KIT_XENLA
ID KIT_XENLA Reviewed; 954 AA.
AC Q91909;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mast/stem cell growth factor receptor-related protein Kit;
DE EC=2.7.10.1;
DE AltName: Full=Kit-related kinase 1;
DE Short=xKrk1;
DE AltName: Full=Tyrosine-protein kinase kit;
DE Flags: Precursor;
GN Name=kit; Synonyms=krk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=7619732; DOI=10.1016/0925-4773(94)00338-n;
RA Baker C.V.H., Sharpe C.R., Torpey N.P., Heasman J., Wylie C.C.;
RT "A Xenopus c-kit-related receptor tyrosine kinase expressed in migrating
RT stem cells of the lateral line system.";
RL Mech. Dev. 50:217-228(1995).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for the cytokine kitlg/scf and plays an essential role in the
CC regulation of cell survival and proliferation, hematopoiesis, stem cell
CC maintenance, gametogenesis, mast cell development, migration and
CC function, and in melanogenesis. {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in a migratory stem cell population.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, maternal transcripts levels
CC are very low through cleavage and blastula stages. Zygotic transcripts
CC are first detected in the early gastrula at stage 10. Transcripts
CC levels increase through tailbud and tadpole stages. At stages 31/32,
CC expression is seen at the surface of the embryo in a line ventral to
CC the posterior edge of the optic cup. At stages 33/34, two short lines
CC of cells exist running ventrally from the anterior edge of the otic
CC vesicle. At stages 35/36, expression is seen in cells near the cement
CC gland and in a patch of cells located posterior to the gill arches, and
CC just beneath or within the inner layer of the epidermis. At stages
CC 37/38, expression forms a ribbon on either side of the embryo. At
CC stages 40, a second line runs caudally along the flank of the embryo.
CC By stage 42, extension occurs and a line is observed ventro-caudally
CC around the anus. {ECO:0000269|PubMed:7619732}.
CC -!- PTM: Ubiquitinated. Rapidly ubiquitinated after autophosphorylation
CC induced by kitlg/scf binding, leading to internalization and
CC degradation. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues. Phosphorylated tyrosine
CC residues are important for interaction with specific binding partners
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; Z48770; CAA88688.1; -; mRNA.
DR PIR; I51703; I51703.
DR RefSeq; NP_001079048.1; NM_001085579.1.
DR AlphaFoldDB; Q91909; -.
DR SMR; Q91909; -.
DR GeneID; 373579; -.
DR KEGG; xla:373579; -.
DR CTD; 373579; -.
DR Xenbase; XB-GENE-6253062; kit.L.
DR OrthoDB; 236292at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 373579; Expressed in pancreas and 15 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
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:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 5.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500951; SCGF_recepter; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..954
FT /note="Mast/stem cell growth factor receptor-related
FT protein Kit"
FT /id="PRO_0000248274"
FT TOPO_DOM 20..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..109
FT /note="Ig-like C2-type 1"
FT DOMAIN 118..200
FT /note="Ig-like C2-type 2"
FT DOMAIN 207..299
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..401
FT /note="Ig-like C2-type 4"
FT DOMAIN 404..499
FT /note="Ig-like C2-type 5"
FT DOMAIN 577..912
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 776
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 584..591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 780
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 781
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 556
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 558
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 691
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 708
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 807
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 133..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 147..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 228..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 419..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 954 AA; 106860 MW; 9748845CBE0B537D CRC64;
MSWTYLLMLL FLLPYTGDAV PKINDGEDRV TVNVGDKVSL ECRDAHLVTL AFQKSGLMKK
PRDLKSRPLN NSETDQFFVI IKADLRHIGR YICTNTETQE NTSVSLFVKD PARPFLDIPF
IDVTEGADTV GMCFPTDPDM DIAIEKCDGS PLPENFTFTT DIEAGITIKT VQLAFDSCYV
CSGNKSGTVK KSSTFSIHVK PVPKKVPTVF LSKSRQLVKT GEPFEVTCAV LDVFSTVKAQ
WLDVKEGVTK QANFRSSNVF SYNLTLKSDG VPYSESRTFT CQAENAIGQV NATFTLDVID
VGYVNLTVLE NTTISVNAGD NLVLKVYIDA YPHPDDGVWT YFNETLLNTS DHYVATKDEG
NNRYVSELHL IRLKGTEKGV YTFYTTNSDD DASVSFNIQV KTRPEILIAE RTSEGTLQCV
ATGFPVPAIQ WYFCPGSEQR CTDYPPLSPV NEKFIQENSS LGRIVVESTI DVNDLKKNGT
VQCVASNEVE SAYSVFSFAI KEKLRTHTLF TPLLIGFIAA AGLMCIAVAV LMYKYLQKPK
YEIQWKVVEE INGNNYVYID PTQLPYDNKW EFPRDRLCFG KILGAGAFGK VVEATAYGLL
KEDSRLTVAV KMLKPSAHST EREALMSELK VLSYLGHHKN IVNLLGACTV GGPTLVITEY
CCYGDLLNYL RRKRDSFICP KFEDNSEAAL YKNLLNTRDM GCEGMSEYID MKPAVSYVVP
TKTDKRRSGS FGDQDVSVSI PEEDDLALDT EDLINFSYQV AQGMNFLASK NCIHRDLAAR
NILLTHGRIT KICDFGLARD IRNDSNYVVK GNARLPVKWM APESIFHCVY TFESDVWSYG
ILLWEIFSLG SSPYPRIPVD SKFYKMIKDG YRMMSPECAP LEMYEIMRSC WNSDPLKRPT
FKQIVQMVEQ QLSDSKGNTP LPYPVSHVPL DHAVRINSVG SSTSSQPLLT NSDR
