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P05111 (INHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibin alpha chain
Gene names
Name:INHA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B.

Subcellular location

Secreted.

Tissue specificity

Originally found in ovary (granulosa cells) and testis (Sertoli cells), but widely distributed in many tissues including brain and placenta. In adrenal cortex expression is limited to the zona reticularis and the innermost zona fasciculata in the normal gland, extending centripetally into the zona fasciculata in hyperplasia. Also found in adrenocortical tumors. Also expressed in prostate epithelium of benign prostatic hyperplasia, in regions of basal cell hyperplasia and in nonmalignant regions of high grade prostate cancer. Only circulating inhibin B is found in male, whereas circulating inhibins A and B are found in female. Ref.9

Post-translational modification

Proteolytic processing yields a number of bioactive forms. The 20/23 kDa forms consist solely of the mature alpha chain, the 26/29 kDa forms consist of the most N-terminal propeptide linked through a disulfide bond to the mature alpha chain, the 50/53 kDa forms encompass the entire proprotein. Each type can be furthermore either mono- or diglycosylated, causing the mass difference. Ref.8

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGrowth factor
Hormone
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Traceable author statement PubMed 12456957. Source: UniProtKB

cell differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

cell surface receptor signaling pathway

Traceable author statement PubMed 12456957. Source: UniProtKB

cell-cell signaling

Traceable author statement PubMed 12456957. Source: UniProtKB

erythrocyte differentiation

Non-traceable author statement PubMed 1310063. Source: UniProtKB

hemoglobin biosynthetic process

Inferred from direct assay PubMed 1310063. Source: UniProtKB

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of B cell differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of cell cycle

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of follicle-stimulating hormone secretion

Non-traceable author statement PubMed 3267209. Source: UniProtKB

negative regulation of interferon-gamma biosynthetic process

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of macrophage differentiation

Traceable author statement PubMed 12456957. Source: UniProtKB

negative regulation of phosphorylation

Traceable author statement PubMed 12456957. Source: UniProtKB

nervous system development

Non-traceable author statement PubMed 10320815. Source: UniProtKB

ovarian follicle development

Non-traceable author statement PubMed 9166111. Source: UniProtKB

positive regulation of follicle-stimulating hormone secretion

Traceable author statement PubMed 12456957. Source: UniProtKB

regulation of cell cycle

Inferred from direct assay PubMed 9032295. Source: HGNC

regulation of cell proliferation

Inferred from direct assay PubMed 9032295. Source: HGNC

response to external stimulus

Traceable author statement PubMed 10320815. Source: UniProtKB

signal transduction

Traceable author statement PubMed 3267209. Source: ProtInc

skeletal system development

Traceable author statement PubMed 10865214. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement PubMed 12456957. Source: UniProtKB

inhibin A complex

Inferred from direct assay PubMed 7890768. Source: HGNC

inhibin-betaglycan-ActRII complex

Inferred from direct assay PubMed 10746731. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

photoreceptor inner segment

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytokine activity

Traceable author statement PubMed 12456957. Source: UniProtKB

growth factor activity

Traceable author statement PubMed 12324653. Source: UniProtKB

hormone activity

Traceable author statement PubMed 12456957. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 9032295. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 6143
PRO_0000033685
Propeptide62 – 232171Inhibin alpha N-terminal region
PRO_0000033686
Chain233 – 366134Inhibin alpha chain
PRO_0000033687

Sites

Site61 – 622Cleavage
Site232 – 2332Cleavage

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Ref.8
Glycosylation3021N-linked (GlcNAc...); partial Ref.8
Disulfide bond262 ↔ 328 By similarity
Disulfide bond291 ↔ 363 By similarity
Disulfide bond295 ↔ 365 By similarity
Disulfide bond327Interchain By similarity

Natural variations

Natural variant2271G → R.
Corresponds to variant rs12720061 [ dbSNP | Ensembl ].
VAR_034016
Natural variant2571A → T Either a rare polymorphism or may play a role in premature ovarian failure. Ref.10
Corresponds to variant rs12720062 [ dbSNP | Ensembl ].
VAR_015110

Experimental info

Mutagenesis56 – 572RR → AA: Loss of cleavage; when associated with 60-AA-61.
Mutagenesis60 – 612RR → AA: Loss of cleavage; when associated with 55-AA-56.
Mutagenesis231 – 2322RR → EA: Loss of cleavage.
Mutagenesis2681N → Q: Loss of glycosylation.
Mutagenesis3021N → Q: Loss of glycosylation.
Sequence conflict171H → V Ref.7
Sequence conflict191C → S Ref.7

Sequences

Sequence LengthMass (Da)Tools
P05111 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 0E03D2AB12BF8E57

FASTA36639,670
        10         20         30         40         50         60 
MVLHLLLFLL LTPQGGHSCQ GLELARELVL AKVRALFLDA LGPPAVTREG GDPGVRRLPR 

