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P05111

- INHA_HUMAN

UniProt

P05111 - INHA_HUMAN

Protein

Inhibin alpha chain

Gene

INHA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. receptor binding Source: HGNC

    GO - Biological processi

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

    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: 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

    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.

    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. 1 interaction.
    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.
    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

    MVLHLLLFLL LTPQGGHSCQ GLELARELVL AKVRALFLDA LGPPAVTREG    50
    GDPGVRRLPR RHALGGFTHR GSEPEEEEDV SQAILFPATD ASCEDKSAAR 100
    GLAQEAEEGL FRYMFRPSQH TRSRQVTSAQ LWFHTGLDRQ GTAASNSSEP 150
    LLGLLALSPG GPVAVPMSLG HAPPHWAVLH LATSALSLLT HPVLVLLLRC 200
    PLCTCSARPE ATPFLVAHTR TRPPSGGERA RRSTPLMSWP WSPSALRLLQ 250
    RPPEEPAAHA NCHRVALNIS FQELGWERWI VYPPSFIFHY CHGGCGLHIP 300
    PNLSLPVPGA PPTPAQPYSL LPGAQPCCAA LPGTMRPLHV RTTSDGGYSF 350
    KYETVPNLLT QHCACI 366
    Length:366
    Mass (Da):39,670
    Last modified:August 13, 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 varianti227 – 2271G → R.
    Corresponds to variant rs12720061 [ dbSNP | Ensembl ].
    VAR_034016
    Natural varianti257 – 2571A → T Either a rare polymorphism or may play a role in premature ovarian failure. 1 Publication
    Corresponds to variant rs12720062 [ dbSNP | Ensembl ].
    VAR_015110

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2444.1.
    PIRi A23556. A24248.
    RefSeqi NP_002182.1. NM_002191.3.
    UniGenei Hs.407506.

    3D structure databases

    ProteinModelPortali P05111.
    SMRi P05111. Positions 261-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109835. 1 interaction.
    DIPi DIP-5826N.
    STRINGi 9606.ENSP00000243786.

    PTM databases

    PhosphoSitei P05111.

    Polymorphism databases

    DMDMi 124274.

    Proteomic databases

    PaxDbi P05111.
    PRIDEi P05111.

    Protocols and materials databases

    DNASUi 3623.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243786 ; ENSP00000243786 ; ENSG00000123999 .
    GeneIDi 3623.
    KEGGi hsa:3623.
    UCSCi uc002vmk.2. human.

    Organism-specific databases

    CTDi 3623.
    GeneCardsi GC02P220433.
    HGNCi HGNC:6065. INHA.
    HPAi CAB000047.
    HPA019141.
    MIMi 147380. gene.
    neXtProti NX_P05111.
    PharmGKBi PA29876.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289440.
    HOGENOMi HOG000013165.
    HOVERGENi HBG052131.
    InParanoidi P05111.
    KOi K05500.
    OMAi GGYSFKY.
    OrthoDBi EOG7BS4BB.
    PhylomeDBi P05111.
    TreeFami TF331531.

    Enzyme and pathway databases

    Reactomei REACT_15398. Glycoprotein hormones.

    Miscellaneous databases

    GeneWikii INHA.
    GenomeRNAii 3623.
    NextBioi 14177.
    PROi P05111.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05111.
    CleanExi HS_INHA.
    Genevestigatori P05111.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR002405. Inhibin_asu.
    IPR017175. Inhibin_asu_subgr.
    IPR001839. TGF-b_C.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037328. Inhibin_alpha_subunit. 1 hit.
    PRINTSi PR00669. INHIBINA.
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(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.
      , 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. 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. 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. Cited for: VARIANT THR-257.

    Entry informationi

    Entry nameiINHA_HUMAN
    AccessioniPrimary (citable) accession number: P05111
    Secondary accession number(s): A8K8H5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 151 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