ID   SRY_MACMU               Reviewed;         204 AA.
AC   Q9BG90;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Sex-determining region Y protein;
DE   AltName: Full=Testis-determining factor;
GN   Name=SRY; Synonyms=TDF;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11112659; DOI=10.1086/316932;
RA   Patel M., Dorman K.S., Zhang Y.-H., Huang B.-L., Arnold A.P.,
RA   Sinsheimer J.S., Vilain E., McCabe E.R.B.;
RT   "Primate DAX1, SRY, and SOX9: evolutionary stratification of sex-
RT   determination pathway.";
RL   Am. J. Hum. Genet. 68:275-280(2001).
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-136 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; AF322901; AAK01652.1; -; mRNA.
DR   RefSeq; NP_001028008.1; NM_001032836.1.
DR   AlphaFoldDB; Q9BG90; -.
DR   SMR; Q9BG90; -.
DR   GeneID; 574155; -.
DR   KEGG; mcc:574155; -.
DR   CTD; 6736; -.
DR   InParanoid; Q9BG90; -.
DR   OrthoDB; 369754at2759; -.
DR   Proteomes; UP000006718; 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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0030238; P:male sex determination; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Activator; Calmodulin-binding; Cytoplasm; Differentiation;
KW   DNA-binding; Nucleus; Reference proteome; Repressor;
KW   Sexual differentiation; Transcription; Transcription regulation.
FT   CHAIN           1..204
FT                   /note="Sex-determining region Y protein"
FT                   /id="PRO_0000048678"
FT   DNA_BIND        60..128
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          175..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  23618 MW;  774EFEC92B3A0B40 CRC64;
     MQSYASAMLS VFNTDGYSPA AQQNIPALRR SSSFICTESC SSKYQCEAGE NSKGSVQDKV
     KRPMNAFIVW SRDQKRKMAL ENPKMRNSEI SKQLGYQWKM LTEADKWPFF QEAQKLQAMH
     REKYPNYKYR PRRKAKMLQN SCSLLPADPS SVPCREVQLD NRLYRDDCTK ATHSRMQHQL
     GHLPPINTAS SPQQRDRYSH STKL