KIN32_CAEEL
ID KIN32_CAEEL Reviewed; 867 AA.
AC Q95YD4; Q8T879;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Inactive tyrosine-protein kinase kin-32 {ECO:0000305};
GN Name=kin-32 {ECO:0000312|WormBase:C30F8.4a};
GN ORFNames=C30F8.4 {ECO:0000312|WormBase:C30F8.4a};
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|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 [2] {ECO:0000305}
RP TISSUE SPECIFICITY, FUNCTION, LACK OF CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18297732; DOI=10.1002/dvdy.21457;
RA Cram E.J., Fontanez K.M., Schwarzbauer J.E.;
RT "Functional characterization of KIN-32, the Caenorhabditis elegans homolog
RT of focal adhesion kinase.";
RL Dev. Dyn. 237:837-846(2008).
CC -!- FUNCTION: Has apparently no tyrosine kinase activity in vitro when
CC expressed in mammalian cells. {ECO:0000269|PubMed:18297732}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C30F8.4a};
CC IsoId=Q95YD4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C30F8.4b};
CC IsoId=Q95YD4-2; Sequence=VSP_057893;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles and some neurons in
CC the head. {ECO:0000269|PubMed:18297732}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no obvious
CC phenotype. {ECO:0000269|PubMed:18297732}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. FAK subfamily. {ECO:0000305}.
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DR EMBL; BX284601; CCD66186.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66187.1; -; Genomic_DNA.
DR RefSeq; NP_740841.1; NM_170854.3. [Q95YD4-1]
DR RefSeq; NP_740842.1; NM_170855.4. [Q95YD4-2]
DR AlphaFoldDB; Q95YD4; -.
DR SMR; Q95YD4; -.
DR STRING; 6239.C30F8.4a; -.
DR EPD; Q95YD4; -.
DR PaxDb; Q95YD4; -.
DR EnsemblMetazoa; C30F8.4a.1; C30F8.4a.1; WBGene00002213. [Q95YD4-1]
DR EnsemblMetazoa; C30F8.4b.1; C30F8.4b.1; WBGene00002213. [Q95YD4-2]
DR EnsemblMetazoa; C30F8.4b.2; C30F8.4b.2; WBGene00002213. [Q95YD4-2]
DR GeneID; 172135; -.
DR KEGG; cel:CELE_C30F8.4; -.
DR UCSC; C30F8.4a.1; c. elegans.
DR CTD; 172135; -.
DR WormBase; C30F8.4a; CE25798; WBGene00002213; kin-32. [Q95YD4-1]
DR WormBase; C30F8.4b; CE30493; WBGene00002213; kin-32. [Q95YD4-2]
DR eggNOG; KOG4257; Eukaryota.
DR GeneTree; ENSGT00940000168088; -.
DR HOGENOM; CLU_002646_1_0_1; -.
DR InParanoid; Q95YD4; -.
DR OMA; EYPTAVK; -.
DR OrthoDB; 43729at2759; -.
DR PhylomeDB; Q95YD4; -.
DR Reactome; R-CEL-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-418885; DCC mediated attractive signaling.
DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-8874081; MET activates PTK2 signaling.
DR Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR PRO; PR:Q95YD4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002213; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd13190; FERM_C_FAK1; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR041784; FAK1/PYK2_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF03623; Focal_AT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF68993; SSF68993; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..867
FT /note="Inactive tyrosine-protein kinase kin-32"
FT /id="PRO_0000434040"
FT DOMAIN 3..327
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 367..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 674..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 662..691
FT /evidence="ECO:0000255"
FT COMPBIAS 680..694
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057893"
SQ SEQUENCE 867 AA; 97999 MW; 148D9DFD4AC276EF CRC64;
MEGLARVFLI GGASKAVRYD EQTTIERVIH VVARGIGISQ VAVAHFALRL VTGPSPQTAG
SGDSLWLHPM LRITQLPHIY ARHLPIGVCD EIKLEMRMRF MPQSVYELQA TDSSAFVYLH
EQVVDEFFSH VAWRSSVEVA LEVAALKVCR DFAEHQHNKG ADHHLEDLDI EACIQSLIPN
VLHNPGFKHS HLKKTFTAYI KKFSATSPNE SIIRSLALLL EVVKFDVELF KASLGAGWTK
PVELVVGPHT GLSYRLNERC DSSRLLELRT IAEITIRKME NGSEKTLMQL NLSGAAKPVL
ITLSTEELSQ SLAHLLDGYQ MLYNQRDSVF KLKGIERCET LTMHEATIRP KTPNNIDSNI
RLRRELITLK ELIGGGQFGN VYKAVYHDLE KDERIAVAVK VCKTDAEPAD TQLILQESSL
MRNFRHSNII QLIGVCVDQP MWLVLELAPK GELREYLQQE KDWLPLRILT LFCSQICDSL
VYLHSTRFVH RDIAARNILV CSPQCVKLAD FGLSRALDYD AVYTASRGKL PIKWLAPESV
NYRQFSMASD VWMFGVCMWE IFSLGVKPWA GVTNSDVIMH IEQGSRPPCP EKCPTALYNF
IRSKMWAIEP HKRPTVDQIY AIIEDVRQQI IQNIPPEQII VGKPMTAAGV IVAEMSSLPG
LTLYRTMEDQ KRQAEEDAKW LEQEDDEDED DQDIDQIPST SHSSVENIRT SNGYLHHTPT
STRSLRFEDK TSRGLRRSVD GVCDAVTKLQ NSFNNLTHND DFLHSVKEVT SQLREMLIVA
SGMRDRVTTT TQRTDVDMTK TLIANDMKQM SRVMGKLQVN GHQATYNTLR RDVVRICGEL
AVNCTTLQLQ LTQPPLENEF SSLLSNC
