ID INHBA_HUMAN Reviewed; 426 AA. AC P08476; Q14599; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 27-MAR-2024, entry version 235. DE RecName: Full=Inhibin beta A chain; DE AltName: Full=Activin beta-A chain; DE AltName: Full=Erythroid differentiation protein; DE Short=EDF; DE Flags: Precursor; GN Name=INHBA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3754442; DOI=10.1016/0006-291x(86)91021-1; RA Mason A.J., Niall H.D., Seeburg P.H.; RT "Structure of two human ovarian inhibins."; RL Biochem. Biophys. Res. Commun. 135:957-964(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3267209; DOI=10.1073/pnas.85.8.2434; RA Murata M., Eto Y., Shibai H., Sakai M., Muramatsu M.; RT "Erythroid differentiation factor is encoded by the same mRNA as that of RT the inhibin beta A chain."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1777673; DOI=10.3109/10425179109039678; RA Tanimoto K., Handa S.I., Ueno N., Murakami K., Fukamizu A.; RT "Structure and sequence analysis of the human activin beta A subunit RT gene."; RL DNA Seq. 2:103-110(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-426. RX PubMed=3758355; DOI=10.1016/0014-5793(86)81006-7; RA Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.; RT "Human inhibin genes. Genomic characterisation and sequencing."; RL FEBS Lett. 206:329-334(1986). RN [7] RP NUCLEOTIDE SEQUENCE OF 311-426. RC TISSUE=Testis; RA Berg H., Walter M., Northemann W.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH FST AND FSTL3. RX PubMed=12697670; DOI=10.1210/en.2002-0203; RA Schneyer A., Schoen A., Quigg A., Sidis Y.; RT "Differential binding and neutralization of activins A and B by follistatin RT and follistatin like-3 (FSTL-3/FSRP/FLRG)."; RL Endocrinology 144:1671-1674(2003). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH RAT ACTRIIB RP EXTRACELLULAR DOMAIN. RX PubMed=12660162; DOI=10.1093/emboj/cdg156; RA Thompson T.B., Woodruff T.K., Jardetzky T.S.; RT "Structures of an ActRIIB:activin A complex reveal a novel binding mode for RT TGF-beta ligand:receptor interactions."; RL EMBO J. 22:1555-1566(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 311-426 IN COMPLEX WITH FSTL3, RP AND DISULFIDE BONDS. RX PubMed=18768470; DOI=10.1074/jbc.m801266200; RA Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., RA Thompson T.B.; RT "The structure of FSTL3.activin A complex. Differential binding of N- RT terminal domains influences follistatin-type antagonist specificity."; RL J. Biol. Chem. 283:32831-32838(2008). RN [11] RP VARIANTS GLU-280 AND SER-386, AND CHARACTERIZATION OF VARIANT SER-386. RX PubMed=24302632; DOI=10.1002/humu.22489; RA Tournier I., Marlin R., Walton K., Charbonnier F., Coutant S., Thery J.C., RA Charbonnier C., Spurrell C., Vezain M., Ippolito L., Bougeard G., Roman H., RA Tinat J., Sabourin J.C., Stoppa-Lyonnet D., Caron O., RA Bressac-de Paillerets B., Vaur D., King M.C., Harrison C., Frebourg T.; RT "Germline mutations of inhibins in early-onset ovarian epithelial tumors."; RL Hum. Mutat. 35:294-297(2014). CC -!- FUNCTION: Inhibins and activins inhibit and activate, respectively, the CC secretion of follitropin by the pituitary gland. Inhibins/activins are CC involved in regulating a number of diverse functions such as CC hypothalamic and pituitary hormone secretion, gonadal hormone CC secretion, germ cell development and maturation, erythroid CC differentiation, insulin secretion, nerve cell survival, embryonic CC axial development or bone growth, depending on their subunit CC composition. Inhibins appear to oppose the functions of activins. CC -!- SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a CC dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. CC Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. CC Activin AB is a dimer of beta-A and beta-B. Interacts with FST and CC FSTL3. {ECO:0000269|PubMed:12660162, ECO:0000269|PubMed:12697670, CC ECO:0000269|PubMed:18768470}. CC -!- INTERACTION: CC P08476; P21674: Fst; Xeno; NbExp=2; IntAct=EBI-8077140, EBI-5746973; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Activin entry; CC URL="https://en.wikipedia.org/wiki/Activin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13436; AAA59168.1; -; mRNA. DR EMBL; X04447; CAA28041.1; -; Genomic_DNA. DR EMBL; X57578; CAA40805.1; -; Genomic_DNA. DR EMBL; X57579; CAA40805.1; JOINED; Genomic_DNA. DR EMBL; X57579; CAA40806.1; -; Genomic_DNA. DR EMBL; AC005027; AAQ96861.1; -; Genomic_DNA. DR EMBL; BC007858; AAH07858.1; -; mRNA. DR EMBL; J03634; AAA35787.1; -; mRNA. DR EMBL; X72498; CAA51163.1; -; mRNA. DR CCDS; CCDS5464.1; -. DR PIR; S30488; B24248. DR RefSeq; NP_002183.1; NM_002192.3. DR RefSeq; XP_016867663.1; XM_017012174.1. DR RefSeq; XP_016867665.1; XM_017012176.1. DR PDB; 1NYS; X-ray; 3.05 A; B/D=311-426. DR PDB; 1NYU; X-ray; 3.10 A; B/D=311-426. DR PDB; 1S4Y; X-ray; 2.30 A; B/D=311-426. DR PDB; 2ARP; X-ray; 2.00 A; A=311-426. DR PDB; 2ARV; X-ray; 2.00 A; A/B=311-426. DR PDB; 2B0U; X-ray; 2.80 A; A/B=311-426. DR PDB; 2P6A; X-ray; 3.40 A; A/B=311-426. DR PDB; 3B4V; X-ray; 2.48 A; A/B/E/F=311-426. DR PDB; 4MID; X-ray; 2.14 A; A=334-426. DR PDB; 5HLY; X-ray; 2.30 A; A=30-426. DR PDB; 5HLZ; X-ray; 2.85 A; A/C/E/G=30-305, B/D/F/H=311-426. DR PDB; 6Y6N; X-ray; 2.03 A; A/B=311-426. DR PDB; 6Y6O; X-ray; 2.04 A; A/B=311-426. DR PDB; 7OLY; X-ray; 3.27 A; A=311-426. DR PDB; 7U5P; X-ray; 3.14 A; B/D/F/H=311-426. DR PDBsum; 1NYS; -. DR PDBsum; 1NYU; -. DR PDBsum; 1S4Y; -. DR PDBsum; 2ARP; -. DR PDBsum; 2ARV; -. DR PDBsum; 2B0U; -. DR PDBsum; 2P6A; -. DR PDBsum; 3B4V; -. DR PDBsum; 4MID; -. DR PDBsum; 5HLY; -. DR PDBsum; 5HLZ; -. DR PDBsum; 6Y6N; -. DR PDBsum; 6Y6O; -. DR PDBsum; 7OLY; -. DR PDBsum; 7U5P; -. DR AlphaFoldDB; P08476; -. DR SMR; P08476; -. DR BioGRID; 109836; 20. DR DIP; DIP-5824N; -. DR IntAct; P08476; 2. DR MINT; P08476; -. DR STRING; 9606.ENSP00000242208; -. DR ChEMBL; CHEMBL3588735; -. DR DrugBank; DB16379; Garetosmab. DR GlyCosmos; P08476; 3 sites, 3 glycans. DR GlyGen; P08476; 4 sites, 4 O-linked glycans (3 sites). DR iPTMnet; P08476; -. DR PhosphoSitePlus; P08476; -. DR BioMuta; INHBA; -. DR DMDM; 124279; -. DR EPD; P08476; -. DR MassIVE; P08476; -. DR MaxQB; P08476; -. DR PaxDb; 9606-ENSP00000242208; -. DR PeptideAtlas; P08476; -. DR ProteomicsDB; 52111; -. DR ABCD; P08476; 22 sequenced antibodies. DR Antibodypedia; 13122; 632 antibodies from 36 providers. DR DNASU; 3624; -. DR Ensembl; ENST00000242208.5; ENSP00000242208.4; ENSG00000122641.11. DR Ensembl; ENST00000442711.1; ENSP00000397197.1; ENSG00000122641.11. DR Ensembl; ENST00000638023.1; ENSP00000490646.1; ENSG00000122641.11. DR GeneID; 3624; -. DR KEGG; hsa:3624; -. DR MANE-Select; ENST00000242208.5; ENSP00000242208.4; NM_002192.4; NP_002183.1. DR UCSC; uc003thq.4; human. DR AGR; HGNC:6066; -. DR CTD; 3624; -. DR DisGeNET; 3624; -. DR GeneCards; INHBA; -. DR HGNC; HGNC:6066; INHBA. DR HPA; ENSG00000122641; Tissue enhanced (gallbladder). DR MalaCards; INHBA; -. DR MIM; 147290; gene. DR neXtProt; NX_P08476; -. DR OpenTargets; ENSG00000122641; -. DR Orphanet; 213504; Adenocarcinoma of ovary. DR PharmGKB; PA29877; -. DR VEuPathDB; HostDB:ENSG00000122641; -. DR eggNOG; KOG3900; Eukaryota. DR GeneTree; ENSGT00940000157116; -. DR HOGENOM; CLU_020515_5_1_1; -. DR InParanoid; P08476; -. DR OMA; LALCWIR; -. DR OrthoDB; 3015718at2759; -. DR PhylomeDB; P08476; -. DR TreeFam; TF351791; -. DR PathwayCommons; P08476; -. DR Reactome; R-HSA-1502540; Signaling by Activin. DR Reactome; R-HSA-201451; Signaling by BMP. DR