GENTAUR Molecular Products.

 ACVR1_HUMAN             Reviewed;         509 AA.
 Q04771;
 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1994, sequence version 1.
 28-MAR-2018, entry version 185.
 RecName: Full=Activin receptor type-1;
          EC=2.7.11.30;
 AltName: Full=Activin receptor type I;
          Short=ACTR-I;
 AltName: Full=Activin receptor-like kinase 2;
          Short=ALK-2;
 AltName: Full=Serine/threonine-protein kinase receptor R1;
          Short=SKR1;
 AltName: Full=TGF-B superfamily receptor type I;
          Short=TSR-I;
 Flags: Precursor;
 Name=ACVR1; Synonyms=ACVRLK2;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=8389764;
 Matsuzaki K., McKeehan W.L.;
 "A widely expressed transmembrane serine/threonine kinase that does
 not bind activin, inhibin, transforming growth factor beta, or bone
 morphogenic factor.";
 J. Biol. Chem. 268:12719-12723(1993).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Placenta;
 PubMed=8397373;
 ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J.,
 Toyoshima H., Heldin C.-H., Miyazono K.;
 "Activin receptor-like kinases: a novel subclass of cell-surface
 receptors with predicted serine/threonine kinase activity.";
 Oncogene 8:2879-2887(1993).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Lung;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
 Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
 Mann M., Daub H.;
 "Large-scale proteomics analysis of the human kinome.";
 Mol. Cell. Proteomics 8:1751-1764(2009).
 [5]
 INTERACTION WITH FCHO1.
 PubMed=22484487; DOI=10.1038/ncb2473;
 Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
 Tsang M., Traub L.M.;
 "Distinct and separable activities of the endocytic clathrin-coat
 components Fcho1/2 and AP-2 in developmental patterning.";
 Nat. Cell Biol. 14:488-501(2012).
 [6]
 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 172-499 IN COMPLEX WITH
 FKBP1A.
 Structural genomics consortium (SGC);
 "Crystal structure of the kinase domain of type I activin receptor
 (ACVR1) in complex with FKBP12 and dorsomorphin.";
 Submitted (JUN-2009) to the PDB data bank.
 [7]
 VARIANT FOP HIS-206.
 PubMed=16642017; DOI=10.1038/ng1783;
 Shore E.M., Xu M., Feldman G.J., Fenstermacher D.A., Brown M.A.,
 Kaplan F.S.;
 "A recurrent mutation in the BMP type I receptor ACVR1 causes
 inherited and sporadic fibrodysplasia ossificans progressiva.";
 Nat. Genet. 38:525-527(2006).
 [8]
 VARIANTS [LARGE SCALE ANALYSIS] GLY-15; PHE-41; GLN-47 AND SER-115.
 PubMed=17344846; DOI=10.1038/nature05610;
 Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
 Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
 O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
 Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
 Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
 Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
 Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
 West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
 Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
 DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
 Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
 Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
 "Patterns of somatic mutation in human cancer genomes.";
 Nature 446:153-158(2007).
 [9]
 VARIANTS FOP 197-PRO-PHE-198 DELINS LEU; HIS-206; GLU-207; ARG-328;
 TRP-328; GLU-328; ASP-356 AND PRO-375.
 PubMed=19085907; DOI=10.1002/humu.20868;
 Kaplan F.S., Xu M., Seemann P., Connor J.M., Glaser D.L., Carroll L.,
 Delai P., Fastnacht-Urban E., Forman S.J., Gillessen-Kaesbach G.,
 Hoover-Fong J., Koester B., Pauli R.M., Reardon W., Zaidi S.A.,
 Zasloff M., Morhart R., Mundlos S., Groppe J., Shore E.M.;
 "Classic and atypical fibrodysplasia ossificans progressiva (FOP)
 phenotypes are caused by mutations in the bone morphogenetic protein
 (BMP) type I receptor ACVR1.";
 Hum. Mutat. 30:379-390(2009).
 [10]
 VARIANTS FOP ILE-202 AND GLU-328.
