ID A0A498LGU0_LABRO Unreviewed; 1699 AA.
AC A0A498LGU0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=ROHU_033979 {ECO:0000313|EMBL:RXN04625.1};
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:RXN04625.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN04625.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN04625.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN04625.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:RXN04625.1}.
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DR EMBL; QBIY01013432; RXN04625.1; -; Genomic_DNA.
DR STRING; 84645.A0A498LGU0; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 8.
DR CDD; cd00063; FN3; 3.
DR CDD; cd05043; PTK_Ryk; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.60.40.2170; Wnt, WIF domain; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00469; WIF; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 8.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS50814; WIF; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1699
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019781357"
FT TRANSMEM 1320..1342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..272
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 282..323
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 325..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 360..396
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 428..463
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 511..547
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 550..586
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 614..671
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 671..707
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 712..804
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 805..906
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 907..999
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1103..1139
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1156..1283
FT /note="WIF"
FT /evidence="ECO:0000259|PROSITE:PS50814"
FT DOMAIN 1422..1695
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 997..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 313..322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 386..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 453..462
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 537..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 576..585
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 642..669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 697..706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1699 AA; 188439 MW; 84DF59297DF189AB CRC64;
MGWLRRLVLS TCMLVILLHG VEPAVPLEEF YPFGLDEGDS QTIEQDDGGS GLVAISVAFP
FFGERHNGLY VSIVCMWESV VRENQVNNNG LVSFLREVSQ FTPVAFPIAG DRRVVAPFWA
DVDNRRAGQV FYRESKDPAI LRRANADINR YFPEFPMFIT TWVLIATWHQ VTFFGGSSIT
PVNTFQVVLI TDGELSFTIF QYHNISWTTG MHATSGGDLA GLGGIAAQAG FNAGDGRRYF
NIPGSRTDDI VDVETTTNVG YPGRWVFRID DSQVQVGSCN DSASVCANLR PCQNGGRCID
DCITGNPSFT CSCLAGFTGR RCQIDIDECQ ETPCLNGAQC IQGVGNFTCV CQAGYTGFLY
INECASMPCL NGGVCEDLVN NYTCTCTTNF TGSYCETVPC DGESCEKHQI CEYTDSGNYN
CTCTPGYYGD DCEEECPCQN GGVCVDVNGT CECPTGFTGL YCQFEVTQTP CSNNRPCPDG
GPCLEYGGTY LCTCQTGVDF DHKDFYPYVQ PRSACDSSPC QNGGYCYERD GGYICECKHG
YRGKHCERVR LSICASSPCR NGGSCKEEAD SYRCVCPYRF TGKHCEVGKP DPCASSPCLN
GGTCFHYIGK YKCLDCGLPV KVKHAEVQYS STTPGSMALY ACHPGYTPLP RATQSICSSQ
GSWSQPPVCE EQDGCEPNPC LNGGVCRGYR RNHLCVCKEG YVGDRCQTYL LPPSGLHVLR
VEENEVELRW DQSDATQNLI SGFAVAFAPI GRGPRKTDFL EKQHSTYVLQ GLNPGQLYNI
STFSVKRNTN SNDISQPAFA LIRTRPRKVE QLEVMNVSSS QVWLRWLVHV GRHAAISQVR
VSLVPADGSG ARTAVLNSSV TEYTFSTLLP GQMYTVDVVT QSGLRPEDLP STSKSSGPLH
FWTRPLPPQN LSLSHITTTS ARITWDHHPR SLPDGFVVNI TRGLSTRSRY LPDGSLGTYT
LRDLAPGQHY RLALTAVRKT GQDNIQSVPQ HLAFTTLPVS KGQSRGDRPK GGPDSQIGQT
LTQVQDGGTD DHTELLEEPQ RYTELIDGRG RITAKFTNLP QKTIRHRTKP EPPVKLEKME
ETTNKISLAL EIPEEATKSK SESSQDCRTQ PCQNGGTCAQ TNESFSCNCA AAFKGRRYKR
TYKVQQDVCF REICEPLLPK KVLPKTPSLD AELYYVRDDV VNHYALSFIL PVPSDTNSLH
FTWHSSSKVD YRLGFQVENT SAMDQPQSNI SVQGEVPRSR SVFRVDLFCS GKADGEAVLT
VQLNLTIPAN NFTVLNFKRR KMCYRRIEQP EPPKILPFPN TTIQRIDPSS SNAPTTSTRV
FYISVCVCCI VIFLVAIILA VLHLHSMKRV EMDDSVSDSG SSQGLSQPST QTTQYLRADT
PNNATPVTSY PSLRIEKNDL RSVTLLEAKA KVKDIAISRE RVTLRDVLHE GTFGRIFHGV
LLDEKDPSKE KQVFVKAVKD HASEVQVTMM LTESCKLRGL HHRNLLPISH VCIEDGEKPM
VLLPYMNWGN LKLFLRQCKL AEANNPQAIS QQDLVHMAIQ ISCGMSYLAR REVIHKDLAA
RNCVIDNSMQ VKITDNALAR DLFPMDYHCL GDNENRPVRW MALESLLNND FSSASDVWAF
GVTLWELMTL GQTPYVDIDP FEMAAYLKDG YRIAQPINCP DELFAVMACC WALDPEERPK
FQQLVQCLTE FHAALGAYV
//
