SRY_BOSMU
ID SRY_BOSMU Reviewed; 229 AA.
AC Q9XS37; Q7JGF8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=SRY; Synonyms=TDF;
OS Bos mutus grunniens (Wild yak) (Bos grunniens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11742636; DOI=10.1186/1297-9686-33-6-687;
RA Cheng H., Shi H., Zhou R., Guo Y., Liu L., Liu J., Jiang Y., Kudo T.,
RA Sutou S.;
RT "Characterization of Bovidae sex-determining gene SRY.";
RL Genet. Sel. Evol. 33:687-694(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12648092; DOI=10.1046/j.1365-2052.2003.00956.x;
RA Kikkawa Y., Takada T., Sutopo X., Nomura K., Namikawa T., Yonekawa H.,
RA Amano T.;
RT "Phylogenies using mtDNA and SRY provide evidence for male-mediated
RT introgression in Asian domestic cattle.";
RL Anim. Genet. 34:96-101(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14739241; DOI=10.1093/molbev/msh064;
RA Verkaar E.L.C., Nijman I.J., Beeke M., Hanekamp E., Lenstra J.A.;
RT "Maternal and paternal lineages in cross-breeding bovine species. Has
RT wisent a hybrid origin?";
RL Mol. Biol. Evol. 21:1165-1170(2004).
CC -!- FUNCTION: Transcriptional regulator that controls a genetic switch in
CC male development. It is necessary and sufficient for initiating male
CC sex determination by directing the development of supporting cell
CC precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells.
CC Involved in different aspects of gene regulation including promoter
CC activation or repression. Binds to the DNA consensus sequence 5'-
CC [AT]AACAA[AT]-3'. SRY HMG box recognizes DNA by partial intercalation
CC in the minor groove and promotes DNA bending. Also involved in pre-mRNA
CC splicing (By similarity). In male adult brain involved in the
CC maintenance of motor functions of dopaminergic neurons (By similarity).
CC {ECO:0000250|UniProtKB:P36394, ECO:0000250|UniProtKB:Q05066}.
CC -!- SUBUNIT: Interacts with CALM, EP300, HDAC3, KPNB1, ZNF208 isoform KRAB-
CC O, PARP1, SLC9A3R2 and WT1. The interaction with EP300 modulates its
CC DNA-binding activity. The interaction with KPNB1 is sensitive to
CC dissociation by Ran in the GTP-bound form. Interaction with PARP1
CC impaired its DNA-binding activity. {ECO:0000250|UniProtKB:Q05066}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q05066}. Nucleus
CC {ECO:0000250|UniProtKB:Q05066}.
CC -!- PTM: Acetylation of Lys-130 contributes to its nuclear localization and
CC enhances its interaction with KPNB1. Deacetylated by HDAC3.
CC {ECO:0000250|UniProtKB:Q05066}.
CC -!- SIMILARITY: Belongs to the SRY family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The tenuous nature of sex
CC - Issue 80 of March 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/080";
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DR EMBL; AF148463; AAD31532.1; -; Genomic_DNA.
DR EMBL; AB077320; BAC41385.1; -; Genomic_DNA.
DR EMBL; AY079144; AAL86545.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XS37; -.
DR SMR; Q9XS37; -.
DR Proteomes; UP000694520; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030238; P:male sex determination; IEA:InterPro.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017253; SRY.
DR PANTHER; PTHR10270:SF199; PTHR10270:SF199; 1.
DR Pfam; PF00505; HMG_box; 1.
DR PIRSF; PIRSF037653; SRY; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; Calmodulin-binding; Cytoplasm; Differentiation;
KW DNA-binding; Nucleus; Reference proteome; Repressor;
KW Sexual differentiation; Transcription; Transcription regulation.
FT CHAIN 1..229
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048647"
FT DNA_BIND 54..122
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 76
FT /note="Y -> N (in Ref. 3; AAL86545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26720 MW; 77FCEF497F331D36 CRC64;
MFRVLNDDVY SPAVVQQQTT LAFRKDSSLC TDSHSANDQC ERGEHVRESS QDHVKRPMNA
FIVWSRERRR KVALEYPKMK NSDISKQLGY EWKRLTDAEK RPFFEEAQRL LAIHRDKYPG
YKYRPRRRAK RPQKSLPADS SILCNPMHVE TLHPFTYRDG CAKTTYSQME SQLSRSQSVI
ITNSLLQKEH HSSWTSLGHN KVTLATRISA DFPFNKSLEP GLSCAYFQY
