ID   SRY_BOSIN               Reviewed;         229 AA.
AC   Q7JGF7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Sex-determining region Y protein;
DE   AltName: Full=Testis-determining factor;
GN   Name=SRY; Synonyms=TDF;
OS   Bos indicus (Zebu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9915;
RN   [1]
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   [2]
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; AB077318; BAC41383.1; -; Genomic_DNA.
DR   EMBL; AY079145; AAL86546.1; -; Genomic_DNA.
DR   RefSeq; XP_019812159.1; XM_019956600.1.
DR   AlphaFoldDB; Q7JGF7; -.
DR   SMR; Q7JGF7; -.
DR   GeneID; 109555752; -.
DR   KEGG; biu:109555752; -.
DR   CTD; 6736; -.
DR   OrthoDB; 369754at2759; -.
DR   Proteomes; UP000515132; Chromosome Y.
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_0000048645"
FT   DNA_BIND        54..122
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          32..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"
SQ   SEQUENCE   229 AA;  26671 MW;  371A6ED61E541D20 CRC64;
     MFRVLNDDVY SPAVVQQQTT LAFRKDSSLC TDSHSANDQC ERGEHVRESS QDHVKRPMNA
     FIVWSRERRR KVALENPKMK NSDISKQLGY EWKRLTDAEK RPFFEEAQRL LAIHRDKYPG
     YKYRPRRRAK RPQKSLPADS SILCNPMHVE TLHPFTYRDG CAKTTYSQME SQLSRSQSVI
     ITNSLLQKEH HSSWTSLGHN KVTLATRISA DFPFNKSLEP GLSCAYFQY