ID A0AAD1SEW2_PELCU Unreviewed; 2594 AA.
AC A0AAD1SEW2;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Mast/stem cell growth factor receptor Kit {ECO:0000256|ARBA:ARBA00014417};
DE EC=1.3.1.22 {ECO:0000256|ARBA:ARBA00012049};
DE EC=1.3.1.94 {ECO:0000256|ARBA:ARBA00012522};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3 {ECO:0000256|ARBA:ARBA00031420};
DE AltName: Full=Polyprenal reductase {ECO:0000256|ARBA:ARBA00047186};
DE AltName: Full=Proto-oncogene c-Kit {ECO:0000256|ARBA:ARBA00032530};
DE AltName: Full=Steroid 5-alpha-reductase 3 {ECO:0000256|ARBA:ARBA00030858};
DE AltName: Full=Tyrosine-protein kinase Kit {ECO:0000256|ARBA:ARBA00032147};
GN ORFNames=PECUL_23A025471 {ECO:0000313|EMBL:CAH2300213.1};
OS Pelobates cultripes (Western spadefoot toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Pelobatidae; Pelobates.
OX NCBI_TaxID=61616 {ECO:0000313|EMBL:CAH2300213.1, ECO:0000313|Proteomes:UP001295444};
RN [1] {ECO:0000313|EMBL:CAH2300213.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a key role in early steps of protein N-linked
CC glycosylation by being involved in the conversion of polyprenol into
CC dolichol. Acts as a polyprenal reductase that mediates the reduction of
CC polyprenal into dolichal in a NADP-dependent mechanism. Dolichols are
CC required for the synthesis of dolichol-linked monosaccharides and the
CC oligosaccharide precursor used for N-glycosylation. Also able to
CC convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT).
CC {ECO:0000256|ARBA:ARBA00045898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = testosterone
CC + NADPH + H(+); Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00049397};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC Evidence={ECO:0000256|ARBA:ARBA00049397};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC NADPH + H(+); Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00048765};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC Evidence={ECO:0000256|ARBA:ARBA00048765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a di-trans,poly-cis-dolichal + NADP(+) = a di-trans,poly-cis-
CC polyprenal + NADPH + H(+); Xref=Rhea:RHEA:80727, Rhea:RHEA-
CC COMP:19536, Rhea:RHEA-COMP:19537, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:231623,
CC ChEBI:CHEBI:231637; EC=1.3.1.94;
CC Evidence={ECO:0000256|ARBA:ARBA00049427};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:80729;
CC Evidence={ECO:0000256|ARBA:ARBA00049427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-4-ene-3,17-dione + NADPH + H(+) = 5alpha-
CC androstan-3,17-dione + NADP(+); Xref=Rhea:RHEA:50816,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00048095};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC Evidence={ECO:0000256|ARBA:ARBA00048095};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU000311}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenal
CC reductase subfamily. {ECO:0000256|ARBA:ARBA00046320}.
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DR EMBL; OW240917; CAH2300213.1; -; Genomic_DNA.
DR Proteomes; UP001295444; Chromosome 06.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0047751; F:3-oxo-5-alpha-steroid 4-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0160198; F:polyprenal reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:UniProtKB-ARBA.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:TreeGrafter.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR GO; GO:0016095; P:polyprenol catabolic process; IEA:UniProtKB-ARBA.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:TreeGrafter.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05104; PTKc_Kit; 1.
DR FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.20.120.1630:FF:000021; Polyprenol reductase 1; 1.
DR FunFam; 1.10.510.10:FF:000077; Vascular endothelial growth factor receptor 2; 1.
DR FunFam; 2.60.40.10:FF:000532; Vascular endothelial growth factor receptor 2; 1.
DR FunFam; 3.30.200.20:FF:000041; Vascular endothelial growth factor receptor 2; 1.
DR FunFam; 2.60.40.10:FF:000143; Vascular endothelial growth factor receptor 3; 1.
