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SAM pointed domain-containing Ets transcription factor (Prostate epithelium-specific Ets transcription factor) (Prostate-specific Ets) (Prostate-derived Ets factor)

 SPDEF_HUMAN             Reviewed;         335 AA.
O95238; B4DWH8; F5H778;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=SAM pointed domain-containing Ets transcription factor;
AltName: Full=Prostate epithelium-specific Ets transcription factor;
Short=Prostate-specific Ets;
AltName: Full=Prostate-derived Ets factor;
Name=SPDEF; Synonyms=PDEF, PSE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostatic carcinoma;
PubMed=10675039; DOI=10.1016/S0378-1119(99)00484-9;
Yamada N., Tamai Y., Miyamoto H., Nozaki M.;
"Cloning and expression of the mouse Pse gene encoding a novel Ets
family member.";
Gene 241:267-274(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH AR.
TISSUE=Prostate;
PubMed=10625666; DOI=10.1074/jbc.275.2.1216;
Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J.,
Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G.,
Kunsch C., Libermann T.A.;
"PDEF, a novel prostate epithelium-specific ets transcription factor,
interacts with the androgen receptor and activates prostate-specific
antigen gene expression.";
J. Biol. Chem. 275:1216-1225(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH NKX3-1.
PubMed=11809674;
Chen H., Nandi A.K., Li X., Bieberich C.J.;
"NKX-3.1 interacts with prostate-derived Ets factor and regulates the
activity of the PSA promoter.";
Cancer Res. 62:338-340(2002).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 247-335 IN COMPLEX WITH DNA.
PubMed=15882048; DOI=10.1021/bi047352t;
Wang Y., Feng L., Said M., Balderman S., Fayazi Z., Liu Y., Ghosh D.,
Gulick A.M.;
"Analysis of the 2.0 A crystal structure of the protein-DNA complex of
the human PDEF Ets domain bound to the prostate specific antigen
regulatory site.";
Biochemistry 44:7095-7106(2005).
[8]
STRUCTURE BY NMR OF 131-213.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SAM_pnt-domain of ETS transcription factor
PDEF (prostate Ets).";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: May function as an androgen-independent transactivator
of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-
3' DNA sequences. May play a role in the regulation of the
prostate gland and/or prostate cancer development. Acts as a
transcriptional activator for SERPINB5 promoter.
{ECO:0000269|PubMed:10625666}.
-!- SUBUNIT: Interacts with the DNA-binding domain of the androgen
receptor. Interacts with NKX3-1. {ECO:0000269|PubMed:10625666,
ECO:0000269|PubMed:11809674, ECO:0000269|PubMed:15882048}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95238-1; Sequence=Displayed;
Name=2;
IsoId=O95238-2; Sequence=VSP_044722;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in a very restricted set of
primarily hormone-regulated epithelial tissues with particularly
high expression in the prostate gland. Significantly lower
expression is seen in other hormone regulated tissues such as
mammary gland, salivary gland, and ovary. Expressed in prostate
carcinoma cells. {ECO:0000269|PubMed:10625666}.
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB031549; BAA89543.1; -; mRNA.
EMBL; AF071538; AAC95296.1; -; mRNA.
EMBL; AK301543; BAG63040.1; -; mRNA.
EMBL; BX255971; CAI23605.1; -; Genomic_DNA.
EMBL; AL157372; CAI23605.1; JOINED; Genomic_DNA.
EMBL; BX255972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX255973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021299; AAH21299.1; -; mRNA.
CCDS; CCDS4794.1; -. [O95238-1]
CCDS; CCDS59013.1; -. [O95238-2]
RefSeq; NP_001239223.1; NM_001252294.1. [O95238-2]
RefSeq; NP_036523.1; NM_012391.2. [O95238-1]
UniGene; Hs.485158; -.
PDB; 1YO5; X-ray; 2.00 A; C=247-335.
PDB; 2DKX; NMR; -; A=131-213.
PDBsum; 1YO5; -.
PDBsum; 2DKX; -.
ProteinModelPortal; O95238; -.
SMR; O95238; -.
BioGrid; 117335; 14.
IntAct; O95238; 7.
STRING; 9606.ENSP00000363149; -.
iPTMnet; O95238; -.
PhosphoSitePlus; O95238; -.
BioMuta; SPDEF; -.
EPD; O95238; -.
MaxQB; O95238; -.
PaxDb; O95238; -.
PeptideAtlas; O95238; -.
PRIDE; O95238; -.
DNASU; 25803; -.
Ensembl; ENST00000374037; ENSP00000363149; ENSG00000124664. [O95238-1]
Ensembl; ENST00000544425; ENSP00000442715; ENSG00000124664. [O95238-2]
GeneID; 25803; -.
