ARK1_CAEEL
ID ARK1_CAEEL Reviewed; 1043 AA.
AC G5EBZ8; C6KRP0;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ack-related non-receptor tyrosine kinase {ECO:0000303|PubMed:10949028};
DE EC=2.7.10.2 {ECO:0000250|UniProtKB:Q07912};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q07912};
DE AltName: Full=Ras-regulating kinase ark-1 {ECO:0000312|WormBase:C01C7.1a};
GN Name=ark-1 {ECO:0000312|WormBase:C01C7.1a};
GN ORFNames=C01C7.1 {ECO:0000312|WormBase:C01C7.1a};
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:CAB65957.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB65957.1};
RX PubMed=10949028; DOI=10.1016/s1097-2765(05)00001-8;
RA Hopper N.A., Lee J., Sternberg P.W.;
RT "ARK-1 inhibits EGFR signaling in C. elegans.";
RL Mol. Cell 6:65-75(2000).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=14657502; DOI=10.1126/science.1087167;
RA Shibata Y., Branicky R., Landaverde I.O., Hekimi S.;
RT "Redox regulation of germline and vulval development in Caenorhabditis
RT elegans.";
RL Science 302:1779-1782(2003).
CC -!- FUNCTION: Probable tyrosine protein kinase which plays a role in vulva
CC development, probably by acting as a negative regulator of the let-
CC 23/EGFR and let-60/ras pathway. Involved in the negative regulation of
CC germline development (PubMed:14657502). {ECO:0000269|PubMed:10949028,
CC ECO:0000269|PubMed:14657502}.
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:0000250|UniProtKB:Q07912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q07912};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q07912};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q07912};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C01C7.1a};
CC IsoId=G5EBZ8-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C01C7.1b};
CC IsoId=G5EBZ8-2; Sequence=VSP_057849;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a gap-1 mutant
CC background causes a hyperinduction of the vulva in 60 percent of
CC animals (PubMed:10949028). In addition, suppresses the slow germline
CC development of clk-1 mutants (PubMed:14657502).
CC {ECO:0000269|PubMed:10949028, ECO:0000269|PubMed:14657502}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ271057; CAB65957.1; -; mRNA.
DR EMBL; BX284604; CAB05120.2; -; Genomic_DNA.
DR EMBL; BX284604; CAZ39159.1; -; Genomic_DNA.
DR PIR; T18802; T18802.
DR RefSeq; NP_001255653.1; NM_001268724.1. [G5EBZ8-2]
DR RefSeq; NP_001255654.1; NM_001268725.1. [G5EBZ8-1]
DR AlphaFoldDB; G5EBZ8; -.
DR SMR; G5EBZ8; -.
DR IntAct; G5EBZ8; 4.
DR STRING; 6239.C01C7.1a; -.
DR EPD; G5EBZ8; -.
DR PaxDb; G5EBZ8; -.
DR PeptideAtlas; G5EBZ8; -.
DR PRIDE; G5EBZ8; -.
DR EnsemblMetazoa; C01C7.1a.1; C01C7.1a.1; WBGene00000186. [G5EBZ8-1]
DR EnsemblMetazoa; C01C7.1b.1; C01C7.1b.1; WBGene00000186. [G5EBZ8-2]
DR GeneID; 178218; -.
DR KEGG; cel:CELE_C01C7.1; -.
DR CTD; 178218; -.
DR WormBase; C01C7.1a; CE26967; WBGene00000186; ark-1. [G5EBZ8-1]
DR WormBase; C01C7.1b; CE43742; WBGene00000186; ark-1. [G5EBZ8-2]
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000173732; -.
DR HOGENOM; CLU_292269_0_0_1; -.
DR InParanoid; G5EBZ8; -.
DR OMA; YYRSEFT; -.
DR OrthoDB; 246393at2759; -.
DR SignaLink; G5EBZ8; -.
DR PRO; PR:G5EBZ8; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000186; Expressed in pharyngeal muscle cell (C elegans) and 4 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR000095; CRIB_dom.
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; 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; PF07653; SH3_2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1043
FT /note="Ack-related non-receptor tyrosine kinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433876"
FT DOMAIN 113..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 379..444
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 484..498
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 443..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 785..812
FT /evidence="ECO:0000255"
FT COMPBIAS 459..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1026..1029
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057849"
SQ SEQUENCE 1043 AA; 115394 MW; 1B011941CB48BCAD CRC64;
MREEPTAGTA DATLNKLLQA ADLSGYESDL RRKLKLRNAA DLQYVEEVDL LSVGMSRPEQ
KRLRKEYTKM FPSGIFGKVK KAFKRAESLD RKTSNSVANQ DDNDHHVIPI EKITLCKELG
QGEFGSVWQA GWKNSAGSDV IQVAVKCVGS DKLLATSSSF LQEAAIMTRM RHEHVVRLYG
VVLDTKKIML VSELATCGSL LECLHKPALR DSFPVHVLCD YAEQIAMGMS YLELQRLIHR
DLAARNVLVF SPKLVKISDF GLSRSLGIGE DYYRSEFTPN LKLPIAWCAP ECINFLKFTS
KSDVWAYGVT IWEMFSYGEM PWKGRSGAQI LELVDRKKEL LTRPKACPED IYDMLKETWT
HQVQDRPTFS DIVAKFPERR AQSVRAVVDC KDSAADHLHF KKDDLIVVIS RSPAQYPDGY
YWFGSLRNGK LGLFRPTDTV AHLGSEPPCS NGTIENGFSE KEKGGKKNKK AEKESERERK
KLLISEPVGD VRHTCHVGID GTAFGLLQLD KKAMCPTSSS PSTSRGSQAS PAPSHTSSST
TSSVHLRETV ARNGVPIKET MSLRDVGPLS RDALNLRDTV SPPVARAPSQ PPSYSQPRPP
PRSVSSVSSG NQHSVQVHDQ FSSLDRSRGS LTPTAPPLTA SAANSLKDPL TGISLSIPSN
NLISYMDDQE DDHRWTRSPG AISQSTTLTA LSSSRKDPIP APRGPVAAVY ARGKDIPTPA
SKSDIALCEK IEDLNRDLTN YSIGTICDYS EDRPLLDSMN RTISSSTTHQ PPPQSSEARI
RFMTEQEVRK INEKSAREHR KTEDLLREER QKEQKPGEIE EPQQPAESLY STRTPQQEGW
SSAAQEAYKL LVECGTNLKQ ASVSPPPMSP TSSRLSTLDR SSISPAPPRP VTPPLSVRNE
TISMRKSQQE EMEHVTVEEN SPKRVHIIET KLIDGPARGM SPIQDRHIPA FTTPMSNGSF
RKAPAPTPVS PAPAGSTDQK PPPCRPPKTR QFPLVIDERN LAYDNLNGFG AGARVAPPVP
PKPKVRTIFS FADDQKKQKE VAN
