ID A0A0D9RH05_CHLSB Unreviewed; 566 AA.
AC A0A0D9RH05;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Muellerian-inhibiting factor {ECO:0000256|ARBA:ARBA00020473, ECO:0000256|PIRNR:PIRNR037270};
GN Name=AMH {ECO:0000313|Ensembl:ENSCSAP00000007894.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000007894.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000007894.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000007894.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in several reproductive functions.
CC Induces Muellerian duct regression during male fetal sexual
CC differentiation and plays a role in Leydig cell differentiation and
CC function. In female acts as a negative regulator of the primordial to
CC primary follicle transition and decreases FSH sensitivity of growing
CC follicles. AMH signals by binding to a specific type-II receptor,
CC AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A),
CC and recruiting SMAD proteins that are translocated to the nucleus to
CC regulate target gene expression. {ECO:0000256|PIRNR:PIRNR037270}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748,
CC ECO:0000256|PIRNR:PIRNR037270}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR037270}.
CC -!- SIMILARITY: Belongs to the TGF-beta family.
CC {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|PIRNR:PIRNR037270,
CC ECO:0000256|RuleBase:RU000354}.
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DR EMBL; AQIB01150337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007992887.1; XM_007994696.1.
DR AlphaFoldDB; A0A0D9RH05; -.
DR STRING; 60711.ENSCSAP00000007894; -.
DR Ensembl; ENSCSAT00000009786.1; ENSCSAP00000007894.1; ENSCSAG00000011706.1.
DR GeneID; 103233641; -.
DR KEGG; csab:103233641; -.
DR CTD; 268; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000006337; -.
DR OMA; NCQGVCG; -.
DR OrthoDB; 3972567at2759; -.
DR BioGRID-ORCS; 103233641; 0 hits in 16 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 6.
DR Bgee; ENSCSAG00000011706; Expressed in pituitary gland and 1 other cell type or tissue.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IEA:Ensembl.
DR GO; GO:1990262; P:anti-Mullerian hormone signaling pathway; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-UniRule.
DR GO; GO:0001880; P:Mullerian duct regression; IEA:UniProtKB-UniRule.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; IEA:UniProtKB-UniRule.
DR CDD; cd13757; TGF_beta_AMH; 1.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR006799; AMH_N.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR021203; Muellerian-inhibiting_factor.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR15009; MUELLERIAN-INHIBITING FACTOR; 1.
DR PANTHER; PTHR15009:SF4; MUELLERIAN-INHIBITING FACTOR; 1.
DR Pfam; PF04709; AMH_N; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037270; Muellerian-inhibiting_factor; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 3: Inferred from homology;
KW Differentiation {ECO:0000256|PIRNR:PIRNR037270};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Gonadal differentiation {ECO:0000256|ARBA:ARBA00023156,
KW ECO:0000256|PIRNR:PIRNR037270};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR037270};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..566
FT /note="Muellerian-inhibiting factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002345037"
FT DOMAIN 447..566
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT REGION 265..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 59665 MW; DDE0E3122D8DFC2A CRC64;
MTRDLPLTSL TLVLSALGAL LGTEALRAEE PAVGTGGLIF REDLDWPPGS PQEPLCLLAL
GGDSNGSGTP LQVMGVLSAY ERAFLGIVQR ARWGPRDLAT FGVCTPGDRQ AALPSLRRLG
AWLRDPGGQR LVVLHLEEVT WEPTPSLRFQ EPPHGVADPP ELALLVLYPG PGPGPEVTVT
RAGLPGAQSL CLSRDTRYLA LAVDRPAGAW RGSGLALTLQ PRGEGSLLST AQLQALLFGD
DHRCFTRMTP ALLLLLRSEP APLPTPLPAQ GQLDTVPFPP PRPTAELEES PPSADPFLET
LTSLVRALRG PPARASAPRL ALDPDALAGF PQGLVNLSDP AALERLLDGE EPLLLLRPTA
ATTGDPAPLH DPTSAPWATA LARRVAAELQ AAVAELHSLP GLPPAAAPLL ARLLALCPGG
SGGPGDPLRA LLLLKALQGL RAEWRGRDPR GPGRAQRSAG TTAADGPCAL RELSVDLRAE
RSVLIPETYQ ANNCQGVCGW PQSDRNPRYG NHVVLLLKMQ ARGAALARPP CCVPTAYAGK
LLISLSEERI SAHHVPNMVA TECGCR
//
