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Sex-determining region Y protein (Testis-determining factor)

 SRY_MOUSE               Reviewed;         395 AA.
Q05738;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 156.
RecName: Full=Sex-determining region Y protein;
AltName: Full=Testis-determining factor;
Name=Sry; Synonyms=Tdf, Tdy;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129; TISSUE=Spleen;
PubMed=1518820; DOI=10.1073/pnas.89.17.7953;
Gubbay J., Vivian N., Economou A., Jackson D., Goodfellow P.;
"Inverted repeat structure of the Sry locus in mice.";
Proc. Natl. Acad. Sci. U.S.A. 89:7953-7957(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8355784; DOI=10.1038/364715a0;
Tucker P.K., Lundrigan B.L.;
"Rapid evolution of the sex determining locus in Old World mice and
rats.";
Nature 364:715-717(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Torino; TISSUE=Liver;
PubMed=8012385; DOI=10.1038/ng0394-245;
Coward P., Nagai K., Chen D., Thomas H.D., Nagamine C.M., Lau Y.-F.C.;
"Polymorphism of a CAG trinucleotide repeat within Sry correlates with
B6.YDom sex reversal.";
Nat. Genet. 6:245-250(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
STRAIN=129;
PubMed=2374589; DOI=10.1038/346245a0;
Gubbay J., Collignon J., Koopman P., Capel B., Economou A.,
Munsterberg A., Vivian N., Goodfellow P., Lovell-Badge R.;
"A gene mapping to the sex-determining region of the mouse Y
chromosome is a member of a novel family of embryonically expressed
genes.";
Nature 346:245-250(1990).
[5]
CHARACTERIZATION OF DNA-BINDING.
PubMed=8190643; DOI=10.1093/nar/22.8.1500;
Harley V.R., Lovell-Badge R., Goodfellow P.N.;
"Definition of a consensus DNA binding site for SRY.";
Nucleic Acids Res. 22:1500-1501(1994).
[6]
CHARACTERIZATION OF DNA-BINDING.
PubMed=8159753; DOI=10.1073/pnas.91.8.3368;
Giese K., Pagel J., Grosschedl R.;
"Distinct DNA-binding properties of the high mobility group domain of
murine and human SRY sex-determining factors.";
Proc. Natl. Acad. Sci. U.S.A. 91:3368-3372(1994).
[7]
DEVELOPMENTAL STAGE.
PubMed=7600978;
Hacker A., Capel B., Goodfellow P., Lovell-Badge R.;
"Expression of Sry, the mouse sex determining gene.";
Development 121:1603-1614(1995).
[8]
DEVELOPMENTAL STAGE.
PubMed=7670499; DOI=10.1038/ng0895-480;
Jeske Y.W., Bowles J., Greenfield A., Koopman P.;
"Expression of a linear Sry transcript in the mouse genital ridge.";
Nat. Genet. 10:480-482(1995).
[9]
TISSUE SPECIFICITY.
PubMed=11085593; DOI=10.1007/s100480000093;
Mayer A., Mosler G., Just W., Pilgrim C., Reisert I.;
"Developmental profile of Sry transcripts in mouse brain.";
Neurogenetics 3:25-30(2000).
[10]
DEVELOPMENTAL STAGE.
PubMed=11784049; DOI=10.1006/dbio.2001.0438;
Albrecht K.H., Eicher E.M.;
"Evidence that Sry is expressed in pre-Sertoli cells and Sertoli and
granulosa cells have a common precursor.";
Dev. Biol. 240:92-107(2001).
[11]
INTERACTION WITH KPNB1, AND SUBCELLULAR LOCATION.
PubMed=11535586; DOI=10.1074/jbc.M101668200;
Forwood J.K., Harley V., Jans D.A.;
"The C-terminal nuclear localization signal of the sex-determining
region Y (SRY) high mobility group domain mediates nuclear import
through importin beta 1.";
J. Biol. Chem. 276:46575-46582(2001).
[12]
FUNCTION, AND DNA-BINDING.
PubMed=15170344; DOI=10.1021/bi049920a;
Phillips N.B., Nikolskaya T., Jancso-Radek A., Ittah V., Jiang F.,
Singh R., Haas E., Weiss M.A.;
"Sry-directed sex reversal in transgenic mice is robust with respect
to enhanced DNA bending: comparison of human and murine HMG boxes.";
Biochemistry 43:7066-7081(2004).
[13]
ACETYLATION AT LYS-81, AND MUTAGENESIS OF LYS-81.
PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
Aldrian-Herrada G., Poulat F., Berta P., Benkirane M.,
Boizet-Bonhoure B.;
"Regulation of human SRY subcellular distribution by its
acetylation/deacetylation.";
EMBO J. 23:3336-3345(2004).
[14]
INTERACTION WITH ZNF208 ISOFORM KRAB-O, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=15469996; DOI=10.1095/biolreprod.104.034447;
Oh H.J., Li Y., Lau Y.-F.C.;
"Sry associates with the heterochromatin protein 1 complex by
interacting with a KRAB domain protein.";
Biol. Reprod. 72:407-415(2005).