 PubMed=19330033; DOI=10.1371/journal.pone.0005005;
 Petrie K.A., Lee W.H., Bullock A.N., Pointon J.J., Smith R.,
 Russell R.G., Brown M.A., Wordsworth B.P., Triffitt J.T.;
 "Novel mutations in ACVR1 result in atypical features in two
 fibrodysplasia ossificans progressiva patients.";
 PLoS ONE 4:E5005-E5005(2009).
 -!- FUNCTION: On ligand binding, forms a receptor complex consisting
     of two type II and two type I transmembrane serine/threonine
     kinases. Type II receptors phosphorylate and activate type I
     receptors which autophosphorylate, then bind and activate SMAD
     transcriptional regulators. Receptor for activin. May be involved
     for left-right pattern formation during embryogenesis (By
     similarity). {ECO:0000250}.
 -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
     protein] phosphate.
 -!- COFACTOR:
     Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
     Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
 -!- SUBUNIT: Interacts with FKBP1A. Interacts with FCHO1.
     {ECO:0000269|PubMed:22484487, ECO:0000269|Ref.6}.
 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
     protein.
 -!- TISSUE SPECIFICITY: Expressed in normal parenchymal cells,
     endothelial cells, fibroblasts and tumor-derived epithelial cells.
 -!- DISEASE: Fibrodysplasia ossificans progressiva (FOP) [MIM:135100]:
     A rare autosomal dominant connective tissue disorder resulting in
     skeletal malformations and progressive extraskeletal ossification.
     Heterotopic ossification begins in childhood and can be induced by
     trauma or may occur without warning. Bone formation is episodic
     and progressive, leading to a debilitating ankylosis of all major
     joints of the axial and appendicular skeleton, rendering movement
     impossible. {ECO:0000269|PubMed:16642017,
     ECO:0000269|PubMed:19085907, ECO:0000269|PubMed:19330033}.
     Note=The disease is caused by mutations affecting the gene
     represented in this entry.
 -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
     protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; L02911; AAA36614.1; -; mRNA.
 EMBL; Z22534; CAA80256.1; -; mRNA.
 EMBL; BC033867; AAH33867.1; -; mRNA.
 CCDS; CCDS2206.1; -.
 PIR; A45992; A45992.
 RefSeq; NP_001096.1; NM_001105.4.
 RefSeq; NP_001104537.1; NM_001111067.2.
 RefSeq; NP_001334592.1; NM_001347663.1.
 RefSeq; NP_001334593.1; NM_001347664.1.
 RefSeq; NP_001334594.1; NM_001347665.1.
 RefSeq; NP_001334595.1; NM_001347666.1.
 RefSeq; NP_001334596.1; NM_001347667.1.
 RefSeq; XP_006712888.1; XM_006712825.3.
 RefSeq; XP_011510410.1; XM_011512108.2.
 UniGene; Hs.470316; -.
 PDB; 3H9R; X-ray; 2.35 A; A=172-499.
 PDB; 3MTF; X-ray; 2.15 A; A/B=201-499.
 PDB; 3OOM; X-ray; 2.00 A; A=201-499.
 PDB; 3Q4U; X-ray; 1.82 A; A/B/C/D=201-499.
 PDB; 4BGG; X-ray; 2.56 A; A/B/C/D=201-499.
 PDB; 4C02; X-ray; 2.17 A; A=172-499.
 PDB; 4DYM; X-ray; 2.42 A; A=201-499.
 PDB; 5OXG; X-ray; 2.13 A; A/B/C/D=201-499.
 PDB; 5OY6; X-ray; 2.56 A; A/B/C/D=201-499.
 PDB; 6EIX; X-ray; 2.30 A; A=172-509.
 PDBsum; 3H9R; -.
 PDBsum; 3MTF; -.
 PDBsum; 3OOM; -.
 PDBsum; 3Q4U; -.
 PDBsum; 4BGG; -.
 PDBsum; 4C02; -.
 PDBsum; 4DYM; -.
