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Protein

Muellerian-inhibiting factor

Gene

Amh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

This glycoprotein, produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. It is also able to inhibit the growth of tumors derived from tissues of Muellerian duct origin.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Biological processi

Differentiation, Gonadal differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Muellerian-inhibiting factor
Alternative name(s):
Anti-Muellerian hormone
Short name:
AMH
Muellerian-inhibiting substance
Short name:
MIS
Gene namesi
Name:Amh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88006. Amh.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 555Muellerian-inhibiting factorPRO_0000033749
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – ?Sequence analysisPRO_0000033748

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi457 ↔ 521By similarity
Disulfide bondi483 ↔ 552By similarity
Disulfide bondi487 ↔ 554By similarity
Disulfide bondi520 – 520InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP27106.
PRIDEiP27106.

PTM databases

iPTMnetiP27106.
PhosphoSiteiP27106.

Expressioni

Tissue specificityi

Sertoli cells of fetal testes, and testes just after birth, but absent in adult testes. In female, AMH is expressed after birth in the granulosa cells of the follicle. AMH expression is dependent on the degree of follicular maturation and not on the age of the ovary.

Gene expression databases

CleanExiMM_AMH.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043153.

Structurei

3D structure databases

ProteinModelPortaliP27106.
SMRiP27106. Positions 454-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
HOGENOMiHOG000113593.
HOVERGENiHBG006358.
InParanoidiP27106.
PhylomeDBiP27106.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR006799. AMH_N.
IPR029034. Cystine-knot_cytokine.
IPR021203. Muellerian-inhibiting_factor.
IPR001839. TGF-b_C.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR15009. PTHR15009. 1 hit.
PfamiPF04709. AMH_N. 1 hit.
PF00019. TGF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF037270. Muellerian-inhibiting_factor. 1 hit.
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.

P27106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGPHLSPLV LLLATMGAVL QPEAVENLAT NTRGLIFLED ELWPPSSPPE
60 70 80 90 100
PLCLVTVRGE GNTSRASLRV VGGLNSYEYA FLEAVQESRW GPQDLATFGV
110 120 130 140 150
SSTDSQATLP ALQRLGAWLG ETGEQQLLVL HLAEVIWEPE LLLKFQEPPP
160 170 180 190 200
GGASRWEQAL LVLYSGPGPQ VTVTGTGLRG TQNLCPTRDT RYLVLTVDFP
210 220 230 240 250
AGAWSGFGLI LTLQPSREGA TLSIDQLQAF LFGSDSRCFT RMTPTLVVLP
260 270 280 290 300
PAEPSPQPAH GQLDTMPFPQ PGLSLEPEAL PHSADPFLET LTRLVRALRG
310 320 330 340 350
PLTQASNTQL ALDPGALASF PQGLVNLSDP AALGRLLDWE EPLLLLLSPT
360 370 380 390 400
AATEREPIRL HGPASAPWAA GLQRRVAVEL QAAASELRDL PGLPPTAPPL
410 420 430 440 450
LARLLALCPN DSRSSGDPLR ALLLLKALQG LRAEWHGREG RGRTRAQRGD
460 470 480 490 500
KGQDGPCALR ELSVDLRAER SVLIPETYQA NNCQGACRWP QSDRNPRYGN
510 520 530 540 550
HVVLLLKMQA RGAALGRLPC CVPTAYAGKL LISLSEERIS ADHVPNMVAT

ECGCR
Length:555
Mass (Da):59,778
Last modified:August 1, 1992 - v1
Checksum:iD6A3A20C50306E29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63240 Genomic DNA. Translation: CAA44912.1.
X83733 Genomic DNA. Translation: CAC10450.1.
PIRiS20100.
UniGeneiMm.376094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63240 Genomic DNA. Translation: CAA44912.1.
X83733 Genomic DNA. Translation: CAC10450.1.
PIRiS20100.
UniGeneiMm.376094.

3D structure databases

ProteinModelPortaliP27106.
SMRiP27106. Positions 454-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043153.

PTM databases

iPTMnetiP27106.
PhosphoSiteiP27106.

Proteomic databases

PaxDbiP27106.
PRIDEiP27106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:88006. Amh.

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
HOGENOMiHOG000113593.
HOVERGENiHBG006358.
InParanoidiP27106.
PhylomeDBiP27106.

Miscellaneous databases

PROiP27106.
SOURCEiSearch...

Gene expression databases

CleanExiMM_AMH.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR006799. AMH_N.
IPR029034. Cystine-knot_cytokine.
IPR021203. Muellerian-inhibiting_factor.
IPR001839. TGF-b_C.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR15009. PTHR15009. 1 hit.
PfamiPF04709. AMH_N. 1 hit.
PF00019. TGF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF037270. Muellerian-inhibiting_factor. 1 hit.
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

  1. "Expression of the mouse anti-Mullerian hormone gene suggests a role in both male and female sexual differentiation."
    Muensterberg A., Lovell-Badge R.
    Development 113:613-624(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
    Tissue: Testis.
  2. "A GNRP-like gene shares a bidirectional promoter with SAP62 immediately upstream of AMH."
    Dresser D.W., Jamin S., Atkins C.J., Guerrier D.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  3. "The genes for a spliceosome protein (SAP62) and the anti-Mullerian hormone (AMH) are contiguous."
    Dresser D.W., Hacker A., Lovell-Badge R., Guerrier D.
    Hum. Mol. Genet. 4:1613-1618(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    Strain: 129.

Entry informationi

Entry nameiMIS_MOUSE
AccessioniPrimary (citable) accession number: P27106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Although it does not compete with EGF for receptor binding sites, MIS can inhibit the autophosphorylation of the EGF receptor in vitro.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.