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Database: UniProt
Entry: A0A3Q3LNT2_9LABR
LinkDB: A0A3Q3LNT2_9LABR
Original site: A0A3Q3LNT2_9LABR 
ID   A0A3Q3LNT2_9LABR        Unreviewed;      1274 AA.
AC   A0A3Q3LNT2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000010400.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000010400.1}
RP   IDENTIFICATION.
RG   Ensembl;
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,
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}.
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DR   AlphaFoldDB; A0A3Q3LNT2; -.
DR   Ensembl; ENSLBET00000010962.1; ENSLBEP00000010400.1; ENSLBEG00000007923.1.
DR   GeneTree; ENSGT00940000164144; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; 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   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   InterPro; IPR041348; VEGFR-2_TMD.
DR   PANTHER; PTHR24416:SF552; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR   Pfam; PF17988; VEGFR-2_TMD; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
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.
PE   3: Inferred from homology;
KW   Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          180..280
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          388..497
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          507..597
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          610..695
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          774..1104
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1126..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1170..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        968
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         808
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         973
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         986
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1274 AA;  142754 MW;  6A21676D67B5FD5B CRC64;
     SKSTECHYPG LCPLMSLSVS FRGHGLLHWT LADPGRSISS EGVKVEQCDS RHHLNSHCSK
     LTVTKLKAVD TGRYSCLYSK DGLDHINSTY VYVQDEEEPF VEPQNHGVLG IYRHETSLVV
     PCRTSSPDTV VPLLQERMVK EMVWDPEVGF KIPYGPFDMI NILTCKTMVK GRKHESTYMP
     KRLTIVLKNV KVTPERVRVL VGDTLSLNCT GETTYNGRIN FTWDFPNRRD NRHYTTKPKF
     SKAEVLVMSK ALFLPNITMD DKGVYRCRAE LEPTIHRNAS AKVIVYEHPF LNISYRHERP
     STVVVKEGRK RLVFEPKVNA LPTPDMLAWY KDGVPIRKNS TCYKMSGFNL IITDVQQKHT
     GIFTISLGNQ AKGLHRNLTY TLVVNMKPSI SEAELATVDV PPYMFGRQHQ LTCTAFGFPL
     PNITWLWQPC HSGPTLKDCN DTMPILVKVE DRENYTRNMI KGISINPELV KGKNKTVSTL
     VIGEASTSGK YTCLAQNEDG ISKWVIPFYI DDQAEEFTIE PGAAIEGDDV NLTCRAARYL
     YTDLQWLDSK NQTITSNVSS LQLSNYSISI SLHLHNVSQN SAKGYRCRGV KLQKRVELPA
     ALNVDARKRP WLSQNLTNQD VNSSSTLILA CFALGVPRPY ILWYKNGVPV EEGPGITLGE
     DGLLTIERVK KDDEGFYECV ASNVEGMAKT SAVVTVLGDE GKPNVEVIIL VCTGAAATFL
     WLMLIIFIRK LRKQPAHYKM GPSIIIDPDE CPLDEQNDFL QYDSSKWEFP RDRLRLGKTL
     GHGAFGKVVE ASAFGIDKLS TCKTVAVKML KGGATSNERK ALMSELKILI HIGHHLNVVN
     LLGACTKPGG PLMMIVEFCK YGNLSNYLRS KREDFIVYKS QDGKVVSSGS GCELSELMKR
     RLESVASTGS SASSGFIEDK SYCDSEEEEE ESEDLYKRIL TLEDLICYSF QVAKGMEFLA
     SRKCIHRDLA ARNILLSENN VVKICDFGLA RDIYKDPDYV RKGDARLPLK WMAPEAIFDK
     VYTTQSDVWS FGVLMWEIFS LGASPYPGVQ IDEEFCCRLK EGTRMRAPEY SSSEIYQTML
     DCWQGEPQER PTFTELVEML GDLLQASVQQ EGKHYIPINT ALLSKVGDPS STGQSEETST
     RPASHRDSGN NWNIKIRPAS VKTFDEVTME HGTNESHEGG HSDSGMGLSS DNMKTLKRLE
     SLASRPLSIM ALAMKAVSKS KESVLSDTEK EKYSSTIPNL DFSLDDSVLD DSALECHSPP
     PDYNYVVRYS TPPV
//
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