INHA_BOVIN
ID INHA_BOVIN Reviewed; 360 AA.
AC P07994; Q2TBQ2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Inhibin alpha chain;
DE Flags: Precursor;
GN Name=INHA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian follicular fluid;
RX PubMed=3458167; DOI=10.1073/pnas.83.10.3091;
RA Forage R.G., Ring J.M., Brown R.W., McInerney B.V., Cobon G.S.,
RA Gregson R.P., Robertson D.M., Morgan F.J., Hearn M.T.W., Findlay J.K.,
RA Wettenhall R.E.H., Burger H.G., de Kretser D.M.;
RT "Cloning and sequence analysis of cDNA species coding for the two subunits
RT of inhibin from bovine follicular fluid.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3091-3095(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
RC TISSUE=Liver;
RX PubMed=7813465; DOI=10.1111/j.1432-1033.1994.00751.x;
RA Thompson D.A., Cronin C.N., Martin F.;
RT "Genomic cloning and sequence analyses of the bovine alpha-, beta A- and
RT beta B-inhibin/activin genes. Identification of transcription factor AP-2-
RT binding sites in the 5'-flanking regions by DNase I footprinting.";
RL Eur. J. Biochem. 226:751-764(1994).
RN [4]
RP PROTEIN SEQUENCE OF 227-230.
RX PubMed=3081385; DOI=10.1016/0303-7207(86)90105-x;
RA Fukuda M., Miyamoto K., Hasegawa Y., Nomura M., Igarashi M., Kangawa K.,
RA Matsuo H.;
RT "Isolation of bovine follicular fluid inhibin of about 32 kDa.";
RL Mol. Cell. Endocrinol. 44:55-60(1986).
RN [5]
RP PROTEIN SEQUENCE OF 18-37 AND 227-246, AND DISULFIDE BOND.
RX PubMed=2930562; DOI=10.1016/0006-291x(89)92255-9;
RA Sugino K., Nakamura T., Takio K., Titani K., Miyamoto K., Hasegawa Y.,
RA Igarashi M., Sugino H.;
RT "Inhibin alpha-subunit monomer is present in bovine follicular fluid.";
RL Biochem. Biophys. Res. Commun. 159:1323-1329(1989).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Proteolytic processing yields a number of bioactive forms,
CC consisting either solely of the mature alpha chain, of the most N-
CC terminal propeptide linked through a disulfide bond to the mature alpha
CC chain, or of the entire proprotein.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; M13273; AAA97414.1; -; mRNA.
DR EMBL; BC109837; AAI09838.1; -; mRNA.
DR EMBL; U16237; AAB60262.1; -; Genomic_DNA.
DR PIR; A25732; A25732.
DR RefSeq; NP_776519.2; NM_174094.4.
DR AlphaFoldDB; P07994; -.
DR STRING; 9913.ENSBTAP00000013154; -.
DR PaxDb; P07994; -.
DR PRIDE; P07994; -.
DR Ensembl; ENSBTAT00000013154; ENSBTAP00000013154; ENSBTAG00000009972.
DR GeneID; 281254; -.
DR KEGG; bta:281254; -.
DR CTD; 3623; -.
DR VEuPathDB; HostDB:ENSBTAG00000009972; -.
DR VGNC; VGNC:30199; INHA.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000005935; -.
DR HOGENOM; CLU_064515_0_0_1; -.
DR InParanoid; P07994; -.
DR OMA; TYVFRPS; -.
DR OrthoDB; 1177863at2759; -.
DR TreeFam; TF331531; -.
DR Reactome; R-BTA-209822; Glycoprotein hormones.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009972; Expressed in granulosa cell and 91 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043512; C:inhibin A complex; IEA:Ensembl.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR017175; Inhibin_asu.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR PANTHER; PTHR11848:SF117; PTHR11848:SF117; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037328; Inhibin_alpha_subunit; 1.
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..17
FT /evidence="ECO:0000269|PubMed:2930562"
FT PROPEP 18..60
FT /evidence="ECO:0000250"
FT /id="PRO_0000033676"
FT PROPEP 61..226
FT /note="Inhibin alpha N-terminal region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033677"
FT CHAIN 227..360
FT /note="Inhibin alpha chain"
FT /id="PRO_0000033678"
FT SITE 60..61
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 226..227
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 256..322
FT /evidence="ECO:0000250"
FT DISULFID 285..357
FT /evidence="ECO:0000250"
FT DISULFID 289..359
FT /evidence="ECO:0000250"
FT DISULFID 321
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 42
FT /note="P -> H (in Ref. 2; AAI09838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38810 MW; FBBF385DD1EFEF46 CRC64;
MWLQLLLLLL APQGGHGCHG LELDRELVLA KVRALFLDAL GPPPVTGEGG DPGVRRLHRR
HAVGGFMRRG SEPEDQDVSQ AILFPAAGAS CGDEPDAGEA EEGLFTYVFQ PSQHTRSRQV
TSAQLWFHTG LDRQETAAAN SSEPLLGLLV LTSGGPMPVP MSLGQAPPRW AVLHLATSAF
PLLTHPVLAL LLRCPLCSCS TRPEATPFLV AHTRAKPPSG GERARRSTPP LPWPWSPAAL
RLLQRPPEEP AAHADCHRAA LNISFQELGW DRWIVHPPSF IFYYCHGGCG LSPPQDLPLP
VPGVPPTPVQ PLSLVPGAQP CCAALPGTMR PLHVRTTSDG GYSFKYEMVP NLLTQHCACI
