INHA_HORSE
ID INHA_HORSE Reviewed; 367 AA.
AC P55101; Q28370;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Inhibin alpha chain;
DE Flags: Precursor;
GN Name=INHA;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=8593300; DOI=10.1292/jvms.57.905;
RA Yamanouchi K., Yoshida S., Hasegawa T., Ikeda A., Chang K.T., Matsuyama S.,
RA Nishihara M., Miyazawa K., Takahashi M.;
RT "Molecular cloning of DNA for inhibin alpha-subunit from equine ovary.";
RL J. Vet. Med. Sci. 57:905-909(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 98-367.
RC TISSUE=Testis;
RA Adams M.H., Baker C.B., McDowell K.J.;
RT "Molecular cloning and sequencing of equine inhibin alpha cDNA.";
RL Anim. Biotechnol. 7:1-9(1996).
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; D50327; BAA08863.1; -; mRNA.
DR EMBL; U21219; AAB00874.1; -; mRNA.
DR RefSeq; NP_001075379.2; NM_001081910.2.
DR AlphaFoldDB; P55101; -.
DR STRING; 9796.ENSECAP00000013503; -.
DR PaxDb; P55101; -.
DR PeptideAtlas; P55101; -.
DR GeneID; 100034077; -.
DR KEGG; ecb:100034077; -.
DR CTD; 3623; -.
DR InParanoid; P55101; -.
DR OrthoDB; 1177863at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Growth factor; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..63
FT /evidence="ECO:0000250"
FT /id="PRO_0000033682"
FT PROPEP 64..233
FT /note="Inhibin alpha N-terminal region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033683"
FT CHAIN 234..367
FT /note="Inhibin alpha chain"
FT /id="PRO_0000033684"
FT SITE 63..64
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 233..234
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 263..329
FT /evidence="ECO:0000250"
FT DISULFID 292..364
FT /evidence="ECO:0000250"
FT DISULFID 296..366
FT /evidence="ECO:0000250"
FT DISULFID 328
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 105
FT /note="Q -> R (in Ref. 2; AAB00874)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> R (in Ref. 2; AAB00874)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="C -> R (in Ref. 2; AAB00874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39423 MW; DC8A6EB2C84B2C61 CRC64;
MVPPLPLLLL LLLVPQGGHG CQGSELDREI VLAKVRALFL DALGPPAVTG EGGDPGVRRL
PRRHALGGFA RRGSEPEEED VSQAILFPAS GSRCEDEPAA GELAQEAEQG LFTYMFRPSQ
HMRSRQVTSA HLWFHTGLDR QGTAASNSSE PLLGLLALSS GGPMAVPVTL GQAPPCWAVL
HLAASALPLL THPVLVLLLR CPLCSCSARP EATPFLVAHT RARPPSGGER TRRSTPPLPW
PWSPAALRLL QRPPEEPAAH ANCHRAALNI SFQELGWDRW IVHPRSFIFH YCHGGCGLSA
PPDLPLPVPE VPPTPIQPLS LVPGAQPCCA ALPGTMRPLR VRTTSDGGYS FKYEIVPNLL
TQHCACI
