INHBA_HUMAN
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 03-AUG-2022, entry version 226.
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";
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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_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 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 AlphaFoldDB; P08476; -.
DR SMR; P08476; -.
DR BioGRID; 109836; 18.
DR DIP; DIP-5824N; -.
DR IntAct; P08476; 1.
DR MINT; P08476; -.
DR STRING; 9606.ENSP00000242208; -.
DR ChEMBL; CHEMBL3588735; -.
DR DrugBank; DB16379; Garetosmab.
DR GlyGen; P08476; 3 sites, 3 O-linked glycans (2 sites).
DR iPTMnet; P08476; -.
DR PhosphoSitePlus; P08476; -.
DR BioMuta; INHBA; -.
DR DMDM; 124279; -.
DR EPD; P08476; -.
DR MassIVE; P08476; -.
DR MaxQB; P08476; -.
DR PaxDb; P08476; -.
DR PeptideAtlas; P08476; -.
DR PRIDE; P08476; -.
DR ProteomicsDB; 52111; -.
DR ABCD; P08476; 22 sequenced antibodies.
DR Antibodypedia; 13122; 568 antibodies from 35 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 CTD; 3624; -.
DR DisGeNET; 3624; -.
DR GeneCards; INHBA; -.
DR HGNC; HGNC:6066; INHBA.
DR HPA; ENSG00000122641; Tissue enhanced (brain, 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; 1385831at2759; -.
DR PhylomeDB; P08476; -.
DR TreeFam; TF351791; -.
DR PathwayCommons; P08476; -.
DR Reactome; R-HSA-1502540; Signaling by Activin.
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; 12 hits in 1076 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 164 other tissues.
DR ExpressionAtlas; P08476; baseline and differential.
DR Genevisible; P08476; HS.
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: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: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: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:0010259; P:multicellular organism aging; 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:UniProtKB.
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:0032689; P:negative regulation of interferon-gamma production; TAS:UniProtKB.
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: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: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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IGI:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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 DisProt; DP02234; -.
DR Gene3D; 2.10.90.10; -; 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; PTHR11848; 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; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
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 pathological
FT 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; alters the ratio of secreted
FT activins and ihibins; uncertain pathological significance;
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 362..364
FT /evidence="ECO:0007829|PDB:2P6A"
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