Reactome; R-HSA-209822; Glycoprotein hormones. DR Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin. DR SignaLink; P08476; -. DR SIGNOR; P08476; -. DR BioGRID-ORCS; 3624; 13 hits in 1160 CRISPR screens. DR ChiTaRS; INHBA; human. DR EvolutionaryTrace; P08476; -. DR GenomeRNAi; 3624; -. DR Pharos; P08476; Tbio. DR PRO; PR:P08476; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P08476; Protein. DR Bgee; ENSG00000122641; Expressed in cartilage tissue and 166 other cell types or tissues. DR ExpressionAtlas; P08476; baseline and differential. DR GO; GO:0043509; C:activin A complex; IDA:HGNC-UCL. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0043512; C:inhibin A complex; IDA:HGNC-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005125; F:cytokine activity; IDA:HGNC-UCL. DR GO; GO:0008083; F:growth factor activity; TAS:UniProtKB. DR GO; GO:0005179; F:hormone activity; TAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0017046; F:peptide hormone binding; IPI:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0070699; F:type II activin receptor binding; IPI:BHF-UCL. DR GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0006914; P:autophagy; IEA:Ensembl. DR GO; GO:0060936; P:cardiac fibroblast cell development; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; TAS:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB. DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl. DR GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl. DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0006952; P:defense response; TAS:UniProtKB. DR GO; GO:0035987; P:endodermal cell differentiation; IDA:BHF-UCL. DR GO; GO:0030218; P:erythrocyte differentiation; NAS:UniProtKB. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL. DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB. DR GO; GO:0097154; P:GABAergic neuron differentiation; IDA:ParkinsonsUK-UCL. DR GO; GO:0001942; P:hair follicle development; IGI:UniProtKB. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB. DR GO; GO:0042541; P:hemoglobin biosynthetic process; IDA:UniProtKB. DR GO; GO:0008584; P:male gonad development; IGI:UniProtKB. DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl. DR GO; GO:0045578; P:negative regulation of B cell differentiation; TAS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:HGNC-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; NAS:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:HGNC-UCL. DR GO; GO:0045650; P:negative regulation of macrophage differentiation; TAS:UniProtKB. DR GO; GO:0042326; P:negative regulation of phosphorylation; TAS:UniProtKB. DR GO; GO:0032689; P:negative regulation of type II interferon production; TAS:UniProtKB. DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB. DR GO; GO:0042476; P:odontogenesis; IGI:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; IGI:UniProtKB. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:HGNC-UCL. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB. DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; TAS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB. DR GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl. DR GO; GO:0042701; P:progesterone secretion; IGI:UniProtKB. DR GO; GO:0046880; P:regulation of follicle-stimulating hormone secretion; IGI:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl. DR GO; GO:0060021; P:roof of mouth development; IGI:UniProtKB. DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl. DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IDA:ParkinsonsUK-UCL. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd19404; TGF_beta_INHBA; 1. DR DisProt; DP02234; -. DR Gene3D; 2.60.120.970; -; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR IDEAL; IID00338; -. