ID A0A498NSW5_LABRO Unreviewed; 1748 AA.
AC A0A498NSW5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=ROHU_014744 {ECO:0000313|EMBL:RXN34659.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN34659.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN34659.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN34659.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN34659.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:RXN34659.1}.
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DR EMBL; QBIY01011170; RXN34659.1; -; Genomic_DNA.
DR STRING; 84645.A0A498NSW5; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00096; Ig; 1.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd05054; PTKc_VEGFR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR InterPro; IPR041348; VEGFR-2_TMD.
DR InterPro; IPR009135; VEGFR1_rcpt.
DR PANTHER; PTHR24416:SF616; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR PRINTS; PR01833; VEGFRECEPTR1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498NSW5};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 1..117
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 122..230
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 314..552
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 737..838
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 939..1062
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1078..1164
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1169..1255
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1336..1652
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1439..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 242..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 254..269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1748 AA; 194658 MW; 74AA0303E81A210D CRC64;
MSFDLYAKYG NNRTLSLVSP KKPYYQWRLR VPSGHVVRLV VLTLQGATPG SCSANKLSAY
DFLLPLQNKI IARWCGLPIS GTSPVMKLTS SGNVMLVTFS FSRQRQGAIF KAYFQAIPKT
ECGGFLTAWN GTVTSPYYPA YYPPNVDCNW KIRAPLPGYL LSVTIVMLDI QDSPASSTCE
KDWLEIGGVK LCNPIGDSSR KRIYSSPVLL HFHSDESLTH KGFYLIYRAF SPESACPRQF
RCGDGKCIPL RKVCDGEKDC SDGRDEAKCN TCKQGEVFCM GQCRPHNQCN IACGDSSEEN
NCGCGTRPRK RAKIVGGTDA QTGSWPWQVS LQMERYGHVC GASLVASRWL VSAAHCFQDS
DAIKYSDVRS WRAYMGMRVM NSVSNAAATR QIRRIVLHAQ YDQFTSDYDI ALLELSAPVF
FNELVQPVCV PAASHAFTSG TSCFVTGWGV LSEEGELATL LQEATVSIIG HNACNKMYDD
AVTPRMLCAG NIQGGVDACQ GDSGGPLVCL ERGRRWFLAG IVSWGEGCAR QNRPGVYTRV
IKFTDWIHQQ TKGQDCKGGI SSDSVGFTAI RGRWELQWVL PSGVPKVYHG TQIEDTRCGK
KNNQYCSRLT LSPALAQHTG SYRCRYHQKQ RKQASVYVYV TDSQQPFVKV QTEIPDVVYM
KEGEPLVFPC RVTNPDAKVS LVKFPFHRLT PDYRNIIWNS RQGFTIRSPT FFYIGLFSCE
TIVNGVKHSN KFLTHRPVNK ILDVYLNSTG LVHTLQGQML ALNCTVTAEW NARVSISWTY
PQKANGSATI IRRISKSRTN MLFYSVLTIP RLSKADRGLY KCHVTSGPSK RETNTTVIVY
DHPFIRLKHR DGPVVQASAG QKFFRLTPKL RAFPAPEIIW LKDGMVAAER CSRYHVDGFS
LVIRDIAEED AGIYTIRTGI QQYGLFQNLT LTLVVNVKPQ IGEKTVSSQH PATVQRGSRK
ALHCTSHGVP PPQIQWLWHP CPPKGLCEKP PPSSWTAVSE KTEVTSTHNP ILTVSHRQEV
LEGKNKTVGV LTVGEALKSG IYRCVASNLM GRDELDIHFY VTDVKGGLIV SLEEEPREGG
DLRLVCIANR HLYSDLSWYR LTNQSTASEG ASVLSGELTE GQFSHTLHLL LKNVTAQDSG
TYRCSATHLL TEEHSHLDTA VEVTVLQAPV LLQNLSDHSV NVSNSVTLRC PSRGIPHPRI
TWYKDQRKLQ QVSGIMLFPE EGTLHIDRIT AEDQGLYTCK ANNERGSVES SAHIWVQSSS
ESLSLEIPTL ACTCVVATLF WLLLTLLIRK LKQPTSTNGK AEYLPIILHP GEEPLVEHCD
RLQYDPAQWE FPRDRLKLEK PLGRGAFGRV MQASAFGICN SASCTTVAVK MLKDGATPSE
HKALMTELKI LNHIGHHLNV VNLLGACTKQ GGPLMVIVEY CKFGNLSAYL KSKREVNREE
EGGMKEGYKG RLASVSSSQS NASSGFSEEK GEISEEDSGS LPESNNPLLL EDLISYSFQV
ARGMEFLASR KCIHRDLAAR NILLSNNNVV KICDFGLARD VYKDPDYVRK GDARLPLKWM
APESIFDKVF TTQSDVWSYG VLLWEIFSLG ASPYPGLNID EEFCHRLKQG TRMCPPEYST
PEIYSIMMAC WENNPEDRPS FSALVEILGD LLQTCVQQDG KDYIPLNAFI SGEGNTVTAH
LDQKDISQKT LGTSSYINSG KIKAISTFED LHKEVPDDNQ SDSGMVLPSE ELIQVKWMDR
FKTKNITK
//