KEGG; hsa:25803; -.
UCSC; uc003ojq.3; human. [O95238-1]
CTD; 25803; -.
DisGeNET; 25803; -.
EuPathDB; HostDB:ENSG00000124664.10; -.
GeneCards; SPDEF; -.
HGNC; HGNC:17257; SPDEF.
HPA; HPA055707; -.
MIM; 608144; gene.
neXtProt; NX_O95238; -.
OpenTargets; ENSG00000124664; -.
PharmGKB; PA134993886; -.
eggNOG; KOG3805; Eukaryota.
eggNOG; ENOG410XSXU; LUCA.
GeneTree; ENSGT00760000118996; -.
HOGENOM; HOG000237327; -.
HOVERGEN; HBG080776; -.
InParanoid; O95238; -.
KO; K09442; -.
OMA; YPEDSSW; -.
OrthoDB; EOG091G07NK; -.
PhylomeDB; O95238; -.
TreeFam; TF318679; -.
EvolutionaryTrace; O95238; -.
GeneWiki; SPDEF; -.
GenomeRNAi; 25803; -.
PRO; PR:O95238; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124664; -.
CleanEx; HS_SPDEF; -.
Genevisible; O95238; HS.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
GO; GO:0060480; P:lung goblet cell differentiation; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0010454; P:negative regulation of cell fate commitment; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:BHF-UCL.
GO; GO:0010455; P:positive regulation of cell fate commitment; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR003118; Pointed_dom.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00178; Ets; 1.
Pfam; PF02198; SAM_PNT; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SMART; SM00251; SAM_PNT; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
PROSITE; PS51433; PNT; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Nucleus; Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 335 SAM pointed domain-containing Ets
transcription factor.
/FTId=PRO_0000223958.
DOMAIN 129 213 PNT. {ECO:0000255|PROSITE-
ProRule:PRU00762}.
DNA_BIND 249 332 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
VAR_SEQ 212 227 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044722.
VARIANT 57 57 A -> T (in dbSNP:rs2233639).
/FTId=VAR_048955.
CONFLICT 49 49 A -> G (in Ref. 3; BAG63040).
{ECO:0000305}.
CONFLICT 76 76 K -> N (in Ref. 3; BAG63040).
{ECO:0000305}.
HELIX 132 139 {ECO:0000244|PDB:2DKX}.
TURN 140 142 {ECO:0000244|PDB:2DKX}.
HELIX 147 149 {ECO:0000244|PDB:2DKX}.
HELIX 155 165 {ECO:0000244|PDB:2DKX}.
HELIX 172 175 {ECO:0000244|PDB:2DKX}.
HELIX 180 185 {ECO:0000244|PDB:2DKX}.
HELIX 188 194 {ECO:0000244|PDB:2DKX}.
STRAND 196 198 {ECO:0000244|PDB:2DKX}.
HELIX 200 213 {ECO:0000244|PDB:2DKX}.
HELIX 251 260 {ECO:0000244|PDB:1YO5}.
HELIX 262 265 {ECO:0000244|PDB:1YO5}.
TURN 266 268 {ECO:0000244|PDB:1YO5}.
STRAND 269 273 {ECO:0000244|PDB:1YO5}.
TURN 274 277 {ECO:0000244|PDB:1YO5}.
STRAND 278 282 {ECO:0000244|PDB:1YO5}.
HELIX 284 295 {ECO:0000244|PDB:1YO5}.
HELIX 302 311 {ECO:0000244|PDB:1YO5}.
TURN 312 316 {ECO:0000244|PDB:1YO5}.
STRAND 317 319 {ECO:0000244|PDB:1YO5}.
STRAND 328 332 {ECO:0000244|PDB:1YO5}.
SEQUENCE 335 AA; 37518 MW; D3117E1AEEBA95EC CRC64;
MGSASPGLSS VSPSHLLLPP DTVSRTGLEK AAAGAVGLER RDWSPSPPAT PEQGLSAFYL
SYFDMLYPED SSWAAKAPGA SSREEPPEEP EQCPVIDSQA PAGSLDLVPG GLTLEEHSLE
QVQSMVVGEV LKDIETACKL LNITADPMDW SPSNVQKWLL WTEHQYRLPP MGKAFQELAG
KELCAMSEEQ FRQRSPLGGD VLHAHLDIWK SAAWMKERTS PGAIHYCAST SEESWTDSEV
DSSCSGQPIH LWQFLKELLL KPHSYGRFIR WLNKEKGIFK IEDSAQVARL WGIRKNRPAM
NYDKLSRSIR QYYKKGIIRK PDISQRLVYQ FVHPI


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