ID   LYN_RAT        STANDARD;      PRT;   511 AA.
AC   Q07014; Q63320;
DT   01-JUN-1994 (Rel. 29, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   TYROSINE-PROTEIN KINASE LYN (EC 2.7.1.112).
GN   LYN.
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   SEQUENCE FROM N.A.
RA   Minoguchi K., Nishikata H., Siraganian R.P.;
RT   "Bacterially expressed rat p56lyn binds several proteins in rat
RT   basophilic leukemia cells including pp72, a tyrosine phosphorylated
RT   protein prominent in activated cells.";
RL   J. Immunol. 150:222-222(1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=94171041; PubMed=8125304;
RA   Rider L.G., Raben N., Miller L., Jelsema C.;
RT   "The cDNAs encoding two forms of the LYN protein tyrosine kinase are
RT   expressed in rat mast cells and human myeloid cells.";
RL   Gene 138:219-222(1994).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=97442484; PubMed=9295361;
RA   Vonakis B.M., Chen H., Haleem-Smith H., Metzger H.;
RT   "The unique domain as the site on Lyn kinase for its constitutive
RT   association with the high affinity receptor for IgE.";
RL   J. Biol. Chem. 272:24072-24080(1997).
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; LYN A (SHOWN HERE) AND LYN B;
CC       ARE PRODUCED BY ALTERNATIVE SPLICING.
CC   -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN B-LYMPHOID AND
CC       MYELOID CELLS.
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.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L14951; AAA41549.1; -.
DR   EMBL; L14782; AAA20944.1; -.
DR   EMBL; L14823; AAA20945.1; -.
DR   EMBL; AF000300; AAB71344.1; -.
DR   EMBL; AF000301; AAB71345.1; -.
DR   EMBL; AF000302; AAB71346.1; -.
DR   HSSP; P08631; 2HCK.
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; 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; Tyrosine-protein kinase; Phosphorylation;
KW   Transferase; ATP-binding; Myristate; SH2 domain; SH3 domain;
KW   Palmitate; Lipoprotein; Alternative splicing.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID         2      2       PALMITATE (BY SIMILARITY).
FT   DOMAIN       62    122       SH3.
FT   DOMAIN      128    225       SH2.
FT   DOMAIN      246    500       PROTEIN KINASE.
FT   NP_BIND     252    260       ATP (BY SIMILARITY).
FT   BINDING     274    274       ATP (BY SIMILARITY).
FT   ACT_SITE    366    366       BY SIMILARITY.
FT   MOD_RES     396    396       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT   MOD_RES     507    507       PHOSPHORYLATION (BY SIMILARITY).
FT   VARSPLIC     24     44       MISSING (IN ISOFORM LYN B).
FT   CONFLICT    230    230       P -> L (IN REF. 2).
FT   CONFLICT    307    307       V -> A (IN REF. 2).
FT   CONFLICT    418    418       C -> Y (IN REF. 2).
SQ   SEQUENCE   511 AA;  58529 MW;  24A2E5E229CD43ED CRC64;
     GCIKSKRKDN LNDDGVDMKT QPVRNTDRTI YVRDPTSNKQ QRPVPESQLL PGQRFQAKDP
     EEQGDIVVAL YPYDGIHPDD LSFKKGEKMK VLEEHGEWWK AKSLSSKREG FIPSNYVAKV
     NTLETEEWFF KDITRKDAER QLLAPGNSAG AFLIRESETL KGSFSLSVRD YDPMHGDVIK
     HYKIRSLDNG GYYISPRITF PCISDMIKHY QKQSDGLCRR LEKACISPKP QKPWDKDAWE
     IPRESIKLVK KLGAGQFGEV WMGYYNNSTK VAVKTLKPGT MSAQAFLEEA NLMKTLQHDK
     LVRLYAVVTK EEPIYIITEF MAKGSLLDFL KSDEGSKVLL PKLIDFSAQI AEGMAYIERK
     NYIHRDLRAA NVLVSESLMC KIADFGLARV IEDNEYTARE GAKFPIKWTA PEAINFGCFT
     IKSDVWSFGI LLYEIVTYGK IPYPGRTNAD VMTALSQGYR MPRMENCPDE LYDIMKMCWK
     ESAEERPTFD YLQSVLDDFY TATEGQYQQQ P
//