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Protein

Inhibin alpha chain

Gene

INHA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 622Cleavage
Sitei232 – 2332Cleavage

GO - Molecular functioni

  1. cytokine activity Source: UniProtKB
  2. growth factor activity Source: UniProtKB
  3. hormone activity Source: UniProtKB
  4. receptor binding Source: HGNC
  5. transforming growth factor beta receptor binding Source: GO_Central

GO - Biological processi

  1. cell-cell signaling Source: UniProtKB
  2. cell cycle arrest Source: UniProtKB
  3. cell development Source: GO_Central
  4. cell differentiation Source: UniProtKB
  5. cell surface receptor signaling pathway Source: UniProtKB
  6. erythrocyte differentiation Source: UniProtKB
  7. hemoglobin biosynthetic process Source: UniProtKB
  8. male gonad development Source: Ensembl
  9. negative regulation of B cell differentiation Source: UniProtKB
  10. negative regulation of cell cycle Source: UniProtKB
  11. negative regulation of follicle-stimulating hormone secretion Source: UniProtKB
  12. negative regulation of interferon-gamma biosynthetic process Source: UniProtKB
  13. negative regulation of macrophage differentiation Source: UniProtKB
  14. negative regulation of phosphorylation Source: UniProtKB
  15. nervous system development Source: UniProtKB
  16. ovarian follicle development Source: UniProtKB
  17. positive regulation of follicle-stimulating hormone secretion Source: UniProtKB
  18. positive regulation of pathway-restricted SMAD protein phosphorylation Source: GO_Central
  19. regulation of apoptotic process Source: GO_Central
  20. regulation of cell cycle Source: HGNC
  21. regulation of cell proliferation Source: HGNC
  22. regulation of MAPK cascade Source: GO_Central
  23. response to external stimulus Source: UniProtKB
  24. signal transduction Source: ProtInc
  25. skeletal system development Source: ProtInc
  26. SMAD protein signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Hormone

Enzyme and pathway databases

ReactomeiREACT_15398. Glycoprotein hormones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibin alpha chain
Gene namesi
Name:INHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6065. INHA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. inhibin A complex Source: HGNC
  3. inhibin-betaglycan-ActRII complex Source: BHF-UCL
  4. neuronal cell body Source: Ensembl
  5. photoreceptor inner segment Source: Ensembl
  6. photoreceptor outer segment Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 572RR → AA: Loss of cleavage; when associated with 60-AA-61. 1 Publication
Mutagenesisi60 – 612RR → AA: Loss of cleavage; when associated with 55-AA-56. 1 Publication
Mutagenesisi231 – 2322RR → EA: Loss of cleavage. 1 Publication
Mutagenesisi268 – 2681N → Q: Loss of glycosylation. 1 Publication
Mutagenesisi302 – 3021N → Q: Loss of glycosylation. 1 Publication

Organism-specific databases

PharmGKBiPA29876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 6143PRO_0000033685Add
BLAST
Propeptidei62 – 232171Inhibin alpha N-terminal regionPRO_0000033686Add
BLAST
Chaini233 – 366134Inhibin alpha chainPRO_0000033687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi262 ↔ 328By similarity
Glycosylationi268 – 2681N-linked (GlcNAc...)1 Publication
Disulfide bondi291 ↔ 363By similarity
Disulfide bondi295 ↔ 365By similarity
Glycosylationi302 – 3021N-linked (GlcNAc...); partial1 Publication
Disulfide bondi327 – 327InterchainBy similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP05111.
PRIDEiP05111.

PTM databases

PhosphoSiteiP05111.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP05111.
CleanExiHS_INHA.
GenevestigatoriP05111.

Organism-specific databases

HPAiCAB000047.
HPA019141.
HPA048834.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi109835. 6 interactions.
DIPiDIP-5826N.
STRINGi9606.ENSP00000243786.

