P17491 (INHBB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibin beta B chain

Alternative name(s):
Activin beta-B chain

Gene names

Name:

Inhbb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subunit structure	Homodimer or heterodimer; disulfide-linked. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3 By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Alpha- and beta-B subunits are the predominant forms found in rat testis. Also expressed in ovary.
Induction	Increased expression in methimazole-induced goiter.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Growth factor Hormone
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cellular response to cholesterol Inferred from direct assay PubMed 19464342. Source: UniProtKB cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to starvation Inferred from sequence or structural similarity. Source: UniProtKB fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB growth Inferred from electronic annotation. Source: InterPro negative regulation of follicle-stimulating hormone secretion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of hepatocyte growth factor biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of insulin secretion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of follicle-stimulating hormone secretion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ovulation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Propeptide	29 – 296	268	Potential		PRO_0000033728
	Chain	297 – 411	115	Inhibin beta B chain		PRO_0000033729
Regions
	Compositional bias	30 – 48	19	Pro-rich
	Compositional bias	59 – 64	6	Poly-Gly
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Disulfide bond	300 ↔ 308		By similarity
	Disulfide bond	307 ↔ 376		By similarity
	Disulfide bond	336 ↔ 408		By similarity
	Disulfide bond	340 ↔ 410		By similarity
	Disulfide bond	375		Interchain By similarity
Natural variations
	Natural variant	270	1	D → H in beta-B20. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P17491 [UniParc]. Last modified November 9, 2004. Version 2. Checksum: 85D4D4CAD9D74620	FASTA	411	45,183
	10 20 30 40 50 60 MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPSPAAPP PPPPPGAPGG SQDTCTSCGG 70 80 90 100 110 120 GGGGFRRPEE LGRVDGDFLE AVKRHILSRL QLRGRPNITH AVPKAAMVTA LRKLHAGKVR 130 140 150 160 170 180 EDGRVEIPHL DGHASPGADG QERVSEIISF AETDGLASSR VRLYFFVSNE GNQNLFVVQA 190 200 210 220 230 240 SLWLYLKLLP YVLEKGSRRK VRVKVYFQEQ GHGDRWNVVE KKVDLKRSGW HTFPITEAIQ 250 260 270 280 290 300 ALFERGERRL NLDVQCDSCQ ELAVVPVFVD PGEESHRPFV VVQARLGDSR HRIRKRGLEC 310 320 330 340 350 360 DGRTSLCCRQ QFFIDFRLIG WNDWIIAPTG YYGNYCEGSC PAYLAGVPGS ASSFHTAVVN 370 380 390 400 410 QYRMRGLNPG PVNSCCIPTK LSSMSMLYFD DEYNIVKRDV PNMIVEECGC A

References

[1]	"Analysis of the 5'-flanking regions of rat inhibin alpha- and beta-B-subunit genes suggests two different regulatory mechanisms." Feng Z.-M., Li Y.-P., Chen C.-L.C. Mol. Endocrinol. 3:1914-1925(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-174. Tissue: Liver.
[2]	"Two messenger ribonucleic acids encoding the common beta B-chain of inhibin and activin have distinct 5'-initiation sites and are differentially regulated in rat granulosa cells." Dykema J.C., Mayo K.E. Endocrinology 135:702-711(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-7. Tissue: Granulocyte.
[3]	"Complementary deoxyribonucleic acid (cDNA) cloning and DNA sequence analysis of rat ovarian inhibins." Esch F.S., Shimasaki S., Cooksey K., Mercado M., Mason A.J., Ying S.-Y., Ueno N., Ling N. Mol. Endocrinol. 1:388-396(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 133-411, VARIANT BETA-B20 HIS-270. Tissue: Ovary.
[4]	"Activin betaB expression in rat experimental goiter and human thyroid tumors." Matsuo S.E., Ebina K.N., Kulcsar M.A., Friguglietti C.U., Kimura E.T. Thyroid 13:239-247(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 158-266. Strain: Wistar. Tissue: Thyroid.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32757, M32756 Genomic DNA. Translation: AAA41438.1. AF478684 mRNA. Translation: AAM46787.1.
IPI	IPI00188355.
PIR	B41398.
RefSeq	NP_542949.1. NM_080771.1.
UniGene	Rn.35074.
3D structure databases
ProteinModelPortal	P17491.
SMR	P17491. Positions 297-411.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000003302.
Proteomic databases
PaxDb	P17491.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25196.
KEGG	rno:25196.
Organism-specific databases
CTD	3625.
RGD	2913. Inhbb.
Phylogenomic databases
eggNOG	NOG278663.
HOGENOM	HOG000220890.
HOVERGEN	HBG105613.
InParanoid	P17491.
KO	K04667.
OMA	FVVVQAR.
OrthoDB	EOG42JNRM.
Gene expression databases
Genevestigator	P17491.
GermOnline	ENSRNOG00000002439. Rattus norvegicus.
Family and domain databases
InterPro	IPR000381. Inhibin_betaB. IPR001839. TGF-b_C. IPR001111. TGF-b_N. IPR015615. TGF-beta-rel. IPR017948. TGFb_CS. [Graphical view]
PANTHER	PTHR11848. PTHR11848. 1 hit. PTHR11848:SF29. PTHR11848:SF29. 1 hit.
Pfam	PF00019. TGF_beta. 1 hit. PF00688. TGFb_propeptide. 1 hit. [Graphical view]
PRINTS	PR00671. INHIBINBB.
SMART	SM00204. TGFB. 1 hit. [Graphical view]
PROSITE	PS00250. TGF_BETA_1. 1 hit. PS51362. TGF_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	605709.

Entry information

Entry name

INHBB_RAT

Accession

Primary (citable) accession number: P17491
Secondary accession number(s): Q8K471

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 9, 2004
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program