[15]
INTERACTION WITH SLC9A3R2.
PubMed=16166090; DOI=10.1074/jbc.M504127200;
Thevenet L., Albrecht K.H., Malki S., Berta P., Boizet-Bonhoure B.,
Poulat F.;
"NHERF2/SIP-1 interacts with mouse SRY via a different mechanism than
human SRY.";
J. Biol. Chem. 280:38625-38630(2005).
[16]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16488877; DOI=10.1016/j.cub.2006.01.017;
Dewing P., Chiang C.W., Sinchak K., Sim H., Fernagut P.-O., Kelly S.,
Chesselet M.-F., Micevych P.E., Albrecht K.H., Harley V.R., Vilain E.;
"Direct regulation of adult brain function by the male-specific factor
SRY.";
Curr. Biol. 16:415-420(2006).
[17]
INTERACTION WITH PARP1, ADP-RIBOSYLATION, DNA-BINDING, AND
DEVELOPMENTAL STAGE.
PubMed=16904257; DOI=10.1016/j.mce.2006.06.008;
Li Y., Oh H.J., Lau Y.-F.C.;
"The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates
its biological functions.";
Mol. Cell. Endocrinol. 257:35-46(2006).
[18]
REVIEW.
PubMed=16996051; DOI=10.1016/j.ydbio.2006.08.049;
Polanco J.C., Koopman P.;
"Sry and the hesitant beginnings of male development.";
Dev. Biol. 302:13-24(2007).
[19]
REVIEW.
PubMed=16414182; DOI=10.1016/j.mce.2005.12.011;
Oh H.J., Lau Y.F.;
"KRAB: a partner for SRY action on chromatin.";
Mol. Cell. Endocrinol. 247:47-52(2006).
-!- FUNCTION: Transcriptional regulator that controls a genetic switch
in male development. It is necessary and sufficient for initiating
male sex determination by directing the development of supporting
cell precursors (pre-Sertoli cells) as Sertoli rather than
granulosa cells. In male adult brain involved in the maintenance
of motor functions of dopaminergic neurons (By similarity).
Involved in different aspects of gene regulation including
promoter activation or repression. SRY HMG box recognizes DNA by
partial intercalation in the minor groove. Promotes DNA bending.
Also involved in pre-mRNA splicing (By similarity). Binds to the
DNA consensus sequence 5'-[AT]AACAA[AT]-3'. {ECO:0000250,
ECO:0000269|PubMed:15170344}.
-!- SUBUNIT: Interacts with KPNB1, ZNF208 isoform KRAB-O, PARP1 and
SLC9A3R2. The interaction with KPNB1 is sensitive to dissociation
by Ran in the GTP-bound form. Interaction with PARP1 impaired its
DNA-binding activity. Interacts with CALM, EP300, HDAC3 and WT1
(By similarity). The interaction with EP300 modulates its DNA-
binding activity (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000250|UniProtKB:Q05066}. Cytoplasm
{ECO:0000269|PubMed:11535586, ECO:0000269|PubMed:15469996,
ECO:0000269|PubMed:16488877}. Nucleus
{ECO:0000250|UniProtKB:Q05066}. Note=Acetylation contributes to
its nuclear localization and deacetylation by HDAC3 induces a
cytoplasmic delocalization (By similarity). Colocalizes in the
nucleus with ZNF208 isoform KRAB-O and tyrosine hydroxylase (TH)
(PubMed:15469996). Colocalizes with SOX6 in speckles. Colocalizes
with CAML in the nucleus (By similarity).
{ECO:0000250|UniProtKB:Q05066, ECO:0000269|PubMed:15469996}.
-!- TISSUE SPECIFICITY: Expressed in the substantia nigra of the brain
(at protein level). Expressed in diencephalon, cortex, the
substantia nigra of the midbrain and the medial mammillary bodies
of the hypothalamus of male, but not female.
{ECO:0000269|PubMed:11085593, ECO:0000269|PubMed:15469996,
ECO:0000269|PubMed:16488877}.
-!- DEVELOPMENTAL STAGE: Expressed in gonadal somatic pre-Sertoli
cells from 10.5 to 11.5 dpc. Expressed in pre-Sertoli cells
located centrally in the genital ridge and then later in cells
located at the cranial and caudal poles (at protein level).
{ECO:0000269|PubMed:11784049, ECO:0000269|PubMed:16904257,
ECO:0000269|PubMed:7600978, ECO:0000269|PubMed:7670499}.
-!- DOMAIN: DNA binding and bending properties of the HMG domains of
mouse and human SRY differ form each other. Mouse SRY shows less
extensive minor groove contacts with DNA and a higher specificity
of sequence recognition than human SRY.
-!- PTM: Phosphorylated on serine residues by PKA. Phosphorylation by
PKA enhances its DNA-binding activity and stimulates transcription
repression. {ECO:0000250}.
-!- PTM: Acetylation of Lys-81 contributes to its nuclear localization
and enhances its interaction with KPNB1.
{ECO:0000269|PubMed:15297880}.
-!- PTM: Poly-ADP-ribosylated by PARP1 (By similarity). ADP-
ribosylation reduces its DNA-binding activity. {ECO:0000250}.