Structurei

3D structure databases

ProteinModelPortaliP05111.
SMRiP05111. Positions 261-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG289440.
GeneTreeiENSGT00390000005935.
HOGENOMiHOG000013165.
HOVERGENiHBG052131.
InParanoidiP05111.
KOiK05500.
OMAiGGYSFKY.
OrthoDBiEOG7BS4BB.
PhylomeDBiP05111.
TreeFamiTF331531.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR002405. Inhibin_asu.
IPR017175. Inhibin_asu_subgr.
IPR001839. TGF-b_C.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF037328. Inhibin_alpha_subunit. 1 hit.
PRINTSiPR00669. INHIBINA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLHLLLFLL LTPQGGHSCQ GLELARELVL AKVRALFLDA LGPPAVTREG
60 70 80 90 100
GDPGVRRLPR RHALGGFTHR GSEPEEEEDV SQAILFPATD ASCEDKSAAR
110 120 130 140 150
GLAQEAEEGL FRYMFRPSQH TRSRQVTSAQ LWFHTGLDRQ GTAASNSSEP
160 170 180 190 200
LLGLLALSPG GPVAVPMSLG HAPPHWAVLH LATSALSLLT HPVLVLLLRC
210 220 230 240 250
PLCTCSARPE ATPFLVAHTR TRPPSGGERA RRSTPLMSWP WSPSALRLLQ
260 270 280 290 300
RPPEEPAAHA NCHRVALNIS FQELGWERWI VYPPSFIFHY CHGGCGLHIP
310 320 330 340 350
PNLSLPVPGA PPTPAQPYSL LPGAQPCCAA LPGTMRPLHV RTTSDGGYSF
360
KYETVPNLLT QHCACI
Length:366
Mass (Da):39,670
Last modified:August 12, 1987 - v1
Checksum:i0E03D2AB12BF8E57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171H → V (PubMed:3754442).Curated
Sequence conflicti19 – 191C → S (PubMed:3754442).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → L Found in a patient with early-onset epithelial ovarian tumor; unknown pathological significance; alters the ratio of secreted activins and ihibins. 1 Publication
VAR_072639
Natural varianti227 – 2271G → R.
Corresponds to variant rs12720061 [ dbSNP | Ensembl ].
VAR_034016
Natural varianti257 – 2571A → T Polymorphism; may play a role in premature ovarian failure. 1 Publication
Corresponds to variant rs12720062 [ dbSNP | Ensembl ].
VAR_015110

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2444.1.
PIRiA23556. A24248.
RefSeqiNP_002182.1. NM_002191.3.
UniGeneiHs.407506.

Genome annotation databases

EnsembliENST00000243786; ENSP00000243786; ENSG00000123999.
GeneIDi3623.
KEGGihsa:3623.
UCSCiuc002vmk.2. human.

Polymorphism databases

DMDMi124274.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Inhibin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2444.1.
PIRiA23556. A24248.
RefSeqiNP_002182.1. NM_002191.3.
UniGeneiHs.407506.

3D structure databases

ProteinModelPortaliP05111.
SMRiP05111. Positions 261-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109835. 6 interactions.
DIPiDIP-5826N.
STRINGi9606.ENSP00000243786.

PTM databases

PhosphoSiteiP05111.

Polymorphism databases

DMDMi124274.

Proteomic databases

PaxDbiP05111.
PRIDEiP05111.

Protocols and materials databases

DNASUi3623.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243786; ENSP00000243786; ENSG00000123999.
GeneIDi3623.
KEGGihsa:3623.
UCSCiuc002vmk.2. human.

Organism-specific databases

CTDi3623.
GeneCardsiGC02P220433.
HGNCiHGNC:6065. INHA.
HPAiCAB000047.
HPA019141.
HPA048834.
MIMi147380. gene.
neXtProtiNX_P05111.
PharmGKBiPA29876.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289440.
GeneTreeiENSGT00390000005935.
HOGENOMiHOG000013165.
HOVERGENiHBG052131.
InParanoidiP05111.
KOiK05500.
OMAiGGYSFKY.
OrthoDBiEOG7BS4BB.
PhylomeDBiP05111.
TreeFamiTF331531.

Enzyme and pathway databases

ReactomeiREACT_15398. Glycoprotein hormones.

Miscellaneous databases

GeneWikiiINHA.
GenomeRNAii3623.
NextBioi14177.
PROiP05111.
SOURCEiSearch...

Gene expression databases

BgeeiP05111.
CleanExiHS_INHA.
GenevestigatoriP05111.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR002405. Inhibin_asu.
IPR017175. Inhibin_asu_subgr.
IPR001839. TGF-b_C.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF037328. Inhibin_alpha_subunit. 1 hit.
PRINTSiPR00669. INHIBINA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(1985) [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 (SEP-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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. 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(1995) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  10. Cited for: VARIANT THR-257.
  11. Cited for: VARIANT LEU-60, CHARACTERIZATION OF VARIANT LEU-60.

Entry informationi

Entry nameiINHA_HUMAN
AccessioniPrimary (citable) accession number: P05111
Secondary accession number(s): A8K8H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 12, 1987
Last sequence update: August 12, 1987
Last modified: March 31, 2015
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.