INHBA_CHICK
ID INHBA_CHICK Reviewed; 424 AA.
AC P27092; Q90697;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Inhibin beta A chain;
DE AltName: Full=Activin beta-A chain;
DE Flags: Precursor;
GN Name=INHBA;
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 [MRNA].
RC STRAIN=White leghorn;
RA Huang J.X.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=8788196; DOI=10.1095/biolreprod54.2.429;
RA Chen C.C., Johnson P.A.;
RT "Molecular cloning of inhibin/activin beta A-subunit complementary
RT deoxyribonucleic acid and expression of inhibin/activin alpha- and beta A-
RT subunits in the domestic hen.";
RL Biol. Reprod. 54:429-435(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 317-349.
RC TISSUE=Hypoblast;
RX PubMed=2225063; DOI=10.1016/0092-8674(90)90446-l;
RA Mitrani E., Ziv T., Thomsen G., Shimoni Y., Melton D.A., Bril A.;
RT "Activin can induce the formation of axial structures and is expressed in
RT the hypoblast of the chick.";
RL Cell 63:495-501(1990).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7576634; DOI=10.1016/0896-6273(95)90176-0;
RA Darland D.C., Link B.A., Nishi R.;
RT "Activin A and follistatin expression in developing targets of ciliary
RT ganglion neurons suggests a role in regulating neurotransmitter
RT phenotype.";
RL Neuron 15:857-866(1995).
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 Induces somatostatin in the ciliary ganglion neurons and may play a
CC role in regulating neurotransmitter phenotype.
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 Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B.
CC Activin AB is a dimer of beta-A and beta-B.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Ciliary ganglion neurons. Levels are higher in the
CC choroid than the iris.
CC -!- DEVELOPMENTAL STAGE: Levels increase in the iris from embryonic day 9
CC (E9) to E16 and in the choroid, levels are high from E9 to E14 but drop
CC at E16.
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; U26946; AAA68174.1; -; mRNA.
DR EMBL; U42377; AAC59738.1; -; mRNA.
DR EMBL; M61167; AAA48569.1; -; mRNA.
DR EMBL; M57407; AAA03080.1; -; mRNA.
DR PIR; B36193; B36193.
DR RefSeq; NP_990727.1; NM_205396.1.
DR RefSeq; XP_015136806.1; XM_015281320.1.
DR AlphaFoldDB; P27092; -.
DR SMR; P27092; -.
DR STRING; 9031.ENSGALP00000036647; -.
DR PaxDb; P27092; -.
DR PRIDE; P27092; -.
DR GeneID; 396361; -.
DR KEGG; gga:396361; -.
DR CTD; 3624; -.
DR VEuPathDB; HostDB:geneid_396361; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; P27092; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; P27092; -.
DR PRO; PR:P27092; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0043509; C:activin A complex; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043512; C:inhibin A complex; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; NAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0042701; P:progesterone secretion; ISS:UniProtKB.
DR GO; GO:0046880; P:regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
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; IPR000491; Inhibin_betaA.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PRINTS; PR00670; INHIBINBA.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..308
FT /evidence="ECO:0000250"
FT /id="PRO_0000033704"
FT CHAIN 309..424
FT /note="Inhibin beta A chain"
FT /id="PRO_0000033705"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 312..320
FT /evidence="ECO:0000250"
FT DISULFID 319..389
FT /evidence="ECO:0000250"
FT DISULFID 348..421
FT /evidence="ECO:0000250"
FT DISULFID 352..423
FT /evidence="ECO:0000250"
FT DISULFID 388
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 33
FT /note="A -> T (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="T -> I (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> G (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> T (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="Q -> K (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="E -> R (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="E -> G (in Ref. 2; AAC59738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47574 MW; 96E158FE119E1D69 CRC64;
MPLLWKRGFL LVICWIIVRS SPTPGSEGHS SVADCPSCAL TTLSKDVPSS QPEMVEAVKK
HILNMLHLRD RPNITQPVPK AALLNATKKL HVGKVGDDGY VEIEDDVGRR AEMNEVVEQT
SEIITFAESG TPKKTLHFEI SKEGSELSVV EHAEVWLFLK VSKANRSRTK VTIRLFQQQR
QPKGNSEAAE DMEDMGLKGE RSETLISEKA VDARKSTWHI FPISSSVQRL LDQGQSSLDV
RIACDLCQET GASLVLLGKK KKKEDDGEGK EKDGGELTGE EEKEQSHRPF LMMLARHSED
RQHRRRERGL ECDGKVNICC KKQFFVSFKD IGWSDWIIAP TGYHANYCEE ECPSHIAGTS
GSSLSFHSTV INHYRMRGHS PFANLKSCCV PTKLRPMSML YYDDGQNIIK KDIQNMIVEE
CGCS
