SRY_MUSSI
ID SRY_MUSSI Reviewed; 311 AA.
AC Q62565;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=Sry; Synonyms=Tdy;
OS Mus spicilegus (Steppe mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9383069; DOI=10.1093/genetics/147.3.1267;
RA Albrecht K.H., Eicher E.M.;
RT "DNA sequence analysis of Sry alleles (subgenus Mus) implicates
RT misregulation as the cause of C57BL/6J-Y(POS) sex reversal and defines the
RT SRY functional unit.";
RL Genetics 147:1267-1277(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RX PubMed=8015441; DOI=10.1093/oxfordjournals.molbev.a040128;
RA Lundrigan B.L., Tucker P.K.;
RT "Tracing paternal ancestry in mice, using the Y-linked, sex-determining
RT locus, Sry.";
RL Mol. Biol. Evol. 11:483-492(1994).
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 -!- DOMAIN: The Gln- and His-rich domain may mediate protein-protein
CC interactions.
CC -!- PTM: Acetylation of Lys-81 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";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U70658; AAC53448.1; -; Genomic_DNA.
DR EMBL; AF009520; AAC53451.1; -; Genomic_DNA.
DR EMBL; L29550; AAA40140.1; -; Genomic_DNA.
DR AlphaFoldDB; Q62565; -.
DR SMR; Q62565; -.
DR MGI; MGI:98660; Sry.
DR Proteomes; UP000694415; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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 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; Repeat; Sexual differentiation;
KW Transcription; Transcription regulation.
FT CHAIN 1..311
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048688"
FT DNA_BIND 5..73
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 135..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 38469 MW; C24E414D4A2D3DDB CRC64;
MEGHVKRPMN AFMVWSRGER HKLAQQNPSM QNTEISKQLG CRWKSLTEAE KRPFFQEAQR
LKTLHREKYP NYKYQPHRRA KVSQRSGILQ PRVASTKLYN LLQWDRNPHA ITYRQDWSRA
AHLYSKNQQS FYLQPVDIPT GHPQQQQQQQ FHNHHQQKQQ FHDHHQQQQQ QQFHDHHQQK
QQFHDHQQQQ QQFHDHHHHQ QQQQFHDHQQ QQQQLHNHHH QQQQQFHDYP QQQQQFHDHP
QQKQQFHDRP QQQQQFHDHH QQQQQFHDHH HQQQQQQFHD QQLTYLLTAD ITGEHTPYQE
HLSKALWLAV S
