSKI L., CHAHWALA S.B., WHITMAN M., CANTLEY L., SCHINDLER D.,
RA   CHOW E.P., SINCLAIR L.K., PEPINSKY R.B.;
RL   BIOCHEMISTRY 27:3682-3690(1988).
RN   [5]
RP   DIMERIC FORM.
RX   MEDLINE; 90104259.
RA   PEPINSKY R.B., SINCLAIR L.K., CHOW E.P., O'BRINE-GRECO B.;
RL   BIOCHEM. J. 263:97-103(1989).
RN   [6]
RP   ACETYLATION.
RX   MEDLINE; 87292145.
RA   BIEMANN K., SCOBLE H.A.;
RL   SCIENCE 237:992-998(1987).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE; 93200922.
RA   WENG X., LUECKE H., SONG I.S., KANG D.S., KIM S.-H., HUBER R.;
RL   PROTEIN SCI. 2:448-458(1993).
CC   -!- FUNCTION: THIS PROTEIN REGULATES PHOSPHOLIPASE A2 ACTIVITY. IT
CC       SEEMS TO BIND FROM TWO TO FOUR CALCIUM IONS WITH HIGH AFFINITY.
CC   -!- PTM: PHOSPHORYLATION OF ANNEXIN 1 RESULTS IN LOSS OF ITS
CC       INHIBITORY ACTIVITY.
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   -!- SIMILARITY: TO OTHER PROTEINS OF THE ANNEXIN FAMILY.
CC   -!- SUBUNIT: IN PLACENTA 20% OF THE PROTEIN IS FOUND AS A COVALENTLY
CC       CROSS-LINKED DIMER WHICH IS GENERATED BY A TRANSGLUTAMINASE.
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DR   EMBL; X05908; G34388; -.
DR   PIR; A03080; LUHU.
DR   PIR; S28846; S28846.
DR   PDB; 1AIN; 15-JUL-93.
DR   MIM; 151690; 11TH EDITION.
DR   PROSITE; PS00223; ANNEXIN.
KW   ANNEXIN; CALCIUM/PHOSPHOLIPID-BINDING; REPEAT; 3D-STRUCTURE;
KW   PHOSPHOLIPASE A2 INHIBITOR; PHOSPHORYLATION; ACETYLATION.
FT   INIT_MET      0      0
FT   MOD_RES       1      1       ACETYLATION.
FT   MOD_RES      18     18       INTERCHAIN CROSS-LINK.
FT   REPEAT       50    110       ANNEXIN.
FT   REPEAT      122    182       ANNEXIN.
FT   REPEAT      206    266       ANNEXIN.
FT   REPEAT      281    341       ANNEXIN.
FT   MOD_RES      20     20       PHOSPHORYLATION (BY TYR-KINASES).
FT   MOD_RES      23     23       PHOSPHORYLATION.
SQ   SEQUENCE   345 AA;  38583 MW;  0DA6DC18 CRC32;
     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
//