ID   HCK_MOUSE      STANDARD;      PRT;   524 AA.
AC   P08103;
DT   01-AUG-1988 (Rel. 08, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   TYROSINE-PROTEIN KINASE HCK (EC 2.7.1.112) (P56-HCK AND P60-HCK)
DE   (HEMOPOIETIC CELL KINASE) (B-CELL/MYELOID KINASE) (BMK).
GN   HCK.
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   SEQUENCE OF 22-524 FROM N.A.
RC   STRAIN=ICR; TISSUE=MACROPHAGE;
RX   MEDLINE=88067781; PubMed=3684607;
RA   Klemsz M.J., McKercher S.R., Maki R.A.;
RT   "Nucleotide sequence of the mouse hck gene.";
RL   Nucleic Acids Res. 15:9600-9600(1987).
RN   [2]
RP   SEQUENCE OF 22-524 FROM N.A.
RX   MEDLINE=88068587; PubMed=3317404;
RA   Holtzman D.A., Cook W.D., Dunn A.R.;
RT   "Isolation and sequence of a cDNA corresponding to a src-related gene
RT   expressed in murine hemopoietic cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:8325-8329(1987).
RN   [3]
RP   SEQUENCE OF 1-22 FROM N.A., AND ALTERNATIVE INITIATION.
RX   MEDLINE=91342636; PubMed=1875927;
RA   Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
RT   "Two isoforms of murine hck, generated by utilization of alternative
RT   translational initiation codons, exhibit different patterns of
RT   subcellular localization.";
RL   Mol. Cell. Biol. 11:4363-4370(1991).
CC   -!- FUNCTION: MAY SERVE AS PART OF A SIGNALING PATHWAY COUPLING THE FC
CC       RECEPTOR TO THE ACTIVATION OF THE RESPIRATORY BURST. MAY ALSO
CC       CONTRIBUTE TO NEUTROPHIL MIGRATION AND MAY REGULATE THE
CC       DEGRANULATION PROCESS OF NEUTROPHILS.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- SUBCELLULAR LOCATION: P59-HCK AND P56-HCK ARE ASSOCIATED WITH
CC       MEMBRANES. P59-HCK IS ALSO CYTOPLASMIC.
CC   -!- ALTERNATIVE PRODUCTS: THE P59-HCK AND P56-HCK ARE PRODUCED BY THE
CC       USE OF ALTERNATIVE INITIATION SITES.
CC   -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN CELLS OF THE
CC       MYELOID AND B-LYMPHOID LINEAGES.
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; Y00487; CAA68544.1; -.
DR   EMBL; J03023; AAA37305.1; -.
DR   PIR; A27282; TVMSHC.
DR   PIR; A39973; A39973.
DR   HSSP; P08631; 2HCK.
DR   MGD; MGI:96052; Hck.
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   Transferase; Tyrosine-protein kinase; Phosphorylation; ATP-binding;
KW   Myristate; SH2 domain; SH3 domain; Alternative initiation.
FT   CHAIN         1    524       TYROSINE-PROTEIN KINASE P59-HCK.
FT   CHAIN        22    524       TYROSINE-PROTEIN KINASE P56-HCK.
FT   INIT_MET     22     22       FOR P56-HCK.
FT   LIPID         2      2       MYRISTATE (BY SIMILARITY).
FT   LIPID        23     23       MYRISTATE (BY SIMILARITY).
FT   DOMAIN       76    136       SH3.
FT   DOMAIN      142    239       SH2.
FT   DOMAIN      260    513       PROTEIN KINASE.
FT   NP_BIND     266    274       ATP (BY SIMILARITY).
FT   BINDING     288    288       ATP (BY SIMILARITY).
FT   ACT_SITE    379    379       BY SIMILARITY.
FT   MOD_RES     409    409       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   524 AA;  59129 MW;  DF72FD69B38C9706 CRC64;
     MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY VPDPTSSSKL
     GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG DQMVVLEEAG EWWKARSLAT
     KKEGYIPSNY VARVNSLETE EWFFKGISRK DAERHLLAPG NMLGSFMIRD SETTKGSYSL
     SVRDFDPQHG DTVKHYKIRT LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV
     SPKPQKPWEK DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF
     LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK QPLPKLIDFS
     AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK
     WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALEH GYRMPRPDNC
     PEELYNIMIR CWKNRPEERP TFEYIQSVLD DFYTATESQY QQQP
//