SRY_PONPY
ID SRY_PONPY Reviewed; 233 AA.
AC Q28783;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Sex-determining region Y protein;
DE AltName: Full=Testis-determining factor;
GN Name=SRY; Synonyms=TDF;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8355783; DOI=10.1038/364713a0;
RA Whitfield L.S., Lovell-Badge R., Goodfellow P.N.;
RT "Rapid sequence evolution of the mammalian sex-determining gene SRY.";
RL Nature 364:713-715(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-136 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; X86383; CAA60143.1; -; Genomic_DNA.
DR PIR; S35561; S35561.
DR AlphaFoldDB; Q28783; -.
DR SMR; Q28783; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030238; P:male sex determination; IEA:InterPro.
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 3: Inferred from homology;
KW Acetylation; Activator; Calmodulin-binding; Cytoplasm; Differentiation;
KW DNA-binding; Nucleus; Sexual differentiation; Transcription;
KW Transcription regulation.
FT CHAIN 1..233
FT /note="Sex-determining region Y protein"
FT /id="PRO_0000048705"
FT DNA_BIND 60..128
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 180..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 27118 MW; AFBA8B596AFB2C75 CRC64;
MQSYASAMLS VFNSDDYSPA VQQNIPALRR SSSFICTESY NSKYQCETGE NSKGSVQDRV
KRPMNAFIVW SRDQRRKMAL ENPKMRNSEI SKQLGYQWKM LTEAEKWPFF QEAQKLQAMH
REKYPNYKYR PRRKAKMLQK SCSSLPADPA SVLCSEVLQL DNRLYRDDCT KATHSRLEHQ
LGHLPPINTA SSPQQRDRYS HSTELYDNRV TLATKTYLDA AFYDNLQPSL SYV