UniProt: A0A7J8JUN6

Database: UniProt
Entry: A0A7J8JUN6_MOLMO

LinkDB:  A0A7J8JUN6_MOLMO 
Original site:  A0A7J8JUN6_MOLMO

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Ontology (20)   
   GO (20)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (26)   
   InterPro (15)   
   Pfam (3)   
   PROSITE (5)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (49)   

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ID   A0A7J8JUN6_MOLMO        Unreviewed;       973 AA.
AC   A0A7J8JUN6;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   08-OCT-2025, entry version 21.
DE   RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
GN   ORFNames=HJG59_007327 {ECO:0000313|EMBL:KAF6500553.1};
OS   Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC   Molossus.
OX   NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6500553.1, ECO:0000313|Proteomes:UP000550707};
RN   [1] {ECO:0000313|EMBL:KAF6500553.1, ECO:0000313|Proteomes:UP000550707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6500553.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAF6500553.1};
RX   PubMed=32699395;
RA   Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA   Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA   Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA   Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA   Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA   Vernes S.C., Myers E.W., Teeling E.C.;
RT   "Six reference-quality genomes reveal evolution of bat adaptations.";
RL   Nature 583:578-584(2020).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051243,
CC         ECO:0000256|PIRNR:PIRNR500951};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC       protein {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|PIRNR:PIRNR500951, ECO:0000256|RuleBase:RU000311}.
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:KAF6500553.1}.
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DR   EMBL; JACASF010000001; KAF6500553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J8JUN6; -.
DR   OrthoDB; 6077854at2759; -.
DR   Proteomes; UP000550707; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0016477; P:cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-ARBA.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0008406; P:gonad development; IEA:UniProtKB-ARBA.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   GO; GO:0070662; P:mast cell proliferation; IEA:UniProtKB-ARBA.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IEA:UniProtKB-ARBA.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:TreeGrafter.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR   GO; GO:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05860; IgI_4_SCFR; 1.
DR   CDD; cd05104; PTKc_Kit; 1.
DR   FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000422; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000429; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000469; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000544; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000815; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR027263; SCGF_receptor.
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   PANTHER; PTHR24416:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR500951};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500951};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR500951};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500951};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500951};
KW   Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR500951};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   CHAIN           24..973
FT                   /note="Mast/stem cell growth factor receptor"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT                   /id="PRO_5029998863"
FT   TRANSMEM        523..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   DOMAIN          212..309
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          587..934
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        789
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         566
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         594..601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         669..675
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         793
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         794
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         807
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            933
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   973 AA;  108518 MW;  A930FC1EBA0F4C61 CRC64;
     MRGARGAWDF LCVLLLLFGL QTGSSPPSVS PGELSPPSIH PAKSELIVSV GDEIRLLCTD
     PGFVKWTFEI LGRLSEKTHN EWITEKAEAT STGNYTCTNE GGLSSSIYVF VRDPAKLFLM
     DLPLYGKEGN DTLVRCPLTD PEVTNYSLTG CEGKPLPKDL AFVADPKAGI TIRNVKREYH
     RLCLHCSADR KGKPVLSKKF TLKVRAAIRA VPVVSVSKAS YLLREGEEFT VTCSIKDVSS
     SVDSMWIKEN SQHTKAQVQS NSWHQGDFNF VRQERLTIGS ARVNDSGVFM CYANNTFGSA
     NVTTTLEVVD KGFINIIPMA NTTVFVNDGE NVDLTVEYEA YPKPEHQQWI YMNKTFTDKW
     ENYPKSENES NIRYVSELHL TRLKGTEGGT YTFLVSNSDV DSSVTFNVYV NTKPEILTHE
     SLANGMLQCV AAGFPEPTVD WYFCPGAEKQ GCSVPIGPVN VQMQNSSVSP FGKIVVQSSI
     DDSAFKFNGS VECRAYNDVG KSSAFFNFAI KEQIHAHTLF TPLLIGFVIA AGIMCIIVMI
     LTYKYLQKPM YEVQWKVVEE INGNNYVYID PTQLPYDHKW EFPRNRLSFG KTLGAGAFGK
     VVEATAYGLI KSDAAMTVAV KMLKPSAHLT EREALMSELK VLSYLGNHMN IVNLLGACTI
     GGPTLVITEY CCYGDLLNFL RRKRDSFICS KQEDHAEAAL YKNLLHSKDS LGDSGNEYMD
     MKPGVSYVVP TKADKRRSAR IGSYIERDVT PAVMDDDELA LDLEDLLSFS YQVAKGMAFL
     ASKNCIHRDL AARNILLTHG RITKICDFGL ARDIKNDSNY VVKGNARLPV KWMAPESIFN
     CVYTFESDVW SYGIFLWELF SLGSSPYPGM PVDSKFYKMI KEGFRMLSPE HAPAEMYDIM
     KTCWDADPLK RPTFKQVVQL IEKQISDSSN HIYSNLANWS PNQENIVVDH SVRINSVGSS
     ASSTQPLLVH EDA
//

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