ACVL1_MOUSE
ID ACVL1_MOUSE Reviewed; 502 AA.
AC Q61288; Q61289; Q91YR0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Serine/threonine-protein kinase receptor R3;
DE Short=SKR3;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor-like kinase 1;
DE Short=ALK-1;
DE AltName: Full=TGF-B superfamily receptor type I;
DE Short=TSR-I;
DE Flags: Precursor;
GN Name=Acvrl1; Synonyms=Acvrlk1, Alk-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7488127; DOI=10.1006/bbrc.1995.2594;
RA Wu X., Robinson C.E., Fong H.W., Crabtree J.S., Rodriguez B.R., Roe B.A.,
RA Gimble J.M.;
RT "Cloning and characterization of the murine activin receptor like kinase-1
RT (ALK-1) homolog.";
RL Biochem. Biophys. Res. Commun. 216:78-83(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7750489; DOI=10.1210/endo.136.6.7750489;
RA Dewulf N., Verschueren K., Lonnoy O., Moren A., Grimsby S., Spiegle K.,
RA Miyazono K., Huylebroeck D., ten Dijke P.;
RT "Distinct spatial and temporal expression patterns of two type I receptors
RT for bone morphogenetic proteins during mouse embryogenesis.";
RL Endocrinology 136:2652-2663(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-159 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Type I receptor for TGF-beta family ligands BMP9/GDF2 and
CC BMP10 and important regulator of normal blood vessel development. On
CC ligand binding, forms a receptor complex consisting of two type II and
CC two type I transmembrane serine/threonine kinases. Type II receptors
CC phosphorylate and activate type I receptors which autophosphorylate,
CC then bind and activate SMAD transcriptional regulators. May bind
CC activin as well. {ECO:0000250|UniProtKB:P37023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37023};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; L48015; AAB03642.1; -; mRNA.
DR EMBL; Z31664; CAA83484.1; -; mRNA.
DR EMBL; AK160915; BAE36089.1; -; mRNA.
DR EMBL; AK170870; BAE42083.1; -; mRNA.
DR EMBL; CH466550; EDL04061.1; -; Genomic_DNA.
DR EMBL; CH466550; EDL04063.1; -; Genomic_DNA.
DR EMBL; BC015083; AAH15083.1; -; mRNA.
DR CCDS; CCDS37215.1; -.
DR PIR; I48241; I48241.
DR PIR; JC4337; JC4337.
DR RefSeq; NP_001264186.1; NM_001277257.1.
DR RefSeq; NP_001264187.1; NM_001277258.1.
DR RefSeq; NP_001264188.1; NM_001277259.1.
DR RefSeq; NP_033742.2; NM_009612.3.
DR AlphaFoldDB; Q61288; -.
DR SMR; Q61288; -.
DR BioGRID; 197957; 1.
DR DIP; DIP-47635N; -.
DR IntAct; Q61288; 4.
DR MINT; Q61288; -.
DR STRING; 10090.ENSMUSP00000000542; -.
DR BindingDB; Q61288; -.
DR ChEMBL; CHEMBL4105896; -.
DR GlyConnect; 2704; 1 N-Linked glycan (1 site).
DR GlyGen; Q61288; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q61288; -.
DR PhosphoSitePlus; Q61288; -.
DR jPOST; Q61288; -.
DR MaxQB; Q61288; -.
DR PaxDb; Q61288; -.
DR PeptideAtlas; Q61288; -.
DR PRIDE; Q61288; -.
DR ProteomicsDB; 281933; -.
DR Antibodypedia; 2055; 614 antibodies from 41 providers.
DR DNASU; 11482; -.
DR Ensembl; ENSMUST00000000542; ENSMUSP00000000542; ENSMUSG00000000530.
DR Ensembl; ENSMUST00000117984; ENSMUSP00000113505; ENSMUSG00000000530.
DR Ensembl; ENSMUST00000119063; ENSMUSP00000113536; ENSMUSG00000000530.
DR Ensembl; ENSMUST00000120028; ENSMUSP00000113297; ENSMUSG00000000530.
DR Ensembl; ENSMUST00000120754; ENSMUSP00000112490; ENSMUSG00000000530.
DR Ensembl; ENSMUST00000121718; ENSMUSP00000114027; ENSMUSG00000000530.
DR GeneID; 11482; -.
DR KEGG; mmu:11482; -.
DR UCSC; uc007xsm.2; mouse.
DR CTD; 94; -.
DR MGI; MGI:1338946; Acvrl1.
DR VEuPathDB; HostDB:ENSMUSG00000000530; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000161446; -.
DR HOGENOM; CLU_000288_8_5_1; -.
DR InParanoid; Q61288; -.
DR OMA; CQGTWCT; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; Q61288; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 11482; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Acvrl1; mouse.
DR PRO; PR:Q61288; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61288; protein.
DR Bgee; ENSMUSG00000000530; Expressed in granulocyte and 183 other tissues.
DR ExpressionAtlas; Q61288; baseline and differential.
DR Genevisible; Q61288; MM.
DR GO; GO:0070724; C:BMP receptor complex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; ISO:MGI.
DR GO; GO:0016361; F:activin receptor activity, type I; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISO:MGI.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0060840; P:artery development; IMP:BHF-UCL.
DR GO; GO:0008015; P:blood circulation; ISO:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042118; P:endothelial cell activation; TAS:DFLAT.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:BHF-UCL.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IDA:DFLAT.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:DFLAT.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:DFLAT.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IDA:DFLAT.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:DFLAT.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:DFLAT.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..502
FT /note="Serine/threonine-protein kinase receptor R3"
FT /id="PRO_0000024421"
FT TOPO_DOM 23..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 171..200
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 201..502
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 72..75
FT /note="Mediates specificity for BMP ligand"
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..50
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT DISULFID 35..40
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT DISULFID 45..68
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT DISULFID 76..88
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT DISULFID 89..94
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT CONFLICT 17
FT /note="F -> L (in Ref. 2; CAA83484)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="R -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="D -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="AK -> RR (in Ref. 1; AAB03642)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="A -> P (in Ref. 2; CAA83484)"
FT /evidence="ECO:0000305"
FT CONFLICT 358..359
FT /note="SD -> NE (in Ref. 2; CAA83484)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="N -> T (in Ref. 2; CAA83484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 56519 MW; 439510D3CC740D65 CRC64;
MTLGSFRRGL LMLSVAFGLT RGDLAKPSKL VNCTCESPHC KRPFCQGSWC TVVLVREQGR
HPQVYRGCGS LNQELCLGRP TEFLNHHCCY RSFCNHNVSL MLEATQTPSE EPEVDAHLPL
ILGPVLALPV LVALGALGLW RVRRRQEKQR DLHSDLGESS LILKASEQAD SMLGDFLDSD
CTTGSGSGLP FLVQRTVARQ VALVECVGKG RYGEVWRGSW HGESVAVKIF SSRDEQSWFR
ETEIYNTVLL RHDNILGFIA SDMTSRNSST QLWLITHYHE HGSLYDFLQR QTLEPQLALR
LAVSAACGLA HLHVEIFGTQ GKPAIAHRDL KSRNVLVKSN LQCCIADLGL AVMHSQSSDY
LDIGNNPRVG TKRYMAPEVL DEHIRTDCFE SYKWTDIWAF GLVLWEIARR TIINGIVEDY
RPPFYDMVPN DPSFEDMKKV VCVDQQTPTI PNRLAADPVL SGLAQMMREC WYPNPSARLT
ALRIKKTLQK LSHNPEKPKV IH
