INHBB_PIG
ID INHBB_PIG Reviewed; 407 AA.
AC P04088; Q8MIM0;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Inhibin beta B chain;
DE AltName: Full=Activin beta-B chain;
DE Flags: Precursor;
GN Name=INHBB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nonneman D.J., Rohrer G.A.;
RT "Molecular cloning of the porcine inhibin-beta B precursor subunit gene and
RT reassignment to chromosome 15.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-407.
RC TISSUE=Ovarian follicular fluid;
RX PubMed=2417121; DOI=10.1038/318659a0;
RA Mason A.J., Hayflick J.S., Ling N., Esch F., Ueno N., Ying S.-Y.,
RA Guillemin R., Niall H., Seeburg P.H.;
RT "Complementary DNA sequences of ovarian follicular fluid inhibin show
RT precursor structure and homology with transforming growth factor-beta.";
RL Nature 318:659-663(1985).
RN [3]
RP PROTEIN SEQUENCE OF 293-307.
RX PubMed=1644823; DOI=10.1016/s0021-9258(18)42014-5;
RA Nakamura T., Asashima M., Eto Y., Takio K., Uchiyama H., Moriya N.,
RA Ariizumi T., Yashiro T., Sugino K., Titani K., Sugino H.;
RT "Isolation and characterization of native activin B.";
RL J. Biol. Chem. 267:16385-16389(1992).
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 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. Interacts with FST and
CC FSTL3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AY116585; AAM66766.1; -; Genomic_DNA.
DR EMBL; X03267; CAA27021.1; -; mRNA.
DR PIR; A01394; WFPGBB.
DR RefSeq; NP_001158314.1; NM_001164842.1.
DR AlphaFoldDB; P04088; -.
DR SMR; P04088; -.
DR PRIDE; P04088; -.
DR GeneID; 397490; -.
DR KEGG; ssc:397490; -.
DR CTD; 3625; -.
DR InParanoid; P04088; -.
DR OrthoDB; 1385831at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0032686; P:negative regulation of hepatocyte growth factor production; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000381; Inhibin_betaB.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR PANTHER; PTHR11848:SF29; PTHR11848:SF29; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..292
FT /evidence="ECO:0000269|PubMed:1644823"
FT /id="PRO_0000033726"
FT CHAIN 293..407
FT /note="Inhibin beta B chain"
FT /id="PRO_0000033727"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..304
FT /evidence="ECO:0000250"
FT DISULFID 303..372
FT /evidence="ECO:0000250"
FT DISULFID 332..404
FT /evidence="ECO:0000250"
FT DISULFID 336..406
FT /evidence="ECO:0000250"
FT DISULFID 371
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 59..64
FT /note="GGFRRP -> RAAGAE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="V -> G (in Ref. 2; CAA27021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 45038 MW; EBC0D72F2A210008 CRC64;
MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPSPAAPP PPPPPGALGG SQDTCTSCGG
FRRPEELGRL DGDFLEAVKR HILNRLQMRG RPNITHAVPK AAMVTALRKL HAGKVREDGR
VEIPHLDGHA SPGADGQERV SEIISFAETD GLASSRVRLY FFISNEGNQN LFVVQASLWL
YLKLLPYVLE KGSRRKVRVK VYFQEPGHGD RWDVVEKRVD LKRSGWHTLP LTEAIQALFE
RGERRLNLDV QCDGCQELAV VPVFVDPGEE SHRPFVVVQA RLVDSRHRIR KRGLECDGRT
NLCCRQQFFI DFRLIGWSDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF HTAVVNQYRM
RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI VEECGCA
