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SP5_MOUSE
ID   SP5_MOUSE               Reviewed;         398 AA.
AC   Q9JHX2; Q149T2;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Transcription factor Sp5;
GN   Name=Sp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RX   PubMed=11071760; DOI=10.1006/dbio.2000.9878;
RA   Harrison S.M., Houzelstein D., Dunwoodie S.L., Beddington R.S.P.;
RT   "Sp5, a new member of the Sp1 family, is dynamically expressed during
RT   development and genetically interacts with Brachyury.";
RL   Dev. Biol. 227:358-372(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds to GC boxes promoters elements. Probable
CC       transcriptional activator that has a role in the coordination of
CC       changes in transcription required to generate pattern in the developing
CC       embryo.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:Q6BEB4}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF279479; AAF87798.1; -; mRNA.
DR   EMBL; AK036234; BAC29355.1; -; mRNA.
DR   EMBL; BC116691; AAI16692.1; -; mRNA.
DR   EMBL; BC117505; AAI17506.1; -; mRNA.
DR   CCDS; CCDS16106.1; -.
DR   RefSeq; NP_071880.1; NM_022435.2.
DR   AlphaFoldDB; Q9JHX2; -.
DR   SMR; Q9JHX2; -.
DR   STRING; 10090.ENSMUSP00000097620; -.
DR   PhosphoSitePlus; Q9JHX2; -.
DR   MaxQB; Q9JHX2; -.
DR   PaxDb; Q9JHX2; -.
DR   PRIDE; Q9JHX2; -.
DR   Antibodypedia; 53490; 52 antibodies from 21 providers.
DR   DNASU; 64406; -.
DR   Ensembl; ENSMUST00000100043; ENSMUSP00000097620; ENSMUSG00000075304.
DR   GeneID; 64406; -.
DR   KEGG; mmu:64406; -.
DR   UCSC; uc008jzg.1; mouse.
DR   CTD; 389058; -.
DR   MGI; MGI:1927715; Sp5.
DR   VEuPathDB; HostDB:ENSMUSG00000075304; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160673; -.
DR   HOGENOM; CLU_019484_5_0_1; -.
DR   InParanoid; Q9JHX2; -.
DR   OMA; PGGCGHR; -.
DR   OrthoDB; 1085860at2759; -.
DR   PhylomeDB; Q9JHX2; -.
DR   TreeFam; TF350150; -.
DR   BioGRID-ORCS; 64406; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Sp5; mouse.
DR   PRO; PR:Q9JHX2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9JHX2; protein.
DR   Bgee; ENSMUSG00000075304; Expressed in 1st arch pharyngeal cleft and 102 other tissues.
DR   Genevisible; Q9JHX2; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISS:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0060349; P:bone morphogenesis; IGI:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IGI:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..398
FT                   /note="Transcription factor Sp5"
FT                   /id="PRO_0000047147"
FT   ZN_FING         296..320
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         326..350
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         356..378
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          160..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           187..195
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q6BEB4"
FT   COMPBIAS        160..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  42052 MW;  B359853755B6B5C9 CRC64;
     MAAVAVLRND SLQAFLQDRT PSASPDLGKH SPLALLAATC SRIGQPGAAA APDFLQVPYD
     PALGSPSRLF HPWTADMPAH SPGALPPPHP SLGLTPQKTH LQPSFGAAHE LPLTPPADPS
     YPYEFSPVKM LPSSMAALPA SCAPAYVPYA AQAALPPGYS NLLPPPPPPP PPPTCRQLSP
     APAPDDLPWW SIPQSGAGPG SSGVPGTSLS SACAGPPHAP RFPASAAAAA AAAAALQRGL
     VLGPSDFAQY QSQIAALLQT KAPLAATARR CRRCRCPNCQ AAGGAPEAEP GKKKQHVCHV
     PGCGKVYGKT SHLKAHLRWH TGERPFVCNW LFCGKSFTRS DELQRHLRTH TGEKRFACPE
     CGKRFMRSDH LAKHVKTHQN KKLKVAEAGV KRENPRDL
 
 
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