ID   SRC2_CAEEL              Reviewed;         507 AA.
AC   O45539;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Tyrosine protein-kinase src-2 {ECO:0000305};
DE            EC=2.7.10.2 {ECO:0000269|PubMed:12527374};
DE   AltName: Full=SRC oncogene related protein 2 {ECO:0000312|WormBase:F49B2.5};
GN   Name=src-2 {ECO:0000312|WormBase:F49B2.5};
GN   Synonyms=kin-22 {ECO:0000312|WormBase:F49B2.5};
GN   ORFNames=F49B2.5 {ECO:0000312|WormBase:F49B2.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-500, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF LYS-268 AND TYR-500.
RX   PubMed=12527374; DOI=10.1016/s0014-5793(02)03819-x;
RA   Hirose T., Koga M., Ohshima Y., Okada M.;
RT   "Distinct roles of the Src family kinases, SRC-1 and KIN-22, that are
RT   negatively regulated by CSK-1 in C. elegans.";
RL   FEBS Lett. 534:133-138(2003).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16024786; DOI=10.1128/mcb.25.15.6485-6495.2005;
RA   Lee J., Li W., Guan K.L.;
RT   "SRC-1 mediates UNC-5 signaling in Caenorhabditis elegans.";
RL   Mol. Cell. Biol. 25:6485-6495(2005).
CC   -!- FUNCTION: Non-receptor tyrosine-protein kinase which may play a role in
CC       larval and pharynx development. Unlike src-1, does not play a role in
CC       embryonic development. {ECO:0000269|PubMed:12527374}.
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:0000269|PubMed:12527374};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:G5EE56};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:G5EE56};
CC   -!- ACTIVITY REGULATION: May be inhibited by csk-1-mediated phosphorylation
CC       at Tyr-500. {ECO:0000305|PubMed:12527374}.
CC   -!- TISSUE SPECIFICITY: Expressed in vulva, cells around anus and
CC       pharyngeal muscles. {ECO:0000269|PubMed:12527374}.
CC   -!- PTM: May be phosphorylated on Tyr-500 by csk-1.
CC       {ECO:0000269|PubMed:12527374}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no obvious effect
CC       on embryonic development (PubMed:12527374). Animals have a slight
CC       decrease in unc-5 tyrosine phosphorylation (PubMed:16024786).
CC       {ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:16024786}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000305}.
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DR   EMBL; BX284601; CAB04427.2; -; Genomic_DNA.
DR   PIR; T22405; T22405.
DR   RefSeq; NP_493502.1; NM_061101.4.
DR   AlphaFoldDB; O45539; -.
DR   SMR; O45539; -.
DR   DIP; DIP-26743N; -.
DR   IntAct; O45539; 42.
DR   MINT; O45539; -.
DR   STRING; 6239.F49B2.5.1; -.
DR   iPTMnet; O45539; -.
DR   EPD; O45539; -.
DR   PaxDb; 6239-F49B2-5; -.
DR   EnsemblMetazoa; F49B2.5.1; F49B2.5.1; WBGene00005078.
DR   GeneID; 173296; -.
DR   KEGG; cel:CELE_F49B2.5; -.
DR   UCSC; F49B2.5; c. elegans.
DR   AGR; WB:WBGene00005078; -.
DR   WormBase; F49B2.5; CE24991; WBGene00005078; src-2.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000167963; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; O45539; -.
DR   OMA; STRDQWE; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; O45539; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   SignaLink; O45539; -.
DR   PRO; PR:O45539; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00005078; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0160094; P:nematode pharynx development; IMP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd05068; PTKc_Frk_like; 1.
DR   CDD; cd10370; SH2_Src_Src42; 1.
DR   CDD; cd11845; SH3_Src_like; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF373; TYROSINE-PROTEIN KINASE SRC42A; 1.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipoprotein; Manganese; Metal-binding; 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:0000255"
FT   CHAIN           2..507
FT                   /note="Tyrosine protein-kinase src-2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000434508"
FT   DOMAIN          57..118
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          124..216
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          240..494
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   ACT_SITE        358
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         246..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         500
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305|PubMed:12527374"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         268
FT                   /note="K->M: Probable loss of kinase activity. In a wild
FT                   type background, 30 percent die at the larval stage and 4
FT                   percent of surviving animals have abnormalities in the
FT                   pharynx structure."
FT                   /evidence="ECO:0000269|PubMed:12527374"
FT   MUTAGEN         500
FT                   /note="Y->F: Abolishes phosphorylation which results in
FT                   constitutive activation. In a wild type background, 76
FT                   percent die at the larval stage and 34 percent of surviving
FT                   animals have abnormalities in the pharynx structure."
FT                   /evidence="ECO:0000269|PubMed:12527374"
SQ   SEQUENCE   507 AA;  57530 MW;  CD3DC68FC91ED86D CRC64;
     MGSCIGKEDP PPGATSPVHT SSTLGRESLP SHPRIPSIGP IAASSSGNTI DKNQNISQSA
     NFVALFQYDA RTDDDLSFKK DDILEILNDT QGDWWFARHK ATGRTGYIPS NYVAREKSIE
     SQPWYFGKMR RIDAEKCLLH TLNEHGAFLV RDSESRQHDL SLSVRENDSV KHYRIRQLDH
     GGYFIARRRP FATLHDLIAH YQREADGLCV NLGAPCAKSE APQTTTFTYD DQWEVDRRSV
     RLIRQIGAGQ FGEVWEGRWN VNVPVAVKKL KAGTADPTDF LAEAQIMKKL RHPKLLSLYA
     VCTRDEPILI VTELMQENLL TFLQRRGRQC QMPQLVEISA QVAAGMAYLE EMNFIHRDLA
     ARNILINNSL SVKIADFGLA RILMKENEYE ARTGARFPIK WTAPEAANYN RFTTKSDVWS
     FGILLTEIVT FGRLPYPGMT NAEVLQQVDA GYRMPCPAGC PVTLYDIMQQ CWRSDPDKRP
     TFETLQWKLE DLFNLDSSEY KEASINF
//