ID   INHA_SHEEP              Reviewed;         265 AA.
AC   P38440;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Inhibin alpha chain;
DE   Flags: Precursor; Fragment;
GN   Name=INHA;
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].
RC   TISSUE=Ovary;
RA   Sadanandan S.L., Jeyaseelan K.;
RL   Submitted (FEB-1994) 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 {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; L28815; AAA31553.1; -; mRNA.
DR   AlphaFoldDB; P38440; -.
DR   STRING; 9940.ENSOARP00000021737; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   Proteomes; UP000002356; 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   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.
FT   PROPEP          <1..131
FT                   /note="Inhibin alpha N-terminal region"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033697"
FT   CHAIN           132..265
FT                   /note="Inhibin alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033698"
FT   SITE            131..132
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..264
FT                   /evidence="ECO:0000250"
FT   DISULFID        226
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   265 AA;  28754 MW;  D880E9AB156B6656 CRC64;
     DAGEAEEGLF TYVFQPSQHT RSRQVTSAQL WFHTGLDRQE TAAANSSEPL LGLLVLTSGG
     PMPVPMSLGQ APPRWAVLHL ATSAFPLLTH PVLALLLRCP LCSCSARPEA TPFLVAHTRA
     KPPSGGERAR RSTPPLPWPW SPAALRLLQR PPEEPAAHAD CHRAALNISF QELGWDRWIV
     HPPSFIFYYC HGGCGLPTLQ DLPLPVPGVP PTPFQPLSLV PGAQACCAAL PGTMRPLRVR
     TTSDGGYSFK YEMVPNLLTQ HCACI