SRY_MOUSE
ID SRY_MOUSE Reviewed; 392 AA.
AC Q05738;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Sex-determining region Y protein {ECO:0000303|PubMed:1518820};
DE AltName: Full=Testis-determining factor {ECO:0000250|UniProtKB:Q05066};
GN Name=Sry {ECO:0000303|PubMed:1518820, ECO:0000312|MGI:MGI:98660};
GN Synonyms=Tdf {ECO:0000250|UniProtKB:Q05066},
GN Tdy {ECO:0000312|MGI:MGI:98660};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Spleen;
RX PubMed=1518820; DOI=10.1073/pnas.89.17.7953;
RA Gubbay J., Vivian N., Economou A., Jackson D., Goodfellow P.;
RT "Inverted repeat structure of the Sry locus in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7953-7957(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS THR-63;
RP LEU-133; 143-LEU--GLN-145 DELINS PRO; 169-HIS-GLN-170 DEL; GLN-209; GLN-211
RP AND 235-GLN--SER-395 DEL.
RC STRAIN=Torino; TISSUE=Liver;
RX PubMed=8012385; DOI=10.1038/ng0394-245;
RA Coward P., Nagai K., Chen D., Thomas H.D., Nagamine C.M., Lau Y.-F.C.;
RT "Polymorphism of a CAG trinucleotide repeat within Sry correlates with
RT B6.YDom sex reversal.";
RL Nat. Genet. 6:245-250(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SRY-T), ALTERNATIVE SPLICING (ISOFORMS
RP SRY-S AND SRY-T), FUNCTION (ISOFORMS SRY-S AND SRY-T), PROTEIN DEGRADATION
RP (ISOFORM SRY-S), TISSUE SPECIFICITY (ISOFORM SRY-T), MUTAGENESIS OF VAL-394
RP (ISOFORM SRY-S), AND DISRUPTION PHENOTYPE (ISOFORM SRY-T).
RX PubMed=33004521; DOI=10.1126/science.abb6430;
RA Miyawaki S., Kuroki S., Maeda R., Okashita N., Koopman P., Tachibana M.;
RT "The mouse Sry locus harbors a cryptic exon that is essential for male sex
RT determination.";
RL Science 370:121-124(2020).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
RC STRAIN=129;
RX PubMed=2374589; DOI=10.1038/346245a0;
RA Gubbay J., Collignon J., Koopman P., Capel B., Economou A., Munsterberg A.,
RA Vivian N., Goodfellow P., Lovell-Badge R.;
RT "A gene mapping to the sex-determining region of the mouse Y chromosome is
RT a member of a novel family of embryonically expressed genes.";
RL Nature 346:245-250(1990).
RN [6]
RP FUNCTION, AND CHARACTERIZATION OF DNA-BINDING.
RX PubMed=8190643; DOI=10.1093/nar/22.8.1500;
RA Harley V.R., Lovell-Badge R., Goodfellow P.N.;
RT "Definition of a consensus DNA binding site for SRY.";
RL Nucleic Acids Res. 22:1500-1501(1994).
RN [7]
RP FUNCTION, AND CHARACTERIZATION OF DNA-BINDING.
RX PubMed=8159753; DOI=10.1073/pnas.91.8.3368;
RA Giese K., Pagel J., Grosschedl R.;
RT "Distinct DNA-binding properties of the high mobility group domain of
RT murine and human SRY sex-determining factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3368-3372(1994).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=7600978; DOI=10.1242/dev.121.6.1603;
RA Hacker A., Capel B., Goodfellow P., Lovell-Badge R.;
RT "Expression of Sry, the mouse sex determining gene.";
RL Development 121:1603-1614(1995).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=7670499; DOI=10.1038/ng0895-480;
RA Jeske Y.W., Bowles J., Greenfield A., Koopman P.;
RT "Expression of a linear Sry transcript in the mouse genital ridge.";
RL Nat. Genet. 10:480-482(1995).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11085593; DOI=10.1007/s100480000093;
RA Mayer A., Mosler G., Just W., Pilgrim C., Reisert I.;
RT "Developmental profile of Sry transcripts in mouse brain.";
RL Neurogenetics 3:25-30(2000).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=11784049; DOI=10.1006/dbio.2001.0438;
RA Albrecht K.H., Eicher E.M.;
RT "Evidence that Sry is expressed in pre-Sertoli cells and Sertoli and
RT granulosa cells have a common precursor.";
RL Dev. Biol. 240:92-107(2001).
RN [12]
RP INTERACTION WITH KPNB1, AND SUBCELLULAR LOCATION.
RX PubMed=11535586; DOI=10.1074/jbc.m101668200;
RA Forwood J.K., Harley V., Jans D.A.;
RT "The C-terminal nuclear localization signal of the sex-determining region Y
RT (SRY) high mobility group domain mediates nuclear import through importin
RT beta 1.";
RL J. Biol. Chem. 276:46575-46582(2001).
RN [13]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15170344; DOI=10.1021/bi049920a;
RA Phillips N.B., Nikolskaya T., Jancso-Radek A., Ittah V., Jiang F.,
RA Singh R., Haas E., Weiss M.A.;
RT "Sry-directed sex reversal in transgenic mice is robust with respect to
RT enhanced DNA bending: comparison of human and murine HMG boxes.";
RL Biochemistry 43:7066-7081(2004).
RN [14]
RP ACETYLATION AT LYS-81, AND MUTAGENESIS OF LYS-81.
RX PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
RA Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
RA Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.;
RT "Regulation of human SRY subcellular distribution by its
RT acetylation/deacetylation.";
RL EMBO J. 23:3336-3345(2004).
RN [15]
RP INTERACTION WITH ZNF208 ISOFORM KRAB-O, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15469996; DOI=10.1095/biolreprod.104.034447;
RA Oh H.J., Li Y., Lau Y.-F.C.;
RT "Sry associates with the heterochromatin protein 1 complex by interacting
RT with a KRAB domain protein.";
RL Biol. Reprod. 72:407-415(2005).
RN [16]
RP INTERACTION WITH SLC9A3R2.
RX PubMed=16166090; DOI=10.1074/jbc.m504127200;
RA Thevenet L., Albrecht K.H., Malki S., Berta P., Boizet-Bonhoure B.,
RA Poulat F.;
RT "NHERF2/SIP-1 interacts with mouse SRY via a different mechanism than human
RT SRY.";
RL J. Biol. Chem. 280:38625-38630(2005).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16488877; DOI=10.1016/j.cub.2006.01.017;
RA Dewing P., Chiang C.W., Sinchak K., Sim H., Fernagut P.-O., Kelly S.,
RA Chesselet M.-F., Micevych P.E., Albrecht K.H., Harley V.R., Vilain E.;
RT "Direct regulation of adult brain function by the male-specific factor
RT SRY.";
RL Curr. Biol. 16:415-420(2006).
RN [18]
RP INTERACTION WITH PARP1, ADP-RIBOSYLATION, DNA-BINDING, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16904257; DOI=10.1016/j.mce.2006.06.008;
RA Li Y., Oh H.J., Lau Y.-F.C.;
RT "The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its
RT biological functions.";
RL Mol. Cell. Endocrinol. 257:35-46(2006).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=19349578; DOI=10.1083/jcb.200810106;
RA Gontan C., Guettler T., Engelen E., Demmers J., Fornerod M., Grosveld F.G.,
RA Tibboel D., Goerlich D., Poot R.A., Rottier R.J.;
RT "Exportin 4 mediates a novel nuclear import pathway for Sox family
RT transcription factors.";
RL J. Cell Biol. 185:27-34(2009).
RN [20]
RP REVIEW.
RX PubMed=16996051; DOI=10.1016/j.ydbio.2006.08.049;
RA Polanco J.C., Koopman P.;
RT "Sry and the hesitant beginnings of male development.";
RL Dev. Biol. 302:13-24(2007).
RN [21]
RP REVIEW.
RX PubMed=16414182; DOI=10.1016/j.mce.2005.12.011;
RA Oh H.J., Lau Y.F.;
RT "KRAB: a partner for SRY action on chromatin.";
RL Mol. Cell. Endocrinol. 247:47-52(2006).
CC -!- FUNCTION: Transcriptional regulator that controls a genetic switch in
CC male development (PubMed:33004521). It is necessary and sufficient for
CC initiating male sex determination by directing the development of
CC supporting cell precursors (pre-Sertoli cells) as Sertoli rather than
CC granulosa cells (PubMed:33004521). Involved in different aspects of
CC gene regulation including promoter activation or repression
CC (PubMed:8190643, PubMed:8159753, PubMed:15170344). Binds to the DNA
CC consensus sequence 5'-[AT]AACAA[AT]-3' (PubMed:8190643, PubMed:8159753,
CC PubMed:15170344). SRY HMG box recognizes DNA by partial intercalation
CC in the minor groove and promotes DNA bending (PubMed:8190643,
CC PubMed:8159753, PubMed:15170344). Also involved in pre-mRNA splicing
CC (By similarity). In male adult brain involved in the maintenance of
CC motor functions of dopaminergic neurons (By similarity).
CC {ECO:0000250|UniProtKB:P36394, ECO:0000250|UniProtKB:Q05066,
CC ECO:0000269|PubMed:15170344, ECO:0000269|PubMed:33004521,
CC ECO:0000269|PubMed:8159753, ECO:0000269|PubMed:8190643}.
CC -!- FUNCTION: [Isoform Sry-T]: Constitutes the major isoform, which is
CC necessary and sufficient for initiating male sex determination.
CC {ECO:0000269|PubMed:33004521}.
CC -!- FUNCTION: [Isoform Sry-S]: Constitutes a minor isoform, which is
CC unstable due to the presence of a degron at the C-terminus that
CC promotes its degradation (PubMed:33004521). Not necessary and
CC sufficient for initiating male sex determination (PubMed:33004521).
CC {ECO:0000269|PubMed:33004521}.
CC -!- SUBUNIT: Interacts with KPNB1, ZNF208 isoform KRAB-O, PARP1 and
CC SLC9A3R2 (PubMed:11535586, PubMed:15469996, PubMed:16166090,
CC PubMed:16904257). The interaction with KPNB1 is sensitive to
CC dissociation by Ran in the GTP-bound form (PubMed:11535586).
CC Interaction with PARP1 impaired its DNA-binding activity
CC (PubMed:16904257). Interacts with CALM, EP300, HDAC3 and WT1 (By
CC similarity). The interaction with EP300 modulates its DNA-binding
CC activity (By similarity). {ECO:0000250|UniProtKB:Q05066,
CC ECO:0000269|PubMed:11535586, ECO:0000269|PubMed:15469996,
CC ECO:0000269|PubMed:16166090, ECO:0000269|PubMed:16904257}.
CC -!- INTERACTION:
CC Q05738; Q15599: SLC9A3R2; Xeno; NbExp=5; IntAct=EBI-7820116, EBI-1149760;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}.
CC Cytoplasm {ECO:0000269|PubMed:11535586, ECO:0000269|PubMed:15469996,
CC ECO:0000269|PubMed:16488877, ECO:0000269|PubMed:19349578}. Nucleus
CC {ECO:0000269|PubMed:19349578}. Note=Acetylation contributes to its
CC nuclear localization and deacetylation by HDAC3 induces a cytoplasmic
CC delocalization (By similarity). Colocalizes in the nucleus with ZNF208
CC isoform KRAB-O and tyrosine hydroxylase (TH) (PubMed:15469996).
CC Colocalizes with SOX6 in speckles. Colocalizes with CAML in the nucleus
CC (By similarity). Nuclear import is facilitated by XPO4, a protein that
CC usually acts as a nuclear export signal receptor (PubMed:19349578).
CC {ECO:0000250|UniProtKB:Q05066, ECO:0000269|PubMed:15469996,
CC ECO:0000269|PubMed:19349578}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Sry-T {ECO:0000303|PubMed:33004521};
CC IsoId=Q05738-1; Sequence=Displayed;
CC Name=Sry-S {ECO:0000303|PubMed:33004521};
CC IsoId=Q05738-2; Sequence=VSP_060898;
CC -!- TISSUE SPECIFICITY: Expressed in gonadal somatic pre-Sertoli cells
CC (PubMed:11784049, PubMed:16904257, PubMed:7600978, PubMed:7670499).
