ID   INHA_CHICK              Reviewed;         329 AA.
AC   P43031; Q90708;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Inhibin alpha chain;
DE   Flags: Precursor;
GN   Name=INHA;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=White leghorn; TISSUE=Ovarian granulosa cell;
RX   PubMed=8399835; DOI=10.1095/biolreprod49.3.453;
RA   Wang S.Y., Johnson P.A.;
RT   "Complementary deoxyribonucleic acid cloning and sequence analysis of the
RT   alpha-subunit of inhibin from chicken ovarian granulosa cells.";
RL   Biol. Reprod. 49:453-458(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Johnson P.A., Chen C.C.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U48438; AAA92569.1; -; Genomic_DNA.
DR   PIR; I51215; I51215.
DR   RefSeq; NP_001026428.1; NM_001031257.1.
DR   AlphaFoldDB; P43031; -.
DR   STRING; 9031.ENSGALP00000018301; -.
DR   PaxDb; P43031; -.
DR   PRIDE; P43031; -.
DR   GeneID; 424197; -.
DR   KEGG; gga:424197; -.
DR   CTD; 3623; -.
DR   VEuPathDB; HostDB:geneid_424197; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_064515_0_0_1; -.
DR   InParanoid; P43031; -.
DR   OrthoDB; 1177863at2759; -.
DR   PhylomeDB; P43031; -.
DR   PRO; PR:P43031; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Growth factor; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..60
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033679"
FT   PROPEP          61..216
FT                   /note="Inhibin alpha N-terminal region"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033680"
FT   CHAIN           217..329
FT                   /note="Inhibin alpha chain"
FT                   /id="PRO_0000033681"
FT   SITE            60..61
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            216..217
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        242..291
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..326
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..328
FT                   /evidence="ECO:0000250"
FT   DISULFID        290
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  35853 MW;  AE331687109A25A1 CRC64;
     MLLLLHLLPA VLPASALGSC TGAGADRQLV LAKVRARVLE HLSPPAMQEP QKDVRRVHRR
     DVLEEVEVPP EEQEDTSQVI LFPSTDVPCE PTQPDKLLEE EGIFTYLFQP SAHALSRTLT
     SAQLWFYSGP SAAPNHSAPA VLTLSPQGRV PVVATASRTP EHWTVFDFGP DALPQLAQPL
     FVLLVRCPGC PCLADGDKMP FLVATTRAKA AGRARRSAVP WSPAALSLLQ RPSEDVAAHT
     NCRRASLNIS FEELGWDNWI VHPSSFVFHY CHGNCAEGHG LSHRLGVQLC CAALPGTMRS
     LRVRTTSDGG YSFKYETVPN ILAQDCTCV