MIS_PIG
ID MIS_PIG Reviewed; 575 AA.
AC P79295;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Muellerian-inhibiting factor;
DE AltName: Full=Anti-Muellerian hormone;
DE Short=AMH;
DE AltName: Full=Muellerian-inhibiting substance;
DE Short=MIS;
DE Flags: Precursor;
GN Name=AMH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Daneau I., Silversides D.W.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=909589; DOI=10.1038/269411a0;
RA Tran D., Muesy-Dessole N., Josso N.;
RT "Anti-Muellerian hormone is a functional marker of foetal Sertoli cells.";
RL Nature 269:411-412(1977).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30063719; DOI=10.1371/journal.pone.0197894;
RA Almeida F.R.C.L., Costermans N.G.J., Soede N.M., Bunschoten A., Keijer J.,
RA Kemp B., Teerds K.J.;
RT "Presence of anti-Muellerian hormone (AMH) during follicular development in
RT the porcine ovary.";
RL PLoS ONE 13:e0197894-e0197894(2018).
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 (By similarity). In female acts as a negative regulator of the
CC primordial to primary follicle transition and decreases FSH sensitivity
CC of growing follicles. AMH signals by binding to a specific type-II
CC receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and
CC BMPR1A), and recruiting SMAD proteins that are translocated to the
CC nucleus to regulate target gene expression (By similarity).
CC {ECO:0000250|UniProtKB:P03971, ECO:0000250|UniProtKB:P27106}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P03971}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P03971}.
CC -!- TISSUE SPECIFICITY: Detected in fetal Sertoli cells (PubMed:909589).
CC Expressed in granulosa cells of growing follicles but also in theca
CC cells of preovulatory follicles and corpora lutea (at protein level)
CC (PubMed:30063719). {ECO:0000269|PubMed:30063719,
CC ECO:0000269|PubMed:909589}.
CC -!- DEVELOPMENTAL STAGE: Appears for the first time during follicular
CC development in the fusiform granulosa cells of recruited primordial
CC follicles and continues to be present in granulosa cells up to the
CC antral stage. {ECO:0000269|PubMed:30063719}.
CC -!- PTM: Preproprotein is proteolytically processed to generate N- and C-
CC terminal cleavage products that homodimerize and associate to form a
CC biologically active non-covalent complex. Binding of the non-covalent
CC complex to AMHR2 induces dissociation of the pro-region from the mature
CC C-terminal dimer. The N-terminal portion of the protein, despite having
CC no intrinsic activity, has the role of amplifying the activity of the
CC C-terminus. {ECO:0000250|UniProtKB:P03971}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; U80853; AAC25968.1; -; mRNA.
DR PIR; T11753; T11753.
DR AlphaFoldDB; P79295; -.
DR SMR; P79295; -.
DR InParanoid; P79295; -.
DR ChiTaRS; AMH; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0033327; P:Leydig cell differentiation; ISS:UniProtKB.
DR GO; GO:0001880; P:Mullerian duct regression; ISS:UniProtKB.
DR GO; GO:2000355; P:negative regulation of ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 2.10.90.10; -; 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; PTHR15009; 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; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Differentiation; Disulfide bond; Glycoprotein; Gonadal differentiation;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..466
FT /evidence="ECO:0000250|UniProtKB:P03971"
FT /id="PRO_0000033750"
FT CHAIN 467..575
FT /note="Muellerian-inhibiting factor"
FT /id="PRO_0000033751"
FT SITE 466..467
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P03971"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 477..541
FT /evidence="ECO:0000250|UniProtKB:P03971"
FT DISULFID 503..572
FT /evidence="ECO:0000250|UniProtKB:P03971"
FT DISULFID 507..574
FT /evidence="ECO:0000250|UniProtKB:P03971"
FT DISULFID 540
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P03971"
SQ SEQUENCE 575 AA; 61505 MW; 69AF63654B390780 CRC64;
MQGPSLSQLV LVLMGALLEA GTPREEVSST PALPREPRTG TEGLIFHWDW NWPPPGAWPP
GGPQDPLCLV TLNGTPGNGS SPFLWVVGTL SSYEQAFLEA VRHARWGPQD LANFGLCPPS
LRQAALPLLQ QLQAWLGEPR GQRLVVLHLE EVSWEPTPLL KFQEPLPGEA SPLELALLVL
YPGPGPEVTV TGAGLPGAQS LCPTRDSGFL ALAVDRPERA WRGSGLALTL RRRGNGASLS
TAQLQALLFG ADSRCFTRMT PALLLLPPQG PVPMPAHGRV DSMPFPQPRL SPEPEEPLPS
TDPFLETLTR LVRALRGPPA RIPPPSLALD PGALAGFPQG QVNLSDPAAL ERLLNSEEPL
LLLLPPPTAV TAGVPAPLQG PVTEMWASSL ARRVATEFQS AAAELRGFPG LPPTATLLLA
RLLALCPGDR GDPGGPLRAV LLLKALQGLR TEWRWRERSG PARAQRSAGT AVSNGPCALR
ELSVDLRAER SVLIPETYQA NNCQGTCGWP QSDRNPRYGN HVVLLLKMQA RGAALARPPC
CVPTAYAGKL LISLSEERIS AHHVPNMVAT ECGCR