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR000491; Inhibin_betaA. DR InterPro; IPR001839; TGF-b_C. DR InterPro; IPR001111; TGF-b_propeptide. DR InterPro; IPR015615; TGF-beta-rel. DR InterPro; IPR017948; TGFb_CS. DR PANTHER; PTHR11848:SF133; INHIBIN BETA A CHAIN; 1. DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00670; INHIBINBA. DR SMART; SM00204; TGFB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. DR PROSITE; PS51362; TGF_BETA_2; 1. DR Genevisible; P08476; HS. PE 1: Evidence at protein level; KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond; KW Glycoprotein; Growth factor; Hormone; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT PROPEP 21..310 FT /id="PRO_0000033708" FT CHAIN 311..426 FT /note="Inhibin beta A chain" FT /id="PRO_0000033709" FT REGION 259..288 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 314..322 FT /evidence="ECO:0000269|PubMed:18768470" FT DISULFID 321..391 FT /evidence="ECO:0000269|PubMed:18768470" FT DISULFID 350..423 FT /evidence="ECO:0000269|PubMed:18768470" FT DISULFID 354..425 FT /evidence="ECO:0000269|PubMed:18768470" FT DISULFID 390 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18768470" FT VARIANT 280 FT /note="G -> E (found in a patient with early-onset FT epithelial ovarian tumor; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24302632" FT /id="VAR_072640" FT VARIANT 299 FT /note="Q -> P (in dbSNP:rs41294833)" FT /id="VAR_052566" FT VARIANT 386 FT /note="N -> S (found in a patient with early-onset FT epithelial ovarian tumor; uncertain significance; alters FT the ratio of secreted activins and ihibins; FT dbSNP:rs1361491625)" FT /evidence="ECO:0000269|PubMed:24302632" FT /id="VAR_072641" FT CONFLICT 377..379 FT /note="RMR -> AC (in Ref. 7; CAA51163)" FT /evidence="ECO:0000305" FT HELIX 52..65 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 80..89 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 107..118 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 149..160 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 170..180 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 201..212 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 217..222 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 224..232 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 237..243 FT /evidence="ECO:0007829|PDB:5HLY" FT TURN 245..251 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:5HLY" FT HELIX 284..289 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:5HLY" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:2ARP" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:2ARP" FT HELIX 330..333 FT /evidence="ECO:0007829|PDB:2ARP" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:2ARP" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:2ARP" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:2ARP" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:2ARP" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:2ARV" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:7U5P" FT HELIX 368..375 FT /evidence="ECO:0007829|PDB:2ARP" FT TURN 378..380 FT /evidence="ECO:0007829|PDB:2B0U" FT TURN 382..386 FT /evidence="ECO:0007829|PDB:2ARV" FT STRAND 391..404 FT /evidence="ECO:0007829|PDB:2ARP" FT TURN 406..408 FT /evidence="ECO:0007829|PDB:2ARV" FT STRAND 410..425 FT /evidence="ECO:0007829|PDB:2ARP" SQ SEQUENCE 426 AA; 47442 MW; 201CDEDF99CB6919 CRC64; MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL AALPKDVPNS QPEMVEAVKK HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK HPQGSLDTGE EAEEVGLKGE RSELLLSEKV VDARKSTWHV FPVSSSIQRL LDQGKSSLDV RIACEQCQES GASLVLLGKK KKKEEEGEGK KKGGGEGGAG ADEEKEQSHR PFLMLQARQS EDHPHRRRRR GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS //