SRC2_CAEEL
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 03-AUG-2022, entry version 173.
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; -.
DR iPTMnet; O45539; -.
DR EPD; O45539; -.
DR PaxDb; O45539; -.
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 CTD; 173296; -.
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; TKDEPIL; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; O45539; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
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 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:0004713; F: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:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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 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
