SRY_MUSSP
ID SRY_MUSSP Reviewed; 355 AA.
AC Q62563;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=Sry; Synonyms=Tdf;
OS Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10096;
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=8355784; DOI=10.1038/364715a0;
RA Tucker P.K., Lundrigan B.L.;
RT "Rapid evolution of the sex determining locus in Old World mice and rats.";
RL Nature 364:715-717(1993).
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";
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DR EMBL; U70659; AAC53449.1; -; Genomic_DNA.
DR EMBL; AF009521; AAC53452.1; -; Genomic_DNA.
DR EMBL; L29544; AAA40102.1; -; Genomic_DNA.
DR PIR; T47235; T47235.
DR AlphaFoldDB; Q62563; -.
DR SMR; Q62563; -.
DR MGI; MGI:98660; Sry.
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; Repeat; Sexual differentiation; Transcription;
KW Transcription regulation.
FT CHAIN 1..355
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048689"
FT DNA_BIND 5..73
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 135..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 274
FT /note="K -> R"
SQ SEQUENCE 355 AA; 44260 MW; 0903265F7A173EFC CRC64;
MEGHVKRPMN AFMVWSRGER HKLAQQNPSM QNTEISKQLG CRWKSLTEAE KRPFFQEAQR
LKTLHREKYP NYKYQPHRRA KVSQRSGILQ PRVASTKLYN LLQWDRNPHA ITYRQDWSRA
AHLYSKNQQS FYLQPVDIPT GHPQQQQQQF HNHHQQKQQF HDHHQQKQQF HDHHQQQQQF
HDHQQQQQQF HDHQQQKQQF HDHQQQQQQF HDHHHQQQQQ QFHDHHHHQQ QQQQFHDHHQ
QKQQFHDHHQ QQQQQQFHDH PQQQQQFHDH PQQKQQFHDH HHHQQQKQQF HDHHQQKQQF
HDHHQQQQQF HDHQQQQQQQ QFHDQQLTYL LTADITGEHT PYQEHLSKAL WLAVS
