ID M3XI74_LATCH Unreviewed; 1379 AA.
AC M3XI74;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Hepatocyte growth factor receptor {ECO:0000256|ARBA:ARBA00019839};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=HGF/SF receptor {ECO:0000256|ARBA:ARBA00033136};
DE AltName: Full=Proto-oncogene c-Met {ECO:0000256|ARBA:ARBA00033117};
DE AltName: Full=Scatter factor receptor {ECO:0000256|ARBA:ARBA00030820};
DE AltName: Full=Tyrosine-protein kinase Met {ECO:0000256|ARBA:ARBA00033031};
GN Name=MET {ECO:0000313|Ensembl:ENSLACP00000022430.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022430.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022430.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; AFYH01075731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005996741.1; XM_005996679.2.
DR Ensembl; ENSLACT00000026536.1; ENSLACP00000022430.1; ENSLACG00000013435.2.
DR GeneID; 102366006; -.
DR KEGG; lcm:102366006; -.
DR CTD; 4233; -.
DR GeneTree; ENSGT00940000158022; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000013435; Expressed in pectoral fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd05058; PTKc_Met_Ron; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625:SF61; HEPATOCYTE GROWTH FACTOR RECEPTOR; 1.
DR PANTHER; PTHR22625; PLEXIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000617-
KW 2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000617-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000617-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1379
FT /note="Hepatocyte growth factor receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004043724"
FT TRANSMEM 931..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..515
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1076..1343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 1202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1082..1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1155..1158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1232
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1233
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1347
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1354
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT DISULFID 97..100
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 134..142
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 298..363
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 520..538
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 526..561
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 529..545
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 541..551
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ SEQUENCE 1379 AA; 153817 MW; 53FD41ED77CF15EE CRC64;
MKHLFLYSIW QLGLLWSLVQ KGHGQCEEAA NGPEMNLNVA YDLFNFLAEE PIQNVVIHNK
YVYVGAVNRI YSLTENLEKL FEYKTGPILE GSDCLPCEGC SKHKGNSTVI GVWKDNVNMA
LLLETFYEDQ LISCGSANQG VCQRHVLHPD NFANISAHVS CLYSSQVDKS QNYADYVISP
LGTKVLAITR DKLVKFFVGN TVNSSLQQSN LHSVSVRTLK EMQNGFEFPS DRSYMDVITT
MKNSYPIKYI YAFESNSFVY FLTVQGESPD SQAFHTRIIR VCSSDNEMRS YVEMPFECIF
TEKRRKRAIK TDTFNILQAA HVSKPGAALA KEMGIAPDED VLFGVFSQSK LDSPEPTKTS
AVCAVGIKTI NELFNKRIEE CNTKHIYHFD NKDSKFCLNK ARSNDAKYCG EKSEEYRMEI
TIPFQRLDLF MGMFSNVLLT SVAVFTQGKL TVANLGTSEG RVMQVVISRT VQKKPHVNFQ
LHLDPVSPQV AIGRPSEHDG YALVITGKKL TKVPLSGPGC DHFKSCSKCL TAPDFMQCGW
CSNQCSRQQE CVNREWIPNT CPPTVFKLSP STAPLEGGTR VSICGLDFGF KKTGRFELTQ
IGVVIGERTC KLETKNCTKN RLICIVGASN STSNVSFKVS NGNRSSQMHV FSYKNPEVTS
ISPAYGPKSG GTILTLTGKY LDIGNLREVS VGRKVCILKR LSDTVIECTT PAQSNLDEYP
VKIKIDAAER KADTLFTYKE DPSVVTIQPT NSFFSGGGTI TVHGRNLNSV SSPQMVITLP
QQGKEFKVTC TKRNELQLVC CTTPSLQGLN LVLPFTSKVS FILDGVTTGH FDLSYVGNPM
FEPFQKPKVI TKSSNNKLEI EISGVDSEAV KGEVLKVGNK SCENIQLTSS SIICTVPTEL
LKSNSELNVE WKQANSSILI GKVMVVEDQN FTGLIAGAIC ATGLLLLLLG LFIWFRKRKQ
FKGSEIVRYD GKVHTPHLDR LVSARSVSPT AEMVSSESVD YRTTLPEDQF QTFAQNGLCR
QVQYPHTDLS PILSSGDSDL SSPLLQTNVH IDVSTLNPEL LKEVQHVVIT SDNLLVHFTE
VIGRGHFGCV YHGTLLDNEG RKVHCAVKSL NRITDIEEVA QFLKEGIIMK DFSHPNVLSL
LGICLPSEGS PLVVLPYMKH GDLRNFIRNE SHNPTVKDLI GFGLQVAKGM EYLASKKFVH
RDLAARNCML DDKFTVKVAD FGLARDVYEK EYYSVHNKNG AKLPVKWMAL ESLQTQKFTT
KSDVWSFGVM LWELMTRGTP PYPDISSFDI TVFLLQGRRL LQPEYCPDSL YEVMLKCWHP
KPEMRPTFSD LVSRISTIFS TFIGEHYVLL NATYVNIKCV TPYPPLLSCQ DDLGKDLST
//
