SP9_MOUSE
ID SP9_MOUSE Reviewed; 484 AA.
AC Q64HY3; Q5QR89;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transcription factor Sp9;
GN Name=Sp9;
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] (ISOFORM 1), FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=15358670; DOI=10.1242/dev.01331;
RA Kawakami Y., Rodriguez Esteban C., Matsui T., Rodriguez-Leon J., Kato S.,
RA Izpisua Belmonte J.C.;
RT "Sp8 and Sp9, two closely related buttonhead-like transcription factors,
RT regulate Fgf8 expression and limb outgrowth in vertebrate embryos.";
RL Development 131:4763-4774(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Favot L., Balmer J., Scott C., Kemp P.R.;
RT "Sp8 and Sp9 two novel murine Sp proteins are activators and inhibitors of
RT promoter activity.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor which plays a key role in limb
CC development. Positively regulates FGF8 expression in the apical
CC ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
CC {ECO:0000269|PubMed:15358670}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64HY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64HY3-2; Sequence=VSP_039467;
CC -!- DEVELOPMENTAL STAGE: Detected in the apical ectodermal ridge (AER)
CC during limb development as well as in the distal region of the
CC ectoderm. {ECO:0000269|PubMed:15358670}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In SP9, the motif is
CC inactive. {ECO:0000250|UniProtKB:P0CG40}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AY591908; AAU04517.1; -; mRNA.
DