SRY_RAT
ID SRY_RAT Reviewed; 169 AA.
AC P36394; O88776; Q63558;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=Sry; Synonyms=Tdf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RC STRAIN=Brown Norway; TISSUE=Bone marrow, and Thymus;
RX PubMed=9203057;
RA An J., Beauchemin N., Albanese J., Abney T.O., Sullivan A.K.;
RT "Use of a rat cDNA probe specific for the Y chromosome to detect male-
RT derived cells.";
RL J. Androl. 18:289-293(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RX PubMed=9571157; DOI=10.1006/bbrc.1998.8441;
RA Margarit E., Guillen A., Rebordosa C., Vidal-Taboada J.M., Sanchez M.,
RA Ballesta F., Oliva R.;
RT "Identification of conserved potentially regulatory sequences of the SRY
RT gene from 10 different species of mammals.";
RL Biochem. Biophys. Res. Commun. 245:370-377(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-67.
RX PubMed=8162230; DOI=10.1111/j.1365-294x.1993.tb00034.x;
RA Griffiths R., Tiwari B.;
RT "Primers for the differential amplification of the sex-determining region Y
RT gene in a range of mammal species.";
RL Mol. Ecol. 2:405-406(1993).
RN [5]
RP FUNCTION, 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 [6]
RP INTERACTION WITH PARP1.
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 [7]
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 [8]
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:16996051, PubMed:16414182). It is necessary
CC and sufficient for initiating male sex determination by directing the
CC development of supporting cell precursors (pre-Sertoli cells) as
CC Sertoli rather than granulosa cells (PubMed:16996051, PubMed:16414182).
CC Involved in different aspects of gene regulation including promoter
CC activation or repression (PubMed:16488877). Binds to the DNA consensus
CC sequence 5'-[AT]AACAA[AT]-3' (By similarity). SRY HMG box recognizes
CC DNA by partial intercalation in the minor groove and promotes DNA
CC bending (By similarity). Also involved in pre-mRNA splicing (By
CC similarity). In male adult brain involved in the maintenance of motor
CC functions of dopaminergic neurons (PubMed:16488877).
CC {ECO:0000250|UniProtKB:Q05066, ECO:0000269|PubMed:16488877,
CC ECO:0000303|PubMed:16414182, ECO:0000303|PubMed:16996051}.
CC -!- SUBUNIT: Interacts with CALM, EP300, HDAC3, KPNB1, ZNF208 isoform KRAB-
CC O, SLC9A3R2 and WT1 (By similarity). The interaction with EP300
CC modulates its DNA-binding activity (By similarity). The interaction
CC with KPNB1 is sensitive to dissociation by Ran in the GTP-bound form
CC (By similarity). Interacts with PARP1; leading to impair its DNA-
CC binding activity (PubMed:16904257). {ECO:0000250|UniProtKB:Q05066,
CC ECO:0000269|PubMed:16904257}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}.
CC Cytoplasm {ECO:0000269|PubMed:16488877}. Nucleus
CC {ECO:0000269|PubMed:16488877}. Note=Acetylation contributes to its
CC nuclear localization and deacetylation by HDAC3 induces a cytoplasmic
CC delocalization. Colocalizes with SOX6 in speckles. Colocalizes with
CC CAML in the nucleus. Colocalizes in the nucleus with ZNF208 isoform
CC KRAB-O and tyrosine hydroxylase (TH). {ECO:0000250|UniProtKB:Q05066,
CC ECO:0000250|UniProtKB:Q05738}.
CC -!- TISSUE SPECIFICITY: Expressed in the substantia nigra (at protein
CC level). {ECO:0000269|PubMed:16488877}.
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; AC243442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X89730; CAA61882.1; -; Genomic_DNA.
DR EMBL; AJ222688; CAA10943.1; -; Genomic_DNA.
DR EMBL; Z26907; CAA81533.1; -; Genomic_DNA.
DR PIR; S58088; S58088.
DR RefSeq; NP_036904.1; NM_012772.1.
DR AlphaFoldDB; P36394; -.
DR SMR; P36394; -.
DR PRIDE; P36394; -.
DR GeneID; 25221; -.
DR KEGG; rno:25221; -.
DR CTD; 6736; -.
DR RGD; 3759; Sry.
DR InParanoid; P36394; -.
DR Proteomes; UP000002494; Chromosome Y.
DR Bgee; ENSRNOG00000062090; Expressed in lung and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0008301; F:DNA binding, bending; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
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; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0030238; P:male sex determination; IEP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:2000020; P:positive regulation of male gonad development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007530; P:sex determination; ISO:RGD.
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; Calmodulin-binding; Cytoplasm; Differentiation;
KW DNA-binding; Nucleus; Reference proteome; Repressor;
KW Sexual differentiation; Transcription; Transcription regulation.
FT CHAIN 1..169
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048706"
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:0000250|UniProtKB:Q05738"
FT REGION 94..138
FT /note="Necessary for interaction with SLC9A3R2 and nuclear
FT accumulation of SLC9A3R2"
FT /evidence="ECO:0000250|UniProtKB:Q05738"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05738"
FT CONFLICT 4
FT /note="H -> Q (in Ref. 2; CAA61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="R -> H (in Ref. 2; CAA61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="Q -> R (in Ref. 4; CAA81533)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="H -> Q (in Ref. 2; CAA61882)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="S -> M (in Ref. 3; CAA10943)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="F -> L (in Ref. 4; CAA81533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 20465 MW; D3A027A6735FE432 CRC64;
MEGHVKRPMN AFMVWSRGER RKLAQQNPSM QNSEISKHLG YQWKSLTEAE KRPFFQEAQR
LKTLHREKYP NYKYQPHRRV KVPQRSYTLQ REVASTKLYN LLQWDNNLHT IIYGQDWARA
AHQSSKNQKS IYLQPVDIPT GYPLQQKQQH QQQQHVHLQQ QQQQQHQFH