DR FunFam; 2.60.40.10:FF:000411; Vascular endothelial growth factor receptor 3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 12.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
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; 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 InterPro; IPR041348; VEGFR-2_TMD.
DR InterPro; IPR055229; VEGFR1-3_5th.
DR InterPro; IPR055238; VEGFR1-3_N_Ig-like.
DR InterPro; IPR009136; VEGFR2_rcpt.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF45; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF22971; Ig_VEGFR-1-like_5th; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF02544; Steroid_dh; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR Pfam; PF22854; VEGFR1-3_N_Ig-like; 1.
DR PIRSF; PIRSF500951; SCGF_recepter; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR PRINTS; PR01834; VEGFRECEPTR2.
DR SMART; SM00409; IG; 12.
DR SMART; SM00408; IGc2; 7.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 11.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50835; IG_LIKE; 8.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 2.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 2.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000615-3}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP001295444};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2594
FT /note="Mast/stem cell growth factor receptor Kit"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042098234"
FT TRANSMEM 513..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1729..1750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2353..2373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2438..2459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2471..2489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2536..2561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..301
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 408..498
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 581..925
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1001..1084
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1177..1282
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1291..1377
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1384..1445
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1488..1617
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1631..1719
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1798..2125
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1929..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2245..2275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1939
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2248..2269
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 780
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 588..595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 663..669
