KIT_CANLF
ID KIT_CANLF Reviewed; 979 AA.
AC O97799; Q7YRV7; Q8WN23;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Mast/stem cell growth factor receptor Kit;
DE Short=SCFR;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene c-Kit;
DE AltName: Full=Tyrosine-protein kinase Kit;
DE AltName: CD_antigen=CD117;
DE Flags: Precursor;
GN Name=KIT;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9989791; DOI=10.1046/j.1523-1747.1999.00488.x;
RA Ma Y., Longley B.J., Wang X., Blount J.L., Langley K., Caughey G.H.;
RT "Clustering of activating mutations in c-KIT's juxtamembrane coding region
RT in canine mast cell neoplasms.";
RL J. Invest. Dermatol. 112:165-170(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zemke D., Yuzbasiyan-Gurkan V.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Tsai K.L., Guyon R., Murphy K.E.;
RT "Characterization of an isoform and RH mapping of canine c-kit.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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. In response to KITLG/SCF binding, KIT
CC can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1,
CC SH2B2/APS and CBL. Activates the AKT1 signaling pathway by
CC phosphorylation of PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase. Activated KIT also transmits signals via
CC GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or
CC MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3,
CC STAT5A and STAT5B. Activation of PLCG1 leads to the production of the
CC cellular signaling molecules diacylglycerol and inositol 1,4,5-
CC trisphosphate. KIT signaling is modulated by protein phosphatases, and
CC by rapid internalization and degradation of the receptor. Activated KIT
CC promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and
CC PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and
CC STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II),
CC LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1 (By similarity).
CC {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 -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. KITLG/SCF binding leads to dimerization and activation
CC by autophosphorylation on tyrosine residues. Activity is down-regulated
CC by PRKCA-mediated phosphorylation on serine residues (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer in the absence of bound KITLG/SCF. Homodimer in the
CC presence of bound KITLG/SCF, forming a heterotetramer with two
CC KITLG/SCF molecules. Interacts (via phosphorylated tyrosine residues)
CC with the adapter proteins GRB2 and GRB7 (via SH2 domain), and
CC SH2B2/APS. Interacts (via C-terminus) with MPDZ (via the tenth PDZ
CC domain). Interacts (via phosphorylated tyrosine residues) with PIK3R1
CC and PIK3 catalytic subunit. Interacts (via phosphorylated tyrosine)
CC with CRK (isoform Crk-II), FYN, SHC1 and MATK/CHK (via SH2 domain).
CC Interacts with LYN and FES/FPS. Interacts (via phosphorylated tyrosine
CC residues) with the protein phosphatases PTPN6/SHP-1 (via SH2 domain),
CC PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with PLCG1.
CC Interacts with DOK1 and TEC. Interacts with IL1RAP (independent of
CC stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced
CC interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88
CC (By similarity). {ECO:0000250|UniProtKB:P05532,
CC ECO:0000250|UniProtKB:P10721}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O97799-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O97799-2; Sequence=VSP_020224;
CC -!- PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after
CC autophosphorylation induced by KITLG/SCF binding, leading to
CC internalization and degradation. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding
CC promotes autophosphorylation. Phosphorylated tyrosine residues are
CC important for interaction with specific binding partners (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Numerous proteins are phosphorylated in response to KIT
CC signaling, but it is not evident to determine which are directly
CC phosphorylated by KIT under in vivo conditions. {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; AF044249; AAD02327.1; -; mRNA.
DR EMBL; AF448148; AAL40833.1; -; mRNA.
DR EMBL; AY296484; AAP51178.1; -; mRNA.
DR EMBL; AY313776; AAP76390.1; -; mRNA.
DR RefSeq; NP_001003181.1; NM_001003181.1.
DR RefSeq; XP_005628025.1; XM_005627968.2. [O97799-1]
DR AlphaFoldDB; O97799; -.
DR SMR; O97799; -.
DR STRING; 9612.ENSCAFP00000039467; -.
DR PaxDb; O97799; -.
DR Ensembl; ENSCAFT00030034940; ENSCAFP00030030471; ENSCAFG00030018961. [O97799-2]
DR Ensembl; ENSCAFT00040028950; ENSCAFP00040025147; ENSCAFG00040015724. [O97799-2]
DR Ensembl; ENSCAFT00845021185; ENSCAFP00845016654; ENSCAFG00845011904. [O97799-1]
DR GeneID; 403811; -.
DR KEGG; cfa:403811; -.
DR CTD; 3815; -.
DR VEuPathDB; HostDB:ENSCAFG00845011904; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000155626; -.
DR InParanoid; O97799; -.
DR OMA; KSSAYFN; -.
DR OrthoDB; 236292at2759; -.
