INHBA_SHEEP
ID INHBA_SHEEP Reviewed; 425 AA.
AC P43032;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Inhibin beta A chain;
DE AltName: Full=Activin beta-A chain;
DE Flags: Precursor;
GN Name=INHBA;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7702862; DOI=10.1002/mrd.1080400102;
RA Fleming J.S., Galloway S.M., Crawford R.J., Tisdall D.J., Greenwood P.J.;
RT "Tissue-specific variation in the length of the 5' untranslated region of
RT the beta A-inhibin mRNA in sheep.";
RL Mol. Reprod. Dev. 40:1-8(1995).
RN [2]
RP PROTEIN SEQUENCE OF 310-322.
RX PubMed=3585232; DOI=10.1677/joe.0.1130213;
RA Leversha L.J., Robertson D.M., de Vos F.L., Morgan F.J., Hearn M.T.,
RA Wettenhall R.E., Findlay J.K., Burger H.G., de Kretser D.M.;
RT "Isolation of inhibin from ovine follicular fluid.";
RL J. Endocrinol. 113:213-221(1987).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; L19218; AAC41621.1; -; mRNA.
DR PIR; I47072; I47072.
DR RefSeq; NP_001009458.1; NM_001009458.1.
DR AlphaFoldDB; P43032; -.
DR SMR; P43032; -.
DR STRING; 9940.ENSOARP00000018756; -.
DR GeneID; 443524; -.
DR KEGG; oas:443524; -.
DR CTD; 3624; -.
DR eggNOG; KOG3900; Eukaryota.
DR OrthoDB; 1385831at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0043509; C:activin A complex; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0043512; C:inhibin A complex; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042701; P:progesterone secretion; ISS:UniProtKB.
DR GO; GO:0046880; P:regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..309
FT /evidence="ECO:0000255"
FT /id="PRO_0000033716"
FT CHAIN 310..425
FT /note="Inhibin beta A chain"
FT /id="PRO_0000033717"
FT REGION 260..289
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 313..321
FT /evidence="ECO:0000250"
FT DISULFID 320..390
FT /evidence="ECO:0000250"
FT DISULFID 349..422
FT /evidence="ECO:0000250"
FT DISULFID 353..424
FT /evidence="ECO:0000250"
FT DISULFID 389
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 47565 MW; C910F7F64FF82F67 CRC64;
MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL ATLPKDVPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
SEIITFAESG TARKTLHFEI SQEGSDLSVV ERAEIWLFLK VPKANRTRSK VTIRLFQQQK
HLQGSLDAGE EAEEVGLKGE KSEMLISEKV VDARKSTWHI FPVSSCIQRL LDQGKSSLDI
RIACEQCQET GASLVLLGKK KRKEEEGEGK KRDGEGGAGG DEEKEQSHRP FLMLQARQSE
DHPHRRRRRG LECDGKVNIC CKKQFYVSFK DIGWNDWIIA PSGYHANYCE GECPSHIAGT
SGSSLSFHST VINHYRMRGH SPFANLKSCC VPTKLRPMSM LYYDDGQNII KKDIQNMIVE
ECGCS