CC Expressed in the substantia nigra of the brain (at protein level).
CC Expressed in diencephalon, cortex, the substantia nigra of the midbrain
CC and the medial mammillary bodies of the hypothalamus of male, but not
CC female. {ECO:0000269|PubMed:11085593, ECO:0000269|PubMed:11784049,
CC ECO:0000269|PubMed:15469996, ECO:0000269|PubMed:16488877,
CC ECO:0000269|PubMed:16904257, ECO:0000269|PubMed:7600978,
CC ECO:0000269|PubMed:7670499}.
CC -!- TISSUE SPECIFICITY: [Isoform Sry-T]: Expressed in gonadal somatic pre-
CC Sertoli cells (PubMed:33004521). While it is expressed at lower level
CC compared to isoform Sry-S, this form is more stable and constitutes the
CC predominant protein product of the Sry locus in XY gonads (at protein
CC level) (PubMed:33004521). {ECO:0000269|PubMed:33004521}.
CC -!- DEVELOPMENTAL STAGE: Expressed in gonadal somatic pre-Sertoli cells
CC from 10.5 to 11.5 dpc. Expressed in pre-Sertoli cells located centrally
CC in the genital ridge and then later in cells located at the cranial and
CC caudal poles (at protein level). {ECO:0000269|PubMed:11784049,
CC ECO:0000269|PubMed:16904257, ECO:0000269|PubMed:7600978,
CC ECO:0000269|PubMed:7670499}.
CC -!- DOMAIN: DNA binding and bending properties of the HMG domains of mouse
CC and human SRY differ form each other. Mouse SRY shows less extensive
CC minor groove contacts with DNA and a higher specificity of sequence
CC recognition than human SRY. {ECO:0000269|PubMed:8159753,
CC ECO:0000269|PubMed:8190643}.
CC -!- PTM: [Isoform Sry-S]: Degraded due to the presence of a degron at the
CC C-terminus that promotes its degradation.
CC {ECO:0000269|PubMed:33004521}.
CC -!- PTM: Phosphorylated on serine residues by PKA (By similarity).
CC Phosphorylation by PKA enhances its DNA-binding activity and stimulates
CC transcription repression (By similarity).
CC {ECO:0000250|UniProtKB:Q05066}.
CC -!- PTM: Acetylation of Lys-81 contributes to its nuclear localization and
CC enhances its interaction with KPNB1. {ECO:0000269|PubMed:15297880}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1 (PubMed:16904257). ADP-ribosylation
CC reduces its DNA-binding activity (PubMed:16904257).
CC {ECO:0000269|PubMed:16904257}.
CC -!- POLYMORPHISM: Different alleles occur in strains of Mus musculus
CC (molossinus or domesticus). In particular the poly-Gln region in 167-
CC 177 is polymorphic with either 11, 12 or 13 Gln. The nature of this
CC poly-Gln tract could affect the protein's function by disturbing its
CC secondary structure, perhaps by preventing efficient contact with
CC another protein. {ECO:0000269|PubMed:8012385}.
CC -!- DISRUPTION PHENOTYPE: [Isoform Sry-T]: Specific deletion of isoform
CC Sry-T in XY mice results in complete male-to-female sex reversal.
CC {ECO:0000269|PubMed:33004521}.
CC -!- MISCELLANEOUS: [Isoform Sry-T]: SRY protein has long been thought to be
CC encoded by a single exon, coding for Sry-S (PubMed:33004521). However,
CC in addition to the isoform coded by a single exon, Sry-S, an isoform
CC harboring an additional exon, isoform Sry-T, was identified
CC (PubMed:33004521). Isoform Sry-T constitues the major isoform, as
CC isoform Sry-S is unstable due to the presence of the degron at the C-
CC terminus (PubMed:33004521). {ECO:0000269|PubMed:33004521}.
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; X67204; CAB56798.1; -; Genomic_DNA.
DR EMBL; U03645; AAB60446.1; -; Genomic_DNA.
DR EMBL; LC532173; BCB24294.1; -; mRNA.
DR EMBL; X55491; CAA39111.1; -; Genomic_DNA.
DR CCDS; CCDS30545.1; -. [Q05738-2]
DR PIR; S35565; S35565.
