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Tyrosine-protein kinase csk-1 (EC 2.7.10.2) (C-terminal src kinase)

 CSK1_CAEEL              Reviewed;         539 AA.
G5ECJ6; V6CL92;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
22-NOV-2017, entry version 62.
RecName: Full=Tyrosine-protein kinase csk-1 {ECO:0000305};
EC=2.7.10.2 {ECO:0000269|PubMed:12527374};
AltName: Full=C-terminal src kinase {ECO:0000305};
Name=csk-1 {ECO:0000312|WormBase:Y48G1C.2a};
ORFNames=Y48G1C.2 {ECO:0000312|WormBase:Y48G1C.2a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:BAC76831.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
SPECIFICITY, AND MUTAGENESIS OF LYS-310.
PubMed=12527374; DOI=10.1016/S0014-5793(02)03819-X;
Hirose T., Koga M., Ohshima Y., Okada M.;
"Distinct roles of the Src family kinases, SRC-1 and KIN-22, that are
negatively regulated by CSK-1 in C. elegans.";
FEBS Lett. 534:133-138(2003).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
LYS-310.
PubMed=19210548; DOI=10.1111/j.1365-2443.2008.01275.x;
Takata N., Itoh B., Misaki K., Hirose T., Yonemura S., Okada M.;
"Non-receptor tyrosine kinase CSK-1 controls pharyngeal muscle
organization in Caenorhabditis elegans.";
Genes Cells 14:381-393(2009).
-!- FUNCTION: Non-receptor tyrosine-protein kinase which plays a role
in pharynx function by regulating pumping and the orientation of
pharyngeal muscle fibers, independently of src-1 and src-2
(PubMed:19210548). May phosphorylate and thereby negatively
regulate src-1 and src-2 activities (PubMed:12527374).
{ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000269|PubMed:12527374}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P41240};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P41240};
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a {ECO:0000312|WormBase:Y48G1C.2a};
IsoId=G5ECJ6-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:Y48G1C.2b};
IsoId=G5ECJ6-2; Sequence=VSP_057936;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed predominantly in pharyngeal muscles
in procorpus, metacorpus and terminal bulb (PubMed:12527374,
PubMed:19210548). Expressed also in some neurons (ASE, ADF, AVA,
AUA, RMDV and BAG) in the head region, anchor cell, vulva, cells
around anus, body wall muscle and gondal distal tip cells
(PubMed:12527374). {ECO:0000269|PubMed:12527374,
ECO:0000269|PubMed:19210548}.
-!- DEVELOPMENTAL STAGE: Expressed mainly in the pharynx in the loop
stage embryo. At L1 larval stage, predominantly expressed in the
pharynx with some expression in body wall muscle, anchor cells and
tail region. {ECO:0000269|PubMed:19210548}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB096875; BAC76831.1; -; mRNA.
EMBL; BX284601; CCD71723.1; -; Genomic_DNA.
EMBL; BX284601; CDK13329.1; -; Genomic_DNA.
RefSeq; NP_001021778.1; NM_001026607.2. [G5ECJ6-1]
RefSeq; NP_001293162.1; NM_001306233.1. [G5ECJ6-2]
UniGene; Cel.5849; -.
ProteinModelPortal; G5ECJ6; -.
SMR; G5ECJ6; -.
STRING; 6239.Y48G1C.2.1; -.
EPD; G5ECJ6; -.
PaxDb; G5ECJ6; -.
PeptideAtlas; G5ECJ6; -.
EnsemblMetazoa; Y48G1C.2a; Y48G1C.2a; WBGene00000812. [G5ECJ6-1]
GeneID; 266817; -.
KEGG; cel:CELE_Y48G1C.2; -.
CTD; 266817; -.
WormBase; Y48G1C.2a; CE34405; WBGene00000812; csk-1. [G5ECJ6-1]
WormBase; Y48G1C.2b; CE49183; WBGene00000812; csk-1. [G5ECJ6-2]
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
KO; K05728; -.
OMA; WALNMKD; -.
OrthoDB; EOG091G05PB; -.
PhylomeDB; G5ECJ6; -.
Reactome; R-CEL-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-CEL-354192; Integrin alphaIIb beta3 signaling.
PRO; PR:G5ECJ6; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00000812; -.
ExpressionAtlas; G5ECJ6; baseline.
GO; GO:0005911; C:cell-cell junction; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0030536; P:larval feeding behavior; IMP:WormBase.
GO; GO:0048747; P:muscle fiber development; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
CDD; cd09937; SH2_csk_like; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035026; CSK.
InterPro; IPR035027; Csk-like_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
PANTHER; PTHR24418:SF307; PTHR24418:SF307; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF55550; SSF55550; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Kinase;
Magnesium; Manganese; Metal-binding; Nucleotide-binding;
Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
CHAIN 1 539 Tyrosine-protein kinase csk-1.
{ECO:0000305}.
/FTId=PRO_0000434504.
DOMAIN 43 110 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 151 241 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 283 535 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 289 297 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 403 403 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 310 310 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 1 1 M -> MPIFSASRSRSHHRNSRNPTKFSNFSIEKRSHSLGG
SSSSPTSSFSSNDEFDDRQNKNKFWRQRNVSNAEIERIIED
FIANGILKM (in isoform b). {ECO:0000305}.
/FTId=VSP_057936.
MUTAGEN 310 310 K->M: Loss of kinase activity. Reduction
in src-1 and src-2-mediated tyrosine
phosphorylation. Mutants arrest at L1
larval stage.
{ECO:0000269|PubMed:12527374,
ECO:0000269|PubMed:19210548}.
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


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