 PDBsum; 5OXG; -.
 PDBsum; 5OY6; -.
 PDBsum; 6EIX; -.
 ProteinModelPortal; Q04771; -.
 SMR; Q04771; -.
 BioGrid; 106605; 71.
 DIP; DIP-212N; -.
 IntAct; Q04771; 14.
 MINT; Q04771; -.
 STRING; 9606.ENSP00000263640; -.
 BindingDB; Q04771; -.
 ChEMBL; CHEMBL5903; -.
 DrugBank; DB00171; Adenosine triphosphate.
 GuidetoPHARMACOLOGY; 1785; -.
 iPTMnet; Q04771; -.
 PhosphoSitePlus; Q04771; -.
 BioMuta; ACVR1; -.
 DMDM; 462447; -.
 EPD; Q04771; -.
 MaxQB; Q04771; -.
 PaxDb; Q04771; -.
 PeptideAtlas; Q04771; -.
 PRIDE; Q04771; -.
 DNASU; 90; -.
 Ensembl; ENST00000263640; ENSP00000263640; ENSG00000115170.
 Ensembl; ENST00000409283; ENSP00000387273; ENSG00000115170.
 Ensembl; ENST00000410057; ENSP00000387127; ENSG00000115170.
 Ensembl; ENST00000434821; ENSP00000405004; ENSG00000115170.
 GeneID; 90; -.
 KEGG; hsa:90; -.
 UCSC; uc002tzm.4; human.
 CTD; 90; -.
 DisGeNET; 90; -.
 EuPathDB; HostDB:ENSG00000115170.13; -.
 GeneCards; ACVR1; -.
 HGNC; HGNC:171; ACVR1.
 HPA; HPA007505; -.
 MalaCards; ACVR1; -.
 MIM; 102576; gene.
 MIM; 135100; phenotype.
 neXtProt; NX_Q04771; -.
 OpenTargets; ENSG00000115170; -.
 Orphanet; 337; Fibrodysplasia ossificans progressiva.
 PharmGKB; PA24492; -.
 eggNOG; KOG2052; Eukaryota.
 eggNOG; ENOG410XQT0; LUCA.
 GeneTree; ENSGT00760000118876; -.
 HOGENOM; HOG000230587; -.
 HOVERGEN; HBG054502; -.
 InParanoid; Q04771; -.
 KO; K04675; -.
 OMA; GHLCNMN; -.
 OrthoDB; EOG091G0BIU; -.
 PhylomeDB; Q04771; -.
 TreeFam; TF314724; -.
 BRENDA; 2.7.10.2; 2681.
 SignaLink; Q04771; -.
 SIGNOR; Q04771; -.
 ChiTaRS; ACVR1; human.
 EvolutionaryTrace; Q04771; -.
 GeneWiki; ACVR1; -.
 GenomeRNAi; 90; -.
 PRO; PR:Q04771; -.
 Proteomes; UP000005640; Chromosome 2.
 Bgee; ENSG00000115170; -.
 CleanEx; HS_ACVR1; -.
 ExpressionAtlas; Q04771; baseline and differential.
 Genevisible; Q04771; HS.
 GO; GO:0048179; C:activin receptor complex; IDA:UniProtKB.
 GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
 GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
 GO; GO:0048185; F:activin binding; IDA:UniProtKB.
 GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
 GO; GO:0005524; F:ATP binding; IDA:HGNC.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0017046; F:peptide hormone binding; NAS:UniProtKB.
 GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
 GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
 GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC.
 GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
 GO; GO:0046332; F:SMAD binding; IDA:HGNC.
 GO; GO:0050431; F:transforming growth factor beta binding; IDA:UniProtKB.
 GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Ensembl.
 GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; NAS:UniProtKB.
 GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
 GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
 GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
 GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
 GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
 GO; GO:0061312; P:BMP signaling pathway involved in heart development; ISS:BHF-UCL.
 GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
 GO; GO:0060923; P:cardiac muscle cell fate commitment; IMP:BHF-UCL.
 GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
 GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
 GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:BHF-UCL.
 GO; GO:0061445; P:endocardial cushion cell fate commitment; IMP:BHF-UCL.
 GO; GO:0003274; P:endocardial cushion fusion; ISS:BHF-UCL.
 GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
 GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:HGNC.
 GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
 GO; GO:0007281; P:germ cell development; IEA:Ensembl.
 GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
 GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
 GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
 GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IMP:HGNC.
 GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
 GO; GO:0009968; P:negative regulation of signal transduction; IMP:HGNC.
 GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
 GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
 GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
 GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
 GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
 GO; GO:0030335; P:positive regulation of cell migration; IGI:BHF-UCL.
 GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:BHF-UCL.
 GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
 GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
 GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
 GO; GO:0006468; P:protein phosphorylation; IDA:HGNC.
 GO; GO:0030278; P:regulation of ossification; IMP:UniProtKB.
 GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
 GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
 InterPro; IPR000472; Activin_recp.
 InterPro; IPR003605; GS_dom.
 InterPro; IPR011009; Kinase-like_dom_sf.
 InterPro; IPR000719; Prot_kinase_dom.
 InterPro; IPR017441; Protein_kinase_ATP_BS.
 InterPro; IPR008271; Ser/Thr_kinase_AS.
 InterPro; IPR000333; TGFB_receptor.
 PANTHER; PTHR23255; PTHR23255; 1.
 Pfam; PF01064; Activin_recp; 1.
 Pfam; PF00069; Pkinase; 1.
 Pfam; PF08515; TGF_beta_GS; 1.
 PRINTS; PR00653; ACTIVIN2R.
 SMART; SM00467; GS; 1.
 SMART; SM00220; S_TKc; 1.
 SUPFAM; SSF56112; SSF56112; 1.
 PROSITE; PS51256; GS; 1.
 PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
 PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
 1: Evidence at protein level;
 3D-structure; ATP-binding; Complete proteome; Disease mutation;
 Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding;
 Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
 Reference proteome; Serine/threonine-protein kinase; Signal;
 Transferase; Transmembrane; Transmembrane helix.
 SIGNAL        1     20       {ECO:0000250}.
 CHAIN        21    509       Activin receptor type-1.
                              /FTId=PRO_0000024394.
 TOPO_DOM     21    123       Extracellular. {ECO:0000255}.
 TRANSMEM    124    146       Helical. {ECO:0000255}.
 TOPO_DOM    147    509       Cytoplasmic. {ECO:0000255}.
 DOMAIN      178    207       GS. {ECO:0000255|PROSITE-
                              ProRule:PRU00585}.
 DOMAIN      208    502       Protein kinase. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 NP_BIND     214    222       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 ACT_SITE    336    336       Proton acceptor. {ECO:0000255|PROSITE-
                              ProRule:PRU00159, ECO:0000255|PROSITE-
                              ProRule:PRU10027}.
 BINDING     235    235       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 MOD_RES     501    501       Phosphoserine.
                              {ECO:0000244|PubMed:19369195}.
 CARBOHYD    102    102       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 VARIANT      15     15       A -> G (in dbSNP:rs13406336).
                              {ECO:0000269|PubMed:17344846}.
                              /FTId=VAR_041392.
 VARIANT      41     41       S -> F (in dbSNP:rs55957214).
                              {ECO:0000269|PubMed:17344846}.
                              /FTId=VAR_041393.
 VARIANT      47     47       H -> Q (in dbSNP:rs34056189).
                              {ECO:0000269|PubMed:17344846}.
                              /FTId=VAR_041394.
 VARIANT     115    115       P -> S (in a melanoma sample; somatic
                              mutation). {ECO:0000269|PubMed:17344846}.
                              /FTId=VAR_041395.
 VARIANT     197    198       PF -> L (in FOP; variant phenotype).
                              {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058418.
 VARIANT     202    202       R -> I (in FOP; with some atypical
                              features; dbSNP:rs387906591).