DR TreeFam; TF325768; -.
DR BRENDA; 2.7.10.1; 1153.
DR Reactome; R-CFA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CFA-1433557; Signaling by SCF-KIT.
DR Reactome; R-CFA-1433559; Regulation of KIT signaling.
DR Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CFA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Proteomes; UP000002254; Chromosome 13.
DR Bgee; ENSCAFG00000002065; Expressed in bone marrow and 45 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0005020; F:stem cell factor receptor activity; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0048565; P:digestive tract development; ISS:UniProtKB.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0038162; P:erythropoietin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0038093; P:Fc receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0035701; P:hematopoietic stem cell migration; IEA:Ensembl.
DR GO; GO:0002327; P:immature B cell differentiation; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0038109; P:Kit signaling pathway; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0060374; P:mast cell differentiation; ISS:UniProtKB.
DR GO; GO:0070662; P:mast cell proliferation; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0097326; P:melanocyte adhesion; ISS:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB.
DR GO; GO:0097324; P:melanocyte migration; ISS:UniProtKB.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0032765; P:positive regulation of mast cell cytokine production; ISS:UniProtKB.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 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; 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; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500951; SCGF_recepter; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
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 Alternative splicing; ATP-binding; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..979
FT /note="Mast/stem cell growth factor receptor Kit"
FT /id="PRO_0000016751"
FT TOPO_DOM 28..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..114
FT /note="Ig-like C2-type 1"
FT DOMAIN 123..207
FT /note="Ig-like C2-type 2"
FT DOMAIN 214..311
FT /note="Ig-like C2-type 3"
FT DOMAIN 320..413
FT /note="Ig-like C2-type 4"
FT DOMAIN 416..510
FT /note="Ig-like C2-type 5"
FT DOMAIN 592..940
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 571..573
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 795
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 674..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 800
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 813
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 571
FT /note="Interaction with SH2B2/APS"
FT /evidence="ECO:0000250"
FT SITE 939
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000250"
FT SITE 939
FT /note="Interaction with SH2B2/APS"
FT /evidence="ECO:0000250"
FT MOD_RES 550
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 556
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 571
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 573
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 706
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 724
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 733
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 744
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 749
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 826
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 903
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 939
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10721"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 235..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 512..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9989791, ECO:0000303|Ref.3"
FT /id="VSP_020224"
FT CONFLICT 23
FT /note="Q -> R (in Ref. 1; AAD02327)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="E -> Q (in Ref. 1; AAD02327)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="D -> G (in Ref. 1; AAD02327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 109753 MW; 46C30D5DEB8E33D3 CRC64;
MRGARGAWDF LCVLLLLLLL GVQTGSSQPS VSPGEPSLPS IHPAKSELIV SVGDELRLSC
TDPGFVKWTF ETLGQLNENT HNEWITEKAE AGHTGNYTCT NRDGLSRSIY VFVRDPAKLF
LVDLPLYGKE GNDTLVRCPL TDPEVTNYSL RGCEGKPLPK DLTFVADPKA GITIRNVKRE
YHRLCLHCSA DQKGRTVLSK KFTLKVRAAI RAVPVVSVSK TSSLLKEGEA FSVMCFIKDV
SSFVDSMWIK ENSQQTNAQT QSNSWHHGDF NFERQEKLII SSARVNDSGV FMCYANNTFG
SANVTTTLEV VDKGFINIFP MMSTTIFVND GENVDLIVEY EAYPKPEHQQ WIYMNRTFTD
KWEDYPKSDN ESNIRYVSEL HLTRLKGNEG GTYTFQVSNS DVNSSVTFNV YVNTKPEILT
HESLTNGMLQ CVVAGFPEPA VDWYFCPGAE QRCSVPIGPM DVQMQNSSLS PSGKLVVQSS
IDYSAFKHNG TVECRAYNNV GRSSAFFNFA FKGNSKEQIH PHTLFTPLLI GFVIAAGMMC
IIVMILTYKY LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA
GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL GNHMNIVNLL
GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFICSKQEDH GEVALYKNLL HSKESSCSDS
TNEYMDMKPG VSYVVPTKAD KRRSARIGSY IERDVTPAIM EDDELALDLE DLLSFSYQVA
KGMAFLASKN CIHRDLAARN ILLTHGRITK ICDFGLARDI KNDSNYVVKG NARLPVKWMA
PESIFNCVYT FESDVWSYGI FLWELFSLGS SPYPGMPVDS KFYKMIKEGF RMLSPEHAPA
EMYDIMKTCW DADPLKRPTF KQIVQLIEKQ ISDSTNHIYS NLANCSPNPE RPVVDHSVRI
NSVGSSASST QPLLVHEDV
