ID   INHA_TRIVU              Reviewed;         361 AA.
AC   O77755;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Inhibin alpha chain;
DE   Flags: Precursor;
GN   Name=INHA;
OS   Trichosurus vulpecula (Brush-tailed possum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX   NCBI_TaxID=9337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9801457; DOI=10.1677/jme.0.0210141;
RA   Vanmontfort D., Fidler A.E., Heath D.A., Lawrence S.B., Tisdall D.J.,
RA   Greenwood P.J., McNatty K.;
RT   "cDNA sequence analysis, gene expression and protein localisation of the
RT   inhibin alpha subunit of Australian brushtail possum (Trichosurus
RT   vulpecula).";
RL   J. Mol. Endocrinol. 21:141-152(1998).
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.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; AF033340; AAC63945.1; -; mRNA.
DR   AlphaFoldDB; O77755; -.
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; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   PROPEP          22..64
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033699"
FT   PROPEP          65..230
FT                   /note="Inhibin alpha N-terminal region"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033700"
FT   CHAIN           231..361
FT                   /note="Inhibin alpha chain"
FT                   /id="PRO_0000033701"
FT   REGION          45..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            64..65
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            230..231
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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..323
FT                   /evidence="ECO:0000250"
FT   DISULFID        289..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        322
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  38945 MW;  D661CDF93CDAA87D CRC64;
     MLPLLLPLQL LLLMVMKGGH GCQGPELDRE LVLAKVRALV LDALGPPNAS KDGGKPVAQR
     LTRRHAHTGG STRRSMENED EDLSQVILFP TTGPGCEDEP EARAAEGLFT YTFRPSLHTR
     SRQVTAAQLW FHTGLDKVGA EVHNDSGPMV TLLAMSSGGP MAVPILLGPA PPHWAVLHLA
     APAFTLLTRP LLVLLLRCPN CPCPAQLDAT PFLVAHTRAR PPSVGERARR SPLPPPWPWS
     PAALRLLQRP SEDPAAHADC HRAALNISFQ ELGWDQWIVH PPSFIFHYCH GGCGLVPSPV
     LSPGAALTPS QPLPLGPGSR PCCAAMPSTM RPLRVRTTSD GGYSFKYEIV PNLLTQHCAC
     I