SRY_HORSE
ID SRY_HORSE Reviewed; 223 AA.
AC P36389; O18729; P79354;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=SRY; Synonyms=TDF;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Thoroughbred; TISSUE=Testis;
RX PubMed=10027176; DOI=10.1292/jvms.61.97;
RA Hasegawa T., Ishida M., Harigaya T., Sato F., Ishida N., Mukoyama H.;
RT "Linear SRY transcript in equine testis.";
RL J. Vet. Med. Sci. 61:97-100(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-108.
RX PubMed=9306070; DOI=10.1111/j.2042-3306.1997.tb03148.x;
RA Meyers-Wallen V.N., Hurtgen J., Schlafer D., Tulleners E., Cleland W.R.,
RA Ruth G.R., Acland G.M.;
RT "Sry-negative XX true hermaphroditism in a Pasa Fino horse.";
RL Equine Vet. J. 29:404-408(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-116.
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).
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 -!- PTM: Acetylation of Lys-130 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; AB004572; BAA22428.1; -; mRNA.
DR EMBL; U66067; AAC10937.1; -; Genomic_DNA.
DR EMBL; Z26908; CAA81534.1; -; Genomic_DNA.
DR RefSeq; NP_001075279.1; NM_001081810.1.
DR AlphaFoldDB; P36389; -.
DR SMR; P36389; -.
DR GeneID; 100033824; -.
DR CTD; 6736; -.
DR InParanoid; P36389; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 PIRSF; PIRSF037653; SRY; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Calmodulin-binding; Cytoplasm; Differentiation;
KW DNA-binding; Nucleus; Reference proteome; Repressor;
KW Sexual differentiation; Transcription; Transcription regulation.
FT CHAIN 1..223
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048670"
FT DNA_BIND 54..122
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 23..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 223 AA; 25353 MW; 3A5C34F8B272D0ED CRC64;
MSRVSNSDNY SLAGQQHTVL GSGRTSSLLW TSNPGSHFRS ETRGNGRENG QDRVKRPMNA
FMVWSRDHRR KVALENPQLQ NSEISKRLGC QWKMLTEAEK LPFFEEAQRL RAMHQEKYPD
YKYRPRRKAK MPQKSDKPLP QTPLLHCAGR RTYTSTSGCP FLIHGRLFLR ATQSQTGGAV
KPFAAGATAI SALQQELSQQ HRTLRCHSGN VGYADIRRRS LSL
