ID   SRY_PHOPH               Reviewed;         196 AA.
AC   Q864Q2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Sex-determining region Y protein;
DE   AltName: Full=Testis-determining factor;
GN   Name=SRY; Synonyms=TDF;
OS   Phocoena phocoena (Harbor porpoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Phocoenidae; Phocoena.
OX   NCBI_TaxID=9742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nishida S., Pastene L.A., Goto M., Koike H.;
RT   "SRY gene structure and phylogeny in the cetacean species.";
RL   Mammal Study 28:57-66(2003).
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   -!- 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; AB108519; BAC75651.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q864Q2; -.
DR   SMR; Q864Q2; -.
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   Activator; Calmodulin-binding; Cytoplasm; Differentiation; DNA-binding;
KW   Nucleus; Sexual differentiation; Transcription; Transcription regulation.
FT   CHAIN           1..196
FT                   /note="Sex-determining region Y protein"
FT                   /id="PRO_0000048701"
FT   DNA_BIND        54..122
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   196 AA;  22487 MW;  39390F4F7C4594C4 CRC64;
     MFRIVNGEDY SPAVQQRNIL DFGKAPSLLW TDNGSSNDRC DTGGNCRESG QDRVKRPMNA
     FIVWSRDQRR KVALENPQMQ NSEISKRLGY DWKMLTEAEK QPFFEEAQRL RAMHRDKYPG
     YKYRPRRKAK EATEIASRRL FSTVQPNAHR GDLVPLHIQG HTFTNGKPVK PLTAHEHKQL
     TPATGASQQS DKPAPQ