SRY_PIG
ID SRY_PIG Reviewed; 236 AA.
AC P36393;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=SRY; Synonyms=TDF;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Urogenital ridge;
RX PubMed=8793057; DOI=10.1095/biolreprod55.1.47;
RA Daneau I., Ethier J.F., Lussier J.G., Silversides D.W.;
RT "Porcine SRY gene locus and genital ridge expression.";
RL Biol. Reprod. 55:47-53(1996).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Silversides D.W.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-123.
RC STRAIN=Large white; TISSUE=Blood;
RX PubMed=7818163; DOI=10.1111/j.1365-2052.1994.tb00362.x;
RA Pailhoux E., Popescu P.C., Parma P., Boscher J., Legault C., Molteni L.,
RA Fellous M., Cotinot C.;
RT "Genetic analysis of 38XX males with genital ambiguities and true
RT hermaphrodites in pigs.";
RL Anim. Genet. 25:299-305(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-121.
RX PubMed=7665371; DOI=10.2527/1995.7351408x;
RA Pomp D., Good B.A., Geisert R.D., Corbin C.J., Conley A.J.;
RT "Sex identification in mammals with polymerase chain reaction and its use
RT to examine sex effects on diameter of day-10 or -11 pig embryos.";
RL J. Anim. Sci. 73:1408-1415(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-124.
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:Q05738}. Nucleus
CC {ECO:0000250|UniProtKB:Q05066}. 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) (By similarity).
CC Colocalizes with SOX6 in speckles. Colocalizes with CAML in the nucleus
CC (By similarity). {ECO:0000250|UniProtKB:Q05066,
CC ECO:0000250|UniProtKB:Q05738}.
CC -!- TISSUE SPECIFICITY: Expressed in the genital ridge.
CC {ECO:0000269|PubMed:8793057}.
CC -!- DEVELOPMENTAL STAGE: Expressed in male pig embryo between E21 and E26.
CC Not detected in E31 embryos. {ECO:0000269|PubMed:8793057}.
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; U49860; AAB00690.2; -; Genomic_DNA.
DR EMBL; Z23070; CAA80611.1; -; Genomic_DNA.
DR EMBL; S79625; AAD14313.1; -; Genomic_DNA.
DR EMBL; Z26909; CAA81535.1; -; Genomic_DNA.
DR PIR; I47151; I47151.
DR RefSeq; NP_999617.2; NM_214452.3.
DR AlphaFoldDB; P36393; -.
DR SMR; P36393; -.
DR STRING; 9823.ENSSSCP00000025359; -.
DR PaxDb; P36393; -.
DR Ensembl; ENSSSCT00000030781; ENSSSCP00000025359; ENSSSCG00000037443.
DR Ensembl; ENSSSCT00070004025; ENSSSCP00070003331; ENSSSCG00070002152.
DR GeneID; 407740; -.
DR KEGG; ssc:407740; -.
DR CTD; 6736; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000165583; -.
DR InParanoid; P36393; -.
DR OMA; DCTKATH; -.
DR OrthoDB; 369754at2759; -.
DR Reactome; R-SSC-3769402; Deactivation of the beta-catenin transactivating complex.
DR Proteomes; UP000008227; Chromosome Y.
DR Proteomes; UP000314985; Unassembled WGS sequence.
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 Activator; Calmodulin-binding; Cytoplasm; Differentiation; DNA-binding;
KW Nucleus; Reference proteome; Sexual differentiation; Transcription;
KW Transcription regulation.
FT CHAIN 1..236
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048704"
FT DNA_BIND 62..130
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 32..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 236 AA; 27019 MW; 1A8E068283FE8E80 CRC64;
MVQSYASAMF RVLKADDYSP AAQQQNILAL GKGSSLFPTD NHSSNDGRET RGSGRESGQD
RVKRPMNAFI VWSRDQRRKV ALENPQMQNS EISKWLGCKW KMLTEAEKRP FFEEAQRLQA
VHRDKYPGYK YRPRRKGERA QNLLPAEAAV LCSQVRVEER MYPFTYTVAK AKCSGTESQL
SHSQPMNITS SLLQQEDRCN WTGLCHSRVT STGQIRADLP FHRGLQPGLS HIYFPY