        70         80         90        100        110        120 
RHALGGFTHR GSEPEEEEDV SQAILFPATD ASCEDKSAAR GLAQEAEEGL FRYMFRPSQH 

       130        140        150        160        170        180 
TRSRQVTSAQ LWFHTGLDRQ GTAASNSSEP LLGLLALSPG GPVAVPMSLG HAPPHWAVLH 

       190        200        210        220        230        240 
LATSALSLLT HPVLVLLLRC PLCTCSARPE ATPFLVAHTR TRPPSGGERA RRSTPLMSWP 

       250        260        270        280        290        300 
WSPSALRLLQ RPPEEPAAHA NCHRVALNIS FQELGWERWI VYPPSFIFHY CHGGCGLHIP 

       310        320        330        340        350        360 
PNLSLPVPGA PPTPAQPYSL LPGAQPCCAA LPGTMRPLHV RTTSDGGYSF KYETVPNLLT 


QHCACI 

« Hide

References

« Hide 'large scale' references
[1]"Inhibin A-subunit cDNAs from porcine ovary and human placenta."
Mayo K.E., Cerelli G.M., Spiess J., Rivier J., Rosenfeld M.G., Evans R.M., Vale W.
Proc. Natl. Acad. Sci. U.S.A. 83:5849-5853(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human inhibin genes. Genomic characterisation and sequencing."
Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.
FEBS Lett. 206:329-334(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Structure of two human ovarian inhibins."
Mason A.J., Niall H.D., Seeburg P.H.
Biochem. Biophys. Res. Commun. 135:957-964(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-366.
[8]"Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A."
Mason A.J., Farnworth P.G., Sullivan J.
Mol. Endocrinol. 10:1055-1065(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-268 AND ASN-302, MUTAGENESIS.
[9]"Loss of the expression and localization of inhibin alpha-subunit in high grade prostate cancer."
Mellor S.L., Richards M.G., Pedersen J.S., Robertson D.M., Risbridger G.P.
J. Clin. Endocrinol. Metab. 83:969-975(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[10]"Inhibin: a candidate gene for premature ovarian failure."
Shelling A.N., Burton K.A., Chand A.L., van Ee C.C., France J.T., Farquhar C.M., Milsom S.R., Love D.R., Gersak K., Aittomaki K., Winship I.M.
Hum. Reprod. 15:2644-2649(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-257.
+Additional computationally mapped references.

Web resources

Wikipedia

Inhibin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13981 mRNA. Translation: AAA59166.1.
X04445, X04446 Genomic DNA. Translation: CAA28040.1.
BT006954 mRNA. Translation: AAP35600.1.
AK292340 mRNA. Translation: BAF85029.1.
CH471063 Genomic DNA. Translation: EAW70774.1.
BC006391 mRNA. Translation: AAH06391.1.
M13144 mRNA. Translation: AAA59167.1.
PIRA24248. A23556.
RefSeqNP_002182.1. NM_002191.3.
UniGeneHs.407506.

3D structure databases

ProteinModelPortalP05111.
SMRP05111. Positions 261-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109835. 1 interaction.
DIPDIP-5826N.
STRING9606.ENSP00000243786.

PTM databases

PhosphoSiteP05111.

Polymorphism databases

DMDM124274.

Proteomic databases

PaxDbP05111.
PRIDEP05111.

Protocols and materials databases

DNASU3623.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243786; ENSP00000243786; ENSG00000123999.
GeneID3623.
KEGGhsa:3623.
UCSCuc002vmk.2. human.

Organism-specific databases

CTD3623.
GeneCardsGC02P220433.
HGNCHGNC:6065. INHA.
HPACAB000047.
HPA019141.
MIM147380. gene.
neXtProtNX_P05111.
PharmGKBPA29876.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289440.
HOGENOMHOG000013165.
HOVERGENHBG052131.
InParanoidP05111.
KOK05500.
OMAGGYSFKY.
OrthoDBEOG7BS4BB.
PhylomeDBP05111.
TreeFamTF331531.

Gene expression databases

BgeeP05111.
CleanExHS_INHA.
GenevestigatorP05111.

Family and domain databases

InterProIPR002405. Inhibin_asu.
IPR017175. Inhibin_asu_subgr.
IPR001839. TGF-b_C.
IPR017948. TGFb_CS.
[Graphical view]
PfamPF00019. TGF_beta. 1 hit.
[Graphical view]
PIRSFPIRSF037328. Inhibin_alpha_subunit. 1 hit.
PRINTSPR00669. INHIBINA.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiINHA.
GenomeRNAi3623.
NextBio14177.
PROP05111.
SOURCESearch...

Entry information

Entry nameINHA_HUMAN
AccessionPrimary (citable) accession number: P05111
Secondary accession number(s): A8K8H5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM