PGFRA_RAT
ID PGFRA_RAT Reviewed; 1088 AA.
AC P20786;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Platelet-derived growth factor receptor alpha;
DE Short=PDGF-R-alpha;
DE Short=PDGFR-alpha;
DE EC=2.7.10.1;
DE AltName: Full=Alpha platelet-derived growth factor receptor;
DE AltName: Full=Alpha-type platelet-derived growth factor receptor;
DE AltName: Full=CD140 antigen-like family member A;
DE AltName: Full=Platelet-derived growth factor alpha receptor;
DE AltName: CD_antigen=CD140a;
DE Flags: Precursor;
GN Name=Pdgfra;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2157969; DOI=10.1128/mcb.10.5.2237-2246.1990;
RA Lee K.H., Bowen-Pope D.F., Reed R.R.;
RT "Isolation and characterization of the alpha platelet-derived growth factor
RT receptor from rat olfactory epithelium.";
RL Mol. Cell. Biol. 10:2237-2246(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-524.
RX PubMed=8318539; DOI=10.1016/0167-4781(93)90127-y;
RA Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
RT "Conservation in sequence and affinity of human and rodent PDGF ligands and
RT receptors.";
RL Biochim. Biophys. Acta 1173:294-302(1993).
RN [3]
RP PROTEIN SEQUENCE OF 833-840, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for PDGFA, PDGFB and PDGFC and plays an essential role in the
CC regulation of embryonic development, cell proliferation, survival and
CC chemotaxis. Depending on the context, promotes or inhibits cell
CC proliferation and cell migration. Plays an important role in the
CC differentiation of bone marrow-derived mesenchymal stem cells. Required
CC for normal skeleton development and cephalic closure during embryonic
CC development. Required for normal development of the mucosa lining the
CC gastrointestinal tract, and for recruitment of mesenchymal cells and
CC normal development of intestinal villi. Plays a role in cell migration
CC and chemotaxis in wound healing. Plays a role in platelet activation,
CC secretion of agonists from platelet granules, and in thrombin-induced
CC platelet aggregation. Binding of its cognate ligands - homodimeric
CC PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFC -leads to the activation of several signaling
CC cascades; the response depends on the nature of the bound ligand and is
CC modulated by the formation of heterodimers between PDGFRA and PDGFRB.
CC Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to
CC the production of the cellular signaling molecules diacylglycerol and
CC inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the
CC activation of protein kinase C. Phosphorylates PIK3R1, the regulatory
CC subunit of phosphatidylinositol 3-kinase, and thereby mediates
CC activation of the AKT1 signaling pathway. Mediates activation of HRAS
CC and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes
CC activation of STAT family members STAT1, STAT3 and STAT5A and/or
CC STAT5B. Receptor signaling is down-regulated by protein phosphatases
CC that dephosphorylate the receptor and its down-stream effectors, and by
CC rapid internalization of the activated receptor (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. Binding of PDGFA and/or PDGFB leads to dimerization
CC and activation by autophosphorylation on tyrosine residues. Inhibited
CC by imatinib, nilotinib and sorafenib (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with
CC heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound
CC ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to
CC receptor dimerization, where both PDGFRA homodimers and heterodimers
CC with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB
CC (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2
CC domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain).
CC Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine
CC phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine
CC phosphorylated) with CRK, GRB2 and GRB7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16234};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16234}.
CC Cell projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P26618}.
CC -!- PTM: Ubiquitinated, leading to its internalization and degradation.
CC {ECO:0000250|UniProtKB:P26618}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-730 and Tyr-741 is important for interaction
CC with PIK3R1. Phosphorylation at Tyr-719 and Tyr-753 is important for
CC interaction with PTPN11. Phosphorylation at Tyr-761 is important for
CC interaction with CRK. Phosphorylation at Tyr-571 and Tyr-573 is
CC important for interaction with SRC and SRC family members.
CC Phosphorylation at Tyr-987 and Tyr-1017 is important for interaction
CC with PLCG1 (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M63837; AAA40743.1; ALT_INIT; mRNA.
DR EMBL; Z14118; CAA78488.1; -; mRNA.
DR PIR; A34710; PFRTGA.
DR RefSeq; NP_036934.1; NM_012802.1.
DR AlphaFoldDB; P20786; -.
DR SMR; P20786; -.
DR BioGRID; 247307; 1.
DR IntAct; P20786; 1.
DR MINT; P20786; -.
DR STRING; 10116.ENSRNOP00000003077; -.
DR ChEMBL; CHEMBL2111344; -.
DR GlyGen; P20786; 7 sites.
DR iPTMnet; P20786; -.
DR PhosphoSitePlus; P20786; -.
DR jPOST; P20786; -.
DR PaxDb; P20786; -.
DR PRIDE; P20786; -.
DR GeneID; 25267; -.
DR KEGG; rno:25267; -.
DR UCSC; RGD:3284; rat.
DR CTD; 5156; -.
DR RGD; 3284; Pdgfra.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P20786; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P20786; -.
DR BRENDA; 2.7.10.1; 5301.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:P20786; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:RGD.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:RGD.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; IEP:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060437; P:lung growth; IMP:RGD.
DR GO; GO:0001553; P:luteinization; ISS:UniProtKB.
DR GO; GO:0030539; P:male genitalia development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; ISO:RGD.
DR GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; ISO:RGD.
DR GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:1904404; P:response to formaldehyde; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027290; PDGFRA.
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 Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Chemotaxis;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Immunoglobulin domain; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..23
FT CHAIN 24..1088
FT /note="Platelet-derived growth factor receptor alpha"
FT /id="PRO_0000016762"
FT TOPO_DOM 24..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..200
FT /note="Ig-like C2-type 2"
FT DOMAIN 201..305
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..409
FT /note="Ig-like C2-type 4"
FT DOMAIN 413..516
FT /note="Ig-like C2-type 5"
FT DOMAIN 592..953
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1017..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 598..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 MOD_RES 571
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 573
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 719
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 730
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 741
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 753
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 761
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 767
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 848
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 987
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 1017
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 434..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 150
FT /note="L -> R (in Ref. 2; CAA78488)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="S -> T (in Ref. 2; CAA78488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1088 AA; 122642 MW; 590C8BB0418801E7 CRC64;
MGTSQAFLVL SCLLTGPSLI VCQLLLPSIL PNENEKIVPL SSSFSLRCFG ESEVSWQHPM
SEEEDPNVEI RTEENNSSLF VTVLEVVNAS AAHTGWYTCY YNHTQTEESE IEGRHIYIYV
PDPDMAFVPL GMTDSLVIVE EDDSAIIPCL TTDPDTEVTL HNNGRLVPAS YDSRQGFNGT
FSVGPYICEA TVRGRTFKTS EFNVYALKAT SELNLEMDTR QTVYKAGETI VVTCAVFNNE
VVDLQWTYPG EVRNKGITML EEIKLPSIKL VYTLTVPKAT VKDSGDYECA ARQATKEVKE
MKTVTISVHE KGFVQIRPTF GHLETVNLHQ VREFVVEVQA YPTPRISWLK DNLTLIENLT
EITTDVQRSQ ETRYQSKLKL IRAKEEDSGH YTIIVQNDDD MKSYTFELST LVPASILELV
DDHHGSGGGQ TVRCTAEGTP LPNIEWMICK DIKKCNNDTS WTVLASNVSN IITEFHQRGR
STVEGRVSFA KVEETIAVRC LAKNDLGIGN RELKLVAPSL RSELTVAAAV LVLLVIVIVS
LIVLVVIWKQ KPRYEIRWRV IESISPDGHE YIYVDPMQLP YDSRWEFPRD GLVLGRILGS
GAFGKVVEGT AYGLSRSQPV MKVAVKMLKP TARSSEKQAL MSELKIMTHL GPHLNIVNLL
GACTKSGPIY IITEYCFYGD LVNYLHKNRD SFMSRHPEKP KKDLDIFGLN PADESTRSYV
ILSFENNGDY VDMKQADTTQ YVPMLERKEV SKYSDIQRSL YDRPASYKKK SMLDSEAKNL
LSDDDSEGLT LLDLLSFTYQ VARGMEFLAS KNCVHRDLAA RNVLLAQGKI VKICDFGLAR
DIMHDSNYVS KGSTFLPVKW MAPESIFDNL YTTLSDVWSY GVLLWEIFSL GGTPYPGMMV
DSTFYNKIKS GYRMAKPDHA TSEVYEIMVQ CWNSEPEKRP SFYHLSEIVE NLLPGQYKKS
YEKIHLDFLK SDHPAVARMR VDSDNAYIGV TYKNEEDKLK EWEGGLDEQR LSADSGYIIP
LPDIDPVPEE EDLGKRNRHS SQTSEESAIE TGSSSSTFIK REDETIEDID MMDDIGIDSS
DLVEDSFL