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2594 AA; 291709 MW; F89CA64CDC336D86 CRC64;
MDWGFLSLLL LLSYHTDKGD AVPSVSNFED PKTILAGQRI QFICKDTEAV SWSYLRPGYG
KKPKQLRTSP FHGSKTDLLY TIERAERKHT GRYICTNTLT EESVSFYLFV KDSTSPFYDD
LKFLDGQEGS DVTGICPRSD PDALDFALQT CDKSPMPKDF IYVVDFENGI TIKTVQTNFK
GCYECTASQN GIVKTSKFTL HVKPVHKTLP TISLTKSRQL VKTGEPFQVT CAVKDVFSTV
EVRWVNHQNM VVSENSQYLA PTVFGRNVTL KSNAVQFNES GTFICQAKNS IGSVNVTFTL
DVIDVGFINL TITDNTTIDV NAGESLVLRV FIDAYPRPYE ELWTFMNETI LNTSDHFVDT
REEGDNRYIS ELHLIRLKGN EKGDYTFYIS NADSNSSVTF SVFVKTRPEI LTAERISDDM
LQCVAAGFPT PTIDWFFCSG SEQRCQNASS ISPVDLKISQ ENSSLGRIVV ESTINVSSIK
KNGTVQCIAS NEVQRTSSVF SLAIKENISS HTLFTPLLIG FIVAAALMCV LVAILMYKYI
QKPKYEIQWK VVEEINGNNY VYIDPTQLPY DNKWEFPRDR LCFGKILGAG AFGKVVEATA
YGLLKADTTL TVAVKMLKPS AHSTEREALM SELKVLSYLG HHKNIVNLLG ACTIGGPTLV
ITEYCCYGDL LNFLRRKRDS FICPKFEEHS DTALYKNLLN SRDHICDGMS EYMDMKPGVS
YVVPAKTGKR RSGSYVDQDV TIAMPEEDDL ALDTEDLISF SFQVAQGMNF LASKNCIHRD
LAARNILLTN GRITKICDFG LARDIKNDSN YVVKGNARLP VKWMAPESIF HCVYTFESDV
WSYGILLWEI FSLGSSPYPR IPVDSKFYKM IKDGYRMLSP ECAPAELYEI MKGCWNSDPL
KRPTFKQIVQ KIEQQLSDGK GHTLLNTSPL ISNQIPLDHS VRINSIGSTT SSTQPLLPQD
FNKEHSQRLI HVTHIMVSGL GALKLSPALA VKTSGFSADV PSLSTETDNL VIAVNDTLNV
TCRGEQPLVW LWPTNLSIAD ERVSVSQCKE SVYCQTLTLS NVATNDTGIY KCFYEDSNAT
SSVHVYVLDK RSPFLSSDQL TALYITENKM ATIPCLASRP DLNVTLHAKY SDAVFHPDGD
SMYWDYRKGF TILSELIKSA SLVFCETKLN GEVYISPDYL VLVIGFKIDS VTMSPHPVVK
LAVGETLLLT CTARTPLNTR VNFKWGYPAT VEDVQERNGK RKEVQGRLEH PGHLVINYVT
MKDEGVYNCT VYTGSTVQET ISTRVIVYEN PFVHIDDKMP PVVVTKVGRH VRVPVQFKSY
PAPEIKWFKN GNSVHPKYVA KGGHLLSIAD VSEKDAGNYT VVLTNPDTRQ HKSHTFRLDV
HVPPHIGEKS VSAPVEPYKF GKPYVLTCTA SGIPAPVSIQ WVWQLEEECS FSFEKSDSGS
SQYTCAEWRD ISDKNGGNVI VANETHTDVI EGKVKTVSKL VIKAANIPAV YKCSARNEAG
EDHRVISFHV TRGLDTTRLP QGHLVQQDNV TLRCFADKLT YENLTWYKLS PKTAEKHIRY
WPMPLCRNLN ALLKITGTVI STNGENATAE LIIPNISFKD QGNYVCVAQD KKTQKIYCSI
MPIIVQALKA PGINPQLENQ TMNVSQTVEV KCQASGIPEP QITWFKNGDS LVGDSGIILK
DKNSTLTIQR VRKQDEGFYA CRACNLLGCD KAEMYFTVND TEEKTNLELI ILVGTGVIAL
FFWLLLVIIL RTVKRPSEEE LKSNYLSIIM DPSEVPLDEQ CERLLYDASK WEFPRDRLKL
GKPLGRGAFG QVLEADAFGI DTSGSCKTVA VKMLKEGATN SEYKALMSEL KILSHIGHHL
NVVNLLGACT KPGGPLMVIV EYCRFGNLSA YLRSKRKEFL PYKTRPTRCR SIKQHYVELP
GDLKRRLDSI GSSQSSASSG FVEEKSLSDV EEEEVEDACK NTLSLEDLIS YSFQVARGME
YMASRKCIHR DLAARNILLA DNNVVKICDF GLARDIYKDP DYVRKGDARL PLKWMAPETI
FDRVYTTQSD VWSFGVLLWE IFSLGASPYP GVQIDEVFCR RLKEGTRMRA PDYATAEIYQ
TMLDCWHGNP LERPNFSELV EHLGNVLQVS VQQNFPERQH GKDYIPITDS LNIEEDSGLS
MPTSPVSCKE EEEISNAKFH HDSAVGIRLQ QNVKRKSRPV SVKTFEDVPV EPAAKSIHDT
DSGMVLASEE LKILGNDQAQ FFSKSKESVT SGSSNQTSDY QSGYQSGYSD DTEIVSDSNE
KTQLLRRDLS PDTCYLEGVS PAGYQLLGRL SLHRMGSRTL LCNVFQDAIR YGKTKTGLQR
PAWLHWLDIP KRWFYHFYIV SIFWNGVLLW LLVRTWLLGF ETPEWIKSVH YFIREDSQQT
SGEELSTMLA LSLIWLHSVQ RLVECLFVSV FSSGVIHLAQ YCFGLVYYLL VGITILSYSR
LDTKAFSVED LLMQGHLGHA IGLMLYIWAS IHQTRCHVIL AKLRKNKSGK VINMNHVIPH
GDWFENVSCP HYFAELLIYV SISIVFGLGN TMWWLVVLYV LCCQALTAAL CHEFYHEKFK
SYPAHRKAFI PFLF
//
