ID A0A2Y9DC56_TRIMA Unreviewed; 1139 AA.
AC A0A2Y9DC56;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=LOC101344277 {ECO:0000313|RefSeq:XP_004371917.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004371917.1};
RN [1] {ECO:0000313|RefSeq:XP_004371917.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_004371917.1; XM_004371860.1.
DR AlphaFoldDB; A0A2Y9DC56; -.
DR STRING; 127582.A0A2Y9DC56; -.
DR GeneID; 101344277; -.
DR KEGG; tmu:101344277; -.
DR InParanoid; A0A2Y9DC56; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00063; FN3; 3.
DR CDD; cd05089; PTKc_Tie1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
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 PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF341; TYROSINE-PROTEIN KINASE RECEPTOR TIE-1; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
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:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|RefSeq:XP_004371917.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_004371917.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1139
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016175587"
FT TRANSMEM 762..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..257
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 312..346
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 447..546
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 549..643
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 647..740
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 840..1119
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 871
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 247..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 336..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1139 AA; 125590 MW; 40AF2FF0D06520EC CRC64;
MVWQGPPLLL PILFLASHVG AAVDLTLLAD LRLTDPQRFF LTCVSGEAGA GRGSDAWDPP
LLLEKEDRIV RTFPPRKPLQ DIHNGSHQVT LRGFSQPSDL VGVFSCVGGA RTRRTRVVYV
HNNPRAHLLP EKVTHTVNKG DTAVLSAHVR KEKQTDVIWK SNGSYFYTLD WHEAQDGQFL
LQLPNVQPSS SGIYSATYLE TSPLGSAFFR LIVRGCGAGH WGPDCAKECP GCLHGGVCHD
QDGECVCPPG FTGTRCEQAC REGRFGQSCQ EQCPGTSGCR GLTFCLPDPY GCSCGSGWRG
IQCQDACAPG HFGADCRLQC QCQNGGTCDR FSGCVCPSGW HGVHCEKSDR IPQILDVTSE
LEFNLEAMPR INCAAAGNPF PVRGSMELRK PDGTVLLSTK AIVEPDRTTA EFEVPRLTLE
DSGLWECRVS TSGGQDSRRF RVNVKVPPVP LTAPRLLAKQ SRQLVVSPLV LFSGDGPISS
VRLHYRPQHS TMAWSTIVVD PSENVTLMNL RPKTGYSVRV QLSRPGEKGE GAWGPPTLMT
TDCPEPSVQP WLEGWHVEGP DRLRVSWSLP SVPGPLVGDG FLLRLWDGAR GQERRENVSS
PQARTALLAG LTPGTHYQLD VRLYHCTLLG PASPPARVLL PPSGPPAPRH LRAQALSDSE
IQLMWQRPEG SSGPISKYIV EVQVAGGSGD PMWIDVDRPE ETSTIIHGLN ASTCYLFRVR
ASVQGPGDWS NVVEESTLGN GLQSEGPVQE SRAAEESLDQ QLILAIMGSV SATCLTILAA
LLALVCIRRS CLHRRRTFTY QSGSGEETIL QFSSGTLTLT RRPKPQPEPL SYPVLEWEDI
TFEDLIGEGN FGQVIRAMIK KDGLKMNAAI KMLKEYASEN DHRDFAGELE VLCKLGHHPN
IINLLGACEN RGYLYIAIEY APYGNLLDFL RKSRVLETDP AFAREHGTAS TLSSRQLLRF
ASDAANGMQY LSEKQFIHRD LAARNVLVGE NLASKIADFG LSRGEEVYVK KTMGRLPVRW
MAIESLNYSV YTTKSDVWSF GVLLWEIVSL GGTPYCGMTC AELYEKLPQG YRMEQPRNCD
DEVYELMRQC WRDRPYERPP FAQIALQLGR MLEARKAYVN MSLFENFTYA GIDATAEEA
//
