ID   SRC1_XENLA              Reviewed;         532 AA.
AC   P13115;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Tyrosine-protein kinase Src-1;
DE            EC=2.7.10.2;
DE   AltName: Full=p60-Src-1;
GN   Name=src-a; Synonyms=src1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2499582; DOI=10.1016/s0021-9258(18)81671-4;
RA   Steele R.E., Unger T.F., Mardis M.J., Fero J.B.;
RT   "The two Xenopus laevis SRC genes are co-expressed and each produces
RT   functional pp60src.";
RL   J. Biol. Chem. 264:10649-10653(1989).
RN   [2]
RP   SEQUENCE REVISION TO 220; 242 AND 340.
RA   Steele R.E.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M24704; AAA49962.2; -; mRNA.
DR   AlphaFoldDB; P13115; -.
DR   SMR; P13115; -.
DR   BRENDA; 2.7.10.2; 6725.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; SH2 domain;
KW   SH3 domain; Transferase; Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..532
FT                   /note="Tyrosine-protein kinase Src-1"
FT                   /id="PRO_0000088145"
FT   DOMAIN          80..141
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          147..244
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          266..519
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        385
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         272..280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         415
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  59895 MW;  83977919D1612D41 CRC64;
     MGATKSKPRE GGPRSRSLDI VEGSHQPFTS LSASQTPNKS LDSHRPPAQP FGGNCDLTPF
     GGINFSDTIT SPQRTGPLAG GVTTFVALYD YESRTETDLS FKKGERLQIV NNTEGDWWLA
     RSLSSGQTGY IPSNYVAPSD SIQAEEWYLG KITRREAERL LLSLENPRGT FLVRESETTK
     GAYCLSVSDY DANRGLNVKH YKIRKLDSGG FYITSRTQFI SLQQLVAYYS KHADGLCHRL
     TTVCPTAKPQ TQGLSRDAWE IPRDSLRLEL KLGQGCFGEV WMGTWNGTTR VAIKTLKPGT
     MSPEAFLQEA QVMKKLRHEK LVQLYAVVSE EPIYIVTEYI SKGSLLDFLK GEMGRYLRLP
     QLVDMAAQIA SGMAYVERMN YVHRDLRAAN ILVGENLVCK VADFGLARLI EDNEYTARQG
     AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELTTKGRV PYPGMVNREV LDQVERGYRM
     PCPPDCPESL HDLMFQCWRK DPEERPTFEY LQAFLEDYFT ATEPQYQPGD NL