CSK1_CAEEL
ID CSK1_CAEEL Reviewed; 539 AA.
AC G5ECJ6; V6CL92;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tyrosine-protein kinase csk-1 {ECO:0000305};
DE EC=2.7.10.2 {ECO:0000269|PubMed:12527374};
DE AltName: Full=C-terminal src kinase {ECO:0000305};
GN Name=csk-1 {ECO:0000312|WormBase:Y48G1C.2a};
GN ORFNames=Y48G1C.2 {ECO:0000312|WormBase:Y48G1C.2a};
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:0000312|EMBL:BAC76831.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF LYS-310.
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LYS-310.
RX PubMed=19210548; DOI=10.1111/j.1365-2443.2008.01275.x;
RA Takata N., Itoh B., Misaki K., Hirose T., Yonemura S., Okada M.;
RT "Non-receptor tyrosine kinase CSK-1 controls pharyngeal muscle organization
RT in Caenorhabditis elegans.";
RL Genes Cells 14:381-393(2009).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase which plays a role in
CC pharynx function by regulating pumping and the orientation of
CC pharyngeal muscle fibers, independently of src-1 and src-2
CC (PubMed:19210548). May phosphorylate and thereby negatively regulate
CC src-1 and src-2 activities (PubMed:12527374).
CC {ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548}.
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:P41240};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P41240};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y48G1C.2a};
CC IsoId=G5ECJ6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y48G1C.2b};
CC IsoId=G5ECJ6-2; Sequence=VSP_057936;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in pharyngeal muscles in
CC procorpus, metacorpus and terminal bulb (PubMed:12527374,
CC PubMed:19210548). Expressed also in some neurons (ASE, ADF, AVA, AUA,
CC RMDV and BAG) in the head region, anchor cell, vulva, cells around
CC anus, body wall muscle and gondal distal tip cells (PubMed:12527374).
CC {ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548}.
CC -!- DEVELOPMENTAL STAGE: Expressed mainly in the pharynx in the loop stage
CC embryo. At L1 larval stage, predominantly expressed in the pharynx with
CC some expression in body wall muscle, anchor cells and tail region.
CC {ECO:0000269|PubMed:19210548}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSK subfamily. {ECO:0000305}.
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DR EMBL; AB096875; BAC76831.1; -; mRNA.
DR EMBL; BX284601; CCD71723.1; -; Genomic_DNA.
DR EMBL; BX284601; CDK13329.1; -; Genomic_DNA.
DR RefSeq; NP_001021778.1; NM_001026607.2.
DR RefSeq; NP_001293162.1; NM_001306233.1. [G5ECJ6-2]
DR AlphaFoldDB; G5ECJ6; -.
DR SMR; G5ECJ6; -.
DR STRING; 6239.Y48G1C.2.2; -.
DR EPD; G5ECJ6; -.
DR PaxDb; G5ECJ6; -.
DR PeptideAtlas; G5ECJ6; -.
DR EnsemblMetazoa; Y48G1C.2a.1; Y48G1C.2a.1; WBGene00000812. [G5ECJ6-1]
DR EnsemblMetazoa; Y48G1C.2a.2; Y48G1C.2a.2; WBGene00000812. [G5ECJ6-1]
DR EnsemblMetazoa; Y48G1C.2a.3; Y48G1C.2a.3; WBGene00000812. [G5ECJ6-1]
DR EnsemblMetazoa; Y48G1C.2b.1; Y48G1C.2b.1; WBGene00000812. [G5ECJ6-2]
DR GeneID; 266817; -.
DR KEGG; cel:CELE_Y48G1C.2; -.
DR CTD; 266817; -.
DR WormBase; Y48G1C.2a; CE34405; WBGene00000812; csk-1. [G5ECJ6-1]
DR WormBase; Y48G1C.2b; CE49183; WBGene00000812; csk-1. [G5ECJ6-2]
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; G5ECJ6; -.
DR OMA; QTMPWFH; -.
DR OrthoDB; 491765at2759; -.
DR PhylomeDB; G5ECJ6; -.
DR Reactome; R-CEL-180292; GAB1 signalosome.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR PRO; PR:G5ECJ6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000812; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5ECJ6; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
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; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:WormBase.
DR GO; GO:0055001; P:muscle cell development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR CDD; cd09937; SH2_csk_like; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035027; Csk-like_SH2.
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; 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 PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 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 Alternative splicing; ATP-binding; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome; SH2 domain;
KW SH3 domain; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..539
FT /note="Tyrosine-protein kinase csk-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434504"
FT DOMAIN 43..110
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 151..241
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 283..535
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 289..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1
FT /note="M -> MPIFSASRSRSHHRNSRNPTKFSNFSIEKRSHSLGGSSSSPTSSFSS
FT NDEFDDRQNKNKFWRQRNVSNAEIERIIEDFIANGILKM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057936"
FT MUTAGEN 310
FT /note="K->M: Loss of kinase activity. Reduction in src-1
FT and src-2-mediated tyrosine phosphorylation. Mutants arrest
FT at L1 larval stage."
FT /evidence="ECO:0000269|PubMed:12527374,
FT ECO:0000269|PubMed:19210548"
SQ SEQUENCE 539 AA; 60157 MW; 35737ADE05B10C1E CRC64;
MSNGNSYNHH HQFPMSIPIS CSSHSIQSQS RMNTLNANRD LLSPGNDVIV TRTVSPSFYS
HGMPARDNVF RKDDHVRILG NTTDPAWYRA RNANQEEGLV HADCVVRING QAYDNGIVRM
RASGCDVAPG AASTTSSTSS HHSTAANHQP WFHSMISREN TEKLLRGKPD GTFLVRESTN
FPGDFTLCMS FHGKVEHYRI EQTSGGQLTC DKEEYFSNLT QLVSHYKRDA DGLCHRLVTP
IICETATFSS NGSSSFGSSS TVDLEDRTSV FRHAGLVISS NDIDVGDTIG HGEFGDVRLG
TYKNRKVALK VSKRHGNGML DSLLDEAKFM VGLSHPNLVT LVGVVLDDVN VYMITEYMAN
GNLIDLLRSR GRHALERRQL MMFAMDICQG MCYLESKQIV HRDLAARNVL LDDDLVAKVS
DFGLAKKANS QSHDSASGKF PIKWTAPEAL RHSQFTTKSD VWSFGILLWE IFSFGRVPYP
RIPIQDVVRY IEKGYRMEAP EGCPPEIFKV MNETWALSAQ DRPSFGQVLQ RLTTIRNTV
