INHA_PIG
ID INHA_PIG Reviewed; 364 AA.
AC P04087; Q2I0D4;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Inhibin alpha chain;
DE Flags: Precursor;
GN Name=INHA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3016724; DOI=10.1073/pnas.83.16.5849;
RA Mayo K.E., Cerelli G.M., Spiess J., Rivier J., Rosenfeld M.G., Evans R.M.,
RA Vale W.;
RT "Inhibin A-subunit cDNAs from porcine ovary and human placenta.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5849-5853(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 231-256.
RC TISSUE=Ovarian follicular fluid;
RX PubMed=2417121; DOI=10.1038/318659a0;
RA Mason A.J., Hayflick J.S., Ling N., Esch F., Ueno N., Ying S.-Y.,
RA Guillemin R., Niall H., Seeburg P.H.;
RT "Complementary DNA sequences of ovarian follicular fluid inhibin show
RT precursor structure and homology with transforming growth factor-beta.";
RL Nature 318:659-663(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16879365; DOI=10.1111/j.1365-2052.2006.01467.x;
RA Kim J.G., Nonneman D.J., Vallet J.L., Wise T.H., Rohrer G.A.;
RT "Sequence variation and evaluation of inhibina-subunit and steroidogenic
RT acute regulatory protein for reproductive traits in swine.";
RL Anim. Genet. 37:424-425(2006).
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; M13980; AAA31057.1; -; mRNA.
DR EMBL; X03265; CAA27019.1; -; mRNA.
DR EMBL; DQ356013; ABC79688.1; -; Genomic_DNA.
DR PIR; A01392; WFPGA.
DR RefSeq; NP_999354.1; NM_214189.1.
DR AlphaFoldDB; P04087; -.
DR STRING; 9823.ENSSSCP00000021670; -.
DR PaxDb; P04087; -.
DR PeptideAtlas; P04087; -.
DR Ensembl; ENSSSCT00000031176; ENSSSCP00000021670; ENSSSCG00000020771.
DR Ensembl; ENSSSCT00005009325; ENSSSCP00005005538; ENSSSCG00005006134.
DR Ensembl; ENSSSCT00015051408; ENSSSCP00015020501; ENSSSCG00015038605.
DR Ensembl; ENSSSCT00025016118; ENSSSCP00025006396; ENSSSCG00025012180.
DR Ensembl; ENSSSCT00030013150; ENSSSCP00030005916; ENSSSCG00030009605.
DR Ensembl; ENSSSCT00035013462; ENSSSCP00035004545; ENSSSCG00035010763.
DR Ensembl; ENSSSCT00040029621; ENSSSCP00040012393; ENSSSCG00040022088.
DR Ensembl; ENSSSCT00045051365; ENSSSCP00045035713; ENSSSCG00045030122.
DR Ensembl; ENSSSCT00055006153; ENSSSCP00055004829; ENSSSCG00055003175.
DR Ensembl; ENSSSCT00060096207; ENSSSCP00060041623; ENSSSCG00060070487.
DR Ensembl; ENSSSCT00065041439; ENSSSCP00065017568; ENSSSCG00065030658.
DR Ensembl; ENSSSCT00070031278; ENSSSCP00070026076; ENSSSCG00070015921.
DR GeneID; 397386; -.
DR KEGG; ssc:397386; -.
DR CTD; 3623; -.
DR VGNC; VGNC:96372; INHA.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000005935; -.
DR InParanoid; P04087; -.
DR OMA; TYVFRPS; -.
DR OrthoDB; 1177863at2759; -.
DR Proteomes; UP000008227; Chromosome 15.
DR Proteomes; UP000314985; Chromosome 15.
DR Bgee; ENSSSCG00000020771; Expressed in granulosa cell and 14 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 PROPEP 18..60
FT /id="PRO_0000033691"
FT PROPEP 61..230
FT /note="Inhibin alpha N-terminal region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033692"
FT CHAIN 231..364
FT /note="Inhibin alpha chain"
FT /id="PRO_0000033693"
FT SITE 60..61
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 230..231
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 260..326
FT /evidence="ECO:0000250"
FT DISULFID 289..361
FT /evidence="ECO:0000250"
FT DISULFID 293..363
FT /evidence="ECO:0000250"
FT DISULFID 325
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 120
FT /note="R -> H (in Ref. 2; CAA27019)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> A (in Ref. 1; AAA31057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39190 MW; A1F3F13E7958A16C CRC64;
MWPQLLLLLL APRSGHGCQG PELDRELVLA KVRALFLDAL GPPAVTGEGG DPGVRRLPRR
HAVGGFMRRG SEPEEEDVSQ AILFPATGAR CGDEPAAGEL AREAEEGLFT YVFRPSQHTR
SRQVTSAQLW FHTGLDRQGM AAANSSGPLL DLLALSSRGP VAVPMSLGQA PPRWAVLHLA
ASALPLLTHP VLVLLLRCPL CSCSARPEAT PFLVAHTRAR PPSGGERARR STAPLPWPWS
PAALRLLQRP PEEPAVHADC HRASLNISFQ ELGWDRWIVH PPSFIFHYCH GGCGLPTLPN
LPLSVPGAPP TPVQPLLLVP GAQPCCAALP GTMRSLRVRT TSDGGYSFKY ETVPNLLTQH
CACI
