ID A0A1D2N0X5_ORCCI Unreviewed; 878 AA.
AC A0A1D2N0X5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=Ocin01_07785 {ECO:0000313|EMBL:ODM98888.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM98888.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM98888.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM98888.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM98888.1}.
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DR EMBL; LJIJ01000313; ODM98888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2N0X5; -.
DR OMA; DVQVFSH; -.
DR OrthoDB; 2999496at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:UniProt.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF579; TYROSINE-PROTEIN KINASE ABL-LIKE PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|RuleBase:RU000312, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 379..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..140
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 565..839
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 332..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 878 AA; 99165 MW; 8D87D00F2453F4F7 CRC64;
MKKKEIYCLG KAIKVNGVRM ELQGGAWCPR NMITSETEEW LQIDLHNVHL ITATETQGRF
GNGQGQEYAE FYKISYWRPE LNNWIRYRDH TGNEVMKGNI NTYLAEKSEL NPPIYASKLR
IIPFSRHRRT VCMRSEVYGC IYKGGLVSYS MPQGSMRGEN WNFYDHTYDG IWDGNHLQNG
LGSLADGRVG PNNFKDDFYT HERGKGWVGW KNDTSKNGSE SVEIIFKFTS PQEFFAMHIH
TSNQFTKEVQ VFSEARVFFS ANGKVFSGDS IVVKQKEDCI FEEPRNITIK LHRRVAQYIK
LQLFWAAKWI LISEVTFDAR PVGSQRVVHS GISTTSSEDG SLAQSDASGS GASNTLSRET
PPMAGPPALS HSKWSPATII ITAVISSVLA IIIILTILLT VILVRRRVLG SRKVPKTPEG
TLPFDNSNDF GYASPDEIRK YKISTSDYTE PFTTAPVAAA PPPLTTFPRS SFNPSTTGGD
SGVGSKRMAD YYICTLIPNA TQPTVADSSN EYEYAVPNEL GKLLPSQQPS PLKSIPNSPA
TANRTRMMLL KFKELGIPEI QKHRLRMLRK LGDGTFGSVF VGELDQSGIA EKQLVAVKHL
LRNATDKDKS DFLEEVRLLW TLRDPNIVQV LGIYVEEDPL SVVLEFLELG DLCQFLRQND
TLLPNSTKKI SFGSLLHIAS QISSGMKFLE SRNIVHRDLA ARNCVVGRGL LVKVSHFAKD
TDLYATDYYR LDGKMPLPIR WMAWESLFLG KYSTKTDVFS FGILFWEILT YCRHSPYPTF
SNQEVLNNLR RLSVVEDLDP FEPLSKPQSC PRDIYQLMCD TWSRNDDNRP TFWEINSFLS
RKNLHFTTHG TISHESYKNS SHVLPTSSSL SGAEHYMV
//