-!- POLYMORPHISM: Different alleles occur in strains of Mus musculus
(molossinus or domesticus). In particular the poly-Gln region in
167-177 is polymorphic with either 11, 12 or 13 Gln. The nature of
this poly-Gln tract could affect the protein's function by
disturbing its secondary structure, perhaps by preventing
efficient contact with another protein.
-!- SIMILARITY: Belongs to the SRY family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The tenuous nature of
sex - Issue 80 of March 2007;
URL="https://web.expasy.org/spotlight/back_issues/080";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X67204; CAB56798.1; -; Genomic_DNA.
EMBL; U03645; AAB60446.1; -; Genomic_DNA.
EMBL; X55491; CAA39111.1; -; Genomic_DNA.
CCDS; CCDS30545.1; -.
PIR; S35565; S35565.
PIR; S43344; S43344.
RefSeq; NP_035694.1; NM_011564.1.
UniGene; Mm.377114; -.
ProteinModelPortal; Q05738; -.
SMR; Q05738; -.
MINT; MINT-1367342; -.
STRING; 10090.ENSMUSP00000088717; -.
iPTMnet; Q05738; -.
PhosphoSitePlus; Q05738; -.
PaxDb; Q05738; -.
PRIDE; Q05738; -.
Ensembl; ENSMUST00000091178; ENSMUSP00000088717; ENSMUSG00000069036.
GeneID; 21674; -.
KEGG; mmu:21674; -.
UCSC; uc012hrv.1; mouse.
CTD; 6736; -.
MGI; MGI:98660; Sry.
eggNOG; KOG0527; Eukaryota.
eggNOG; ENOG410XT0K; LUCA.
GeneTree; ENSGT00760000118988; -.
HOVERGEN; HBG008712; -.
InParanoid; Q05738; -.
KO; K09266; -.
OMA; QQFHDHH; -.
OrthoDB; EOG091G0JDD; -.
Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
PRO; PR:Q05738; -.
Proteomes; UP000000589; Chromosome Y.
Bgee; ENSMUSG00000069036; -.
CleanEx; MM_SRY; -.
ExpressionAtlas; Q05738; differential.
Genevisible; Q05738; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0008584; P:male gonad development; IDA:MGI.
GO; GO:0030238; P:male sex determination; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0007530; P:sex determination; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 1.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR017253; SRY.
PANTHER; PTHR10270:SF199; PTHR10270:SF199; 5.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
Acetylation; Activator; ADP-ribosylation; Calmodulin-binding;
Complete proteome; Cytoplasm; Differentiation; DNA-binding; Nucleus;
Reference proteome; Repressor; Sexual differentiation; Transcription;
Transcription regulation.
CHAIN 1 395 Sex-determining region Y protein.
/FTId=PRO_0000048687.
DNA_BIND 5 73 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 4 81 Sufficient for interaction with KPNB1.
{ECO:0000250}.
REGION 6 22 Required for nuclear localization.
{ECO:0000250}.
REGION 52 84 Sufficient for interaction with EP300.
{ECO:0000250}.
REGION 75 81 Required for nuclear localization.
{ECO:0000250}.
REGION 92 144 Necessary for interaction with ZNF208
isoform KRAB-O.
REGION 94 138 Necessary for interaction with SLC9A3R2
and nuclear accumulation of SLC9A3R2.
{ECO:0000269|PubMed:16166090}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000269|PubMed:15297880}.
VARIANT 63 63 I -> T (in strain: Torino).
VARIANT 133 133 W -> L (in strain: Torino).
VARIANT 143 145 LQQ -> P (in strain: Torino).
VARIANT 169 170 Missing (in strain: Torino).
VARIANT 209 209 H -> Q (in strain: Torino).
VARIANT 211 211 E -> Q (in strain: Torino).
VARIANT 235 395 Missing (in strain: Torino).
MUTAGEN 81 81 K->R: Abolishes acetylation.
{ECO:0000269|PubMed:15297880}.
SEQUENCE 395 AA; 49494 MW; FFBE9C35161CD80C CRC64;
MEGHVKRPMN AFMVWSRGER HKLAQQNPSM QNTEISKQLG CRWKSLTEAE KRPFFQEAQR
LKILHREKYP NYKYQPHRRA KVSQRSGILQ PAVASTKLYN LLQWDRNPHA ITYRQDWSRA
AHLYSKNQQS FYWQPVDIPT GHLQQQQQQQ QQQQFHNHHQ QQQQFYDHHQ QQQQQQQQQQ
QFHDHHQQKQ QFHDHHQQQQ QFHDHHHHHQ EQQFHDHHQQ QQQFHDHQQQ QQQQQQQQFH
DHHQQKQQFH DHHHHQQQQQ FHDHQQQQQQ FHDHQQQQHQ FHDHPQQKQQ FHDHPQQQQQ
FHDHHHQQQQ KQQFHDHHQQ KQQFHDHHQQ KQQFHDHHQQ QQQFHDHHQQ QQQQQQQQQQ
QFHDQQLTYL LTADITGEHT PYQEHLSTAL WLAVS


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