DR PIR; S43344; S43344.
DR RefSeq; NP_035694.1; NM_011564.1. [Q05738-2]
DR AlphaFoldDB; Q05738; -.
DR SMR; Q05738; -.
DR BioGRID; 204096; 4.
DR IntAct; Q05738; 1.
DR MINT; Q05738; -.
DR STRING; 10090.ENSMUSP00000088717; -.
DR iPTMnet; Q05738; -.
DR PhosphoSitePlus; Q05738; -.
DR PaxDb; Q05738; -.
DR PRIDE; Q05738; -.
DR Antibodypedia; 599; 338 antibodies from 32 providers.
DR DNASU; 21674; -.
DR Ensembl; ENSMUST00000091178; ENSMUSP00000088717; ENSMUSG00000069036. [Q05738-2]
DR GeneID; 21674; -.
DR KEGG; mmu:21674; -.
DR UCSC; uc012hrv.1; mouse. [Q05738-1]
DR CTD; 6736; -.
DR MGI; MGI:98660; Sry.
DR VEuPathDB; HostDB:ENSMUSG00000069036; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000165583; -.
DR HOGENOM; CLU_698210_0_0_1; -.
DR InParanoid; Q05738; -.
DR OMA; QQFHDHH; -.
DR OrthoDB; 369754at2759; -.
DR PhylomeDB; Q05738; -.
DR BioGRID-ORCS; 21674; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q05738; -.
DR Proteomes; UP000000589; Chromosome Y.
DR RNAct; Q05738; protein.
DR Bgee; ENSMUSG00000069036; Expressed in gonad primordium and 21 other tissues.
DR ExpressionAtlas; Q05738; baseline and differential.
DR Genevisible; Q05738; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IDA:UniProtKB.
DR GO; GO:0030238; P:male sex determination; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007530; P:sex determination; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Activator; ADP-ribosylation; Alternative splicing;
KW Calmodulin-binding; Cytoplasm; Differentiation; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Sexual differentiation; Transcription;
KW Transcription regulation.
FT CHAIN 1..392
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048687"
FT DNA_BIND 5..73
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 4..81
FT /note="Sufficient for interaction with KPNB1"
FT /evidence="ECO:0000250|UniProtKB:Q05066"
FT REGION 6..22
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q05066"
FT REGION 52..84
FT /note="Sufficient for interaction with EP300"
FT /evidence="ECO:0000250|UniProtKB:Q05066"
FT REGION 75..81
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q05066"
FT REGION 92..144
FT /note="Necessary for interaction with ZNF208 isoform KRAB-
FT O"
FT /evidence="ECO:0000269|PubMed:15469996"
FT REGION 94..138
FT /note="Necessary for interaction with SLC9A3R2 and nuclear
FT accumulation of SLC9A3R2"
FT /evidence="ECO:0000269|PubMed:16166090"
FT REGION 142..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15297880"
FT VAR_SEQ 378..392
FT /note="WKGIKHCTGPDPEPF -> EHTPYQEHLSTALWLAVS (in isoform
FT Sry-S)"
FT /evidence="ECO:0000269|PubMed:33004521"
FT /id="VSP_060898"
FT VARIANT 63
FT /note="I -> T (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 133
FT /note="W -> L (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 143..145
FT /note="LQQ -> P (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 169..170
FT /note="Missing (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 209
FT /note="H -> Q (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 211
FT /note="E -> Q (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT VARIANT 235..392
FT /note="Missing (in strain: Torino)"
FT /evidence="ECO:0000269|PubMed:8012385"
FT MUTAGEN 81
FT /note="K->R: Abolishes acetylation."
FT /evidence="ECO:0000269|PubMed:15297880"
FT MOTIF Q05738-2:389..395
FT /note="Degron"
FT /evidence="ECO:0000269|PubMed:33004521"
FT MUTAGEN Q05738-2:394
FT /note="V->P: Eliminates the C-terminal degron and promotes
FT stabilization of the protein."
FT /evidence="ECO:0000269|PubMed:33004521"
SQ SEQUENCE 392 AA; 49124 MW; 00732B378D702B40 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 LTADITGWKG IKHCTGPDPE PF
