INHA_RAT
ID INHA_RAT Reviewed; 366 AA.
AC P17490;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Inhibin alpha chain;
DE Flags: Precursor;
GN Name=Inha;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2628729; DOI=10.1210/mend-3-12-1914;
RA Feng Z.-M., Li Y.-P., Chen C.-L.C.;
RT "Analysis of the 5'-flanking regions of rat inhibin alpha- and beta-B-
RT subunit genes suggests two different regulatory mechanisms.";
RL Mol. Endocrinol. 3:1914-1925(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3153478; DOI=10.1210/mend-1-8-561;
RA Woodruff T.K., Meunier H., Jones P.B.C., Hsueh A.J.W., Mayo K.E.;
RT "Rat inhibin: molecular cloning of alpha- and beta-subunit complementary
RT deoxyribonucleic acids and expression in the ovary.";
RL Mol. Endocrinol. 1:561-568(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2484214; DOI=10.1210/mend-1-5-388;
RA Esch F.S., Shimasaki S., Cooksey K., Mercado M., Mason A.J., Ying S.-Y.,
RA Ueno N., Ling N.;
RT "Complementary deoxyribonucleic acid (cDNA) cloning and DNA sequence
RT analysis of rat ovarian inhibins.";
RL Mol. Endocrinol. 1:388-396(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=2829170; DOI=10.1073/pnas.85.1.247;
RA Meunier H., Rivier C., Evans R.M., Vale W.;
RT "Gonadal and extragonadal expression of inhibin alpha, beta A, and beta B
RT subunits in various tissues predicts diverse functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:247-251(1988).
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 -!- TISSUE SPECIFICITY: Mainly expressed in ovary and testis. Alpha- and
CC beta-B-subunits are the predominant forms found in testis. Also found
CC in placenta, pituitary, adrenal gland, bone marrow, kidney, spinal cord
CC and brain. {ECO:0000269|PubMed:2829170}.
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; M32755; AAA41437.1; -; Genomic_DNA.
DR EMBL; M32754; AAA41437.1; JOINED; Genomic_DNA.
DR EMBL; M36453; AAA41435.1; -; mRNA.
DR EMBL; BC083564; AAH83564.1; -; mRNA.
DR PIR; A41398; A40056.
DR RefSeq; NP_036722.1; NM_012590.2.
DR AlphaFoldDB; P17490; -.
DR STRING; 10116.ENSRNOP00000027227; -.
DR GlyGen; P17490; 2 sites.
DR PaxDb; P17490; -.
DR Ensembl; ENSRNOT00000027227; ENSRNOP00000027227; ENSRNOG00000020097.
DR GeneID; 24504; -.
DR KEGG; rno:24504; -.
DR UCSC; RGD:2912; rat.
DR CTD; 3623; -.
DR RGD; 2912; Inha.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000005935; -.
DR HOGENOM; CLU_064515_0_0_1; -.
DR InParanoid; P17490; -.
DR OMA; TYVFRPS; -.
DR OrthoDB; 1177863at2759; -.
DR PhylomeDB; P17490; -.
DR TreeFam; TF331531; -.
DR Reactome; R-RNO-209822; Glycoprotein hormones.
DR PRO; PR:P17490; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000020097; Expressed in ovary and 18 other tissues.
DR Genevisible; P17490; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043512; C:inhibin A complex; IDA:RGD.
DR GO; GO:0043513; C:inhibin B complex; IDA:RGD.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:RGD.
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:0034711; F:inhibin binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IMP:RGD.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; IMP:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
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 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_0000033694"
FT PROPEP 64..233
FT /note="Inhibin alpha N-terminal region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033695"
FT CHAIN 234..366
FT /note="Inhibin alpha chain"
FT /id="PRO_0000033696"
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..328
FT /evidence="ECO:0000250"
FT DISULFID 292..363
FT /evidence="ECO:0000250"
FT DISULFID 296..365
FT /evidence="ECO:0000250"
FT DISULFID 327
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 39497 MW; 327A233B9FEDFCDC CRC64;
MVIQPSLLLL LLLTLQDVDS CQGPELVREL VLAKVKALFL DALGPPAMDG EGGGPGIRRL
PRRHALGGFM HRTSEPEEED VSQAILFPAT GATCEDQAAA GGLAQEPEEG LFTYVFRPSQ
HIRSHQVTSA QLWFHTGLDR KSTAASNSSR PLLDLLVLSS GGPMAVPVSL GQSPPRWAVL
HLAASAFPLL THPILVLLLR CPLCSCSGRP ETTPFLVAHT RARAPSAGER ARRSAPSMPW
PWSPAALRLL QRPPEEPSAH AFCHRAALNI SFQELGWDRW IVHPPSFIFH YCHGSCGMPT
SDLPLPVPGA PPTPAQPLFL VPGAKPCCAA LPGSMRSLRV RTTSDGGYSF KYEMVPNLIT
QHCACI
