ID   FYN_XENLA      STANDARD;      PRT;   536 AA.
AC   P13406;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-FEB-1994 (Rel. 28, Last sequence update)
DT   01-NOV-1995 (Rel. 32, Last annotation update)
DE   PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FYN (EC 2.7.1.112) (P59-FYN).
GN   FYN.
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=90191723; PubMed=2179818;
RA   Steele R.E., Deng J.C., Ghosn C.R., Fero J.B.;
RT   "Structure and expression of fyn genes in Xenopus laevis.";
RL   Oncogene 5:369-376(1990).
CC   -!- FUNCTION: IMPLICATED IN THE CONTROL OF CELL GROWTH.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- SUBUNIT: ASSOCIATES THROUGH ITS SH3 DOMAIN, TO THE P85 SUBUNIT OF
CC       PHOSPHATIDYLINOSITOL 3-KINASE.
CC   -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN.
CC   -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC
CC       DOMAIN. BELONGS TO THE SRC SUBFAMILY.
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DR   EMBL; X52188; CAA36435.1; -.
DR   EMBL; M27502; AAA49719.1; -.
DR   PIR; A43806; A43806.
DR   HSSP; P06241; 1FYN.
DR   INTERPRO; IPR000719; -.
DR   INTERPRO; IPR000980; -.
DR   INTERPRO; IPR001245; -.
DR   INTERPRO; IPR001452; -.
DR   PFAM; PF00017; SH2; 1.
DR   PFAM; PF00018; SH3; 1.
DR   PFAM; PF00069; pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
KW   Proto-oncogene; Transferase; Tyrosine-protein kinase; Phosphorylation;
KW   ATP-binding; Myristate; SH3 domain; SH2 domain; Palmitate;
KW   Lipoprotein.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID         2      2       PALMITATE (BY SIMILARITY).
FT   LIPID         5      5       PALMITATE (BY SIMILARITY).
FT   DOMAIN       81    142       SH3.
FT   DOMAIN      148    245       SH2.
FT   DOMAIN      270    523       PROTEIN KINASE.
FT   MOD_RES      11     11       PHOSPHORYLATION (BY PKC) (BY SIMILARITY).
FT   NP_BIND     276    284       ATP (BY SIMILARITY).
FT   BINDING     298    298       ATP (BY SIMILARITY).
FT   ACT_SITE    389    389       BY SIMILARITY.
FT   MOD_RES     419    419       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   536 AA;  60715 MW;  6A437586152A1326 CRC64;
     GCVQCKDKEA TKLTDERDNS LTQSLGYRYG TDPTPQHYPS FTVTTIPNYN NFHATAGQGL
     TVFGGVNSSS HTGTLRTRGG TGVTLFVALY DYEARTEDDL SFQKGEKFQI LNSSEGDWWE
     ARSLTTGGTG YIPSNYVAPV DSIQAEEWYF GKLGRKDAER QLLSFGNPRG TYLIRESETT
     KGAYSLSIRD WDDMKGDHVK HYKIRKLDNG GYYITTRAQF ETLQQLVQHY SERAAGLCCR
     LVVPCHKGMP RLTDLSVKTK DVWEIPRESL QLIKRLGNGQ FGEVWMGTWN GNTKVAIKTL
     KPGTMSPESF LEEAQIMKKL KHDKLVQLYA VVSEEPIYIV TEYMSKGSLL DFLKDGEGRA
     LKLPNLVDMA AQVARGMAYI ERMNYIHRDL RSANILVGNG LICKIADFGL ARLIEDNEYT
     ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELVT KGRVPYPGMN NREVLEQVER
     GYRMPCPQDC PISLHELMLN CWKKDPEERP TFEYLQGFLE DYFTATEPQY QPGDNL
//