ID A0A0L8GJ90_OCTBM Unreviewed; 1106 AA.
AC A0A0L8GJ90;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=OCBIM_22033156mg {ECO:0000313|EMBL:KOF76595.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF76595.1};
RN [1] {ECO:0000313|EMBL:KOF76595.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF76595.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF76595.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; KQ421737; KOF76595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8GJ90; -.
DR STRING; 37653.A0A0L8GJ90; -.
DR EnsemblMetazoa; Ocbimv22033156m; Ocbimv22033156m.p; Ocbimv22033156m.g.
DR EnsemblMetazoa; XM_014925394.1; XP_014780880.1; LOC106876722.
DR OMA; FFILCTC; -.
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 CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF525; INSULIN-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 993..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..99
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 886..983
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1054..1106
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1088
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1106 AA; 126474 MW; CCAC1CE3D7650326 CRC64;
MRREGCEKNI DLILHDYCPN PTRGPDILCT ATSCLFDGVC KEFENGDKRC TCSHDCSNEP
TSQICGTDHK IYANDCLLRK ESCELQTAIN KTHMDFCELC SSIEIKNKIE NFKQLEHCSV
IEGYLRIILL DYMKPEDYQN MRFPKLVEIT DYLIMYRAYG LKTLRDLFPN LSVIRGQELF
YNYALVAFEM PDLEEIGLSS LTVIQRGAVR FNKSPNLCYL ETIDWTKITS EGSNEAHSIA
DNKDPRECVD QCPHTCDHCW NSRECQKNID CLCENRKGYC QQNGSCCHEN CLGGCRGPTA
RDCLACRHVY HDKECKRTCP PNTYKFKNRR CLTERECRSV AYNFKLLEAN MTTNRTALCT
EHCPVGYIEN PDDPNRCLKC KARCPKKCPA KEVKSISSIQ SLKDCTEITG ELILQHLNGV
LAQELEANLG QIEEVHNFIK ITRSDGLVSL SSFKSLKVIH GKKLEDDRYA LYLRDNENIE
ELFSKDVEKN LVIKRGKVFF HDNRRLCQHK IRELMNYTKL NASNHTEHDI STSNGDLIPC
QTKNLNLTII STASAFAILK WNRFEMDDSR EMLGYVIYYR EVADKNVPLF EKQDLCIDRL
WKTVQKPKDR KEPKDNQEFH VLTELKPWTL YATYLKTDTL STAKSTGMSD VEYFRTTTGV
PTNPTNLKIT AKRVGELIVS WDPPKEPKGE VDHYFVYWQS EVLNVADYSI RDYCENRLKP
TAKQDEKRKP IANDTFNENC CECPKDKKVD KTEESERQMQ IFFENFLHNN VFVKRPPDVS
LSDDSHNRHR REAVIEDPHA AGKYLPAHNN FSRPNASRQS TERPFLAMAV YNSRSVVIGN
LAHFQEYNIE VIACHKSNEN GKYCSNRAIV TAKTLPLEIA DHINSSSVNA TLIVNGTGDM
LISWDPPAYV NGLIVTYEVA YKKAAKKNKD DSIVCITQRE YQITRSCRLQ KLDAGNYSYR
IRATSLAALG NWTEYKFFLV PERPGSPPPL NTIMIVIITL LSVLVTVLIF TTICVRYGIC
SRGKGASYVS VNPEYASARE VYEPDETELD RDMISLIREL GQGSFGMVYE GILFTSGDDE
KGITVAVKTA MSADRHSFLK EATVMK
//