                              {ECO:0000269|PubMed:19330033}.
                              /FTId=VAR_058419.
 VARIANT     206    206       R -> H (in FOP; dbSNP:rs121912678).
                              {ECO:0000269|PubMed:16642017,
                              ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_028444.
 VARIANT     207    207       Q -> E (in FOP; with some atypical
                              features). {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058420.
 VARIANT     328    328       G -> E (in FOP; variant phenotype;
                              dbSNP:rs387906589).
                              {ECO:0000269|PubMed:19085907,
                              ECO:0000269|PubMed:19330033}.
                              /FTId=VAR_058421.
 VARIANT     328    328       G -> R (in FOP; variant phenotype;
                              dbSNP:rs387906588).
                              {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058422.
 VARIANT     328    328       G -> W (in FOP; variant phenotype;
                              dbSNP:rs387906588).
                              {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058423.
 VARIANT     356    356       G -> D (in FOP; variant phenotype;
                              dbSNP:rs121912679).
                              {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058424.
 VARIANT     375    375       R -> P (in FOP; variant phenotype;
                              dbSNP:rs387906590).
                              {ECO:0000269|PubMed:19085907}.
                              /FTId=VAR_058425.
 HELIX       180    184       {ECO:0000244|PDB:4C02}.
 STRAND      192    196       {ECO:0000244|PDB:4C02}.
 HELIX       205    207       {ECO:0000244|PDB:3Q4U}.
 STRAND      209    216       {ECO:0000244|PDB:3Q4U}.
 STRAND      218    227       {ECO:0000244|PDB:3Q4U}.
 STRAND      230    237       {ECO:0000244|PDB:3Q4U}.
 HELIX       239    241       {ECO:0000244|PDB:3Q4U}.
 HELIX       242    254       {ECO:0000244|PDB:3Q4U}.
 STRAND      265    273       {ECO:0000244|PDB:3Q4U}.
 STRAND      276    283       {ECO:0000244|PDB:3Q4U}.
 HELIX       291    295       {ECO:0000244|PDB:3Q4U}.
 HELIX       302    320       {ECO:0000244|PDB:3Q4U}.
 STRAND      325    327       {ECO:0000244|PDB:3MTF}.
 STRAND      331    333       {ECO:0000244|PDB:3Q4U}.
 HELIX       339    341       {ECO:0000244|PDB:3Q4U}.
 STRAND      342    344       {ECO:0000244|PDB:3Q4U}.
 STRAND      350    352       {ECO:0000244|PDB:3Q4U}.
 STRAND      359    362       {ECO:0000244|PDB:3Q4U}.
 TURN        363    366       {ECO:0000244|PDB:3Q4U}.
 STRAND      367    369       {ECO:0000244|PDB:3Q4U}.
 HELIX       379    381       {ECO:0000244|PDB:3Q4U}.
 HELIX       384    387       {ECO:0000244|PDB:3Q4U}.
 HELIX       396    415       {ECO:0000244|PDB:3Q4U}.
 TURN        430    434       {ECO:0000244|PDB:3Q4U}.
 HELIX       441    448       {ECO:0000244|PDB:3Q4U}.
 HELIX       459    463       {ECO:0000244|PDB:3Q4U}.
 HELIX       465    477       {ECO:0000244|PDB:3Q4U}.
 HELIX       482    484       {ECO:0000244|PDB:3Q4U}.
 HELIX       488    498       {ECO:0000244|PDB:3Q4U}.
 SEQUENCE   509 AA;  57153 MW;  E2B0F051D19DD052 CRC64;
 MVDGVMILPV LIMIALPSPS MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN
 DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF
 HLEVGLIILS VVFAVCLLAC LLGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL
 ADLLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR
 DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL
 DTVSCLRIVL SIASGLAHLH IEIFGTQGKP AIAHRDLKSK NILVKKNGQC CIADLGLAVM
 HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS
 NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ
 NPSARLTALR IKKTLTKIDN SLDKLKTDC

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