ID   CL2$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-JAN-1990  (REL. 13, LAST ANNOTATION UPDATE)
DE   CALPACTIN II (LIPOCORTIN I) (PHOSPHOLIPASE A2 INHIBITORY PROTEIN)
DE   (P35).
OS   HUMAN (HOMO SAPIENS).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1] (SEQUENCE FROM N.A.)
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] (DIMERIC FORM)
RA   PEPINSKY R.B., SINCLAIR L.K., CHOW E.P., O'BRINE-GRECO B.;
RL   BIOCHEM. J. 263:97-103(1989).
CC   -!- FUNCTION: LIPOCORTIN IS A STEROID-INDUCIBLE PROTEIN THAT REGULATES
CC       PHOSPHOLIPASE A2 ACTIVITY. UNPHOSPHORYLATED IT IS A POTENT
CC       INHIBITOR OF THE ENZYME, MIMICKING THE AMELIORATING EFFECTS
CC       GLUCOCORTICOIDS HAVE ON THE INFLAMMATORY RESPONSE BY BLOCKING
CC       THE HYDROLYSIS OF MEMBRANE PHOSPHOLIPIDS. PHOSPHORYLATION OF
CC       LIPOCORTIN RESULTS IN LOSS OF ITS INHIBITORY ACTIVITY.
CC   -!- P35 SEEMS TO BIND FROM TWO TO FOUR CALCIUM IONS WITH HIGH
CC       AFFINITY.
CC   -!- THIS PROTEIN 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   PIR; A03080; LUHU.
DR   EMBL; X05908; HSLIPCR.
DR   PROSITE; PS00223; ANNEXIN.
KW   ANNEXIN; CALCIUM/PHOSPHOLIPID-BINDING; DUPLICATION; REPEAT;
KW   PHOSPHOLIPASE A2 INHIBITOR; PHOSPHORYLATION.
FT   INIT_MET      0      0
FT   MOD_RES      18     18       INTERCHAIN CROSS-LINK.
FT   DOMAIN       50    110       ANNEXIN-REPEAT.
FT   DOMAIN      122    182       ANNEXIN-REPEAT.
FT   DOMAIN      206    266       ANNEXIN-REPEAT.
FT   DOMAIN      281    341       ANNEXIN-REPEAT.
FT   MOD_RES      20     20       PHOSPHORYLATION (BY TYROSINE KINASES).
FT   MOD_RES      23     23       PHOSPHORYLATION (BY SERINE KINASES).
SQ   SEQUENCE   345 AA;  38583 MW;  568606 CN;
     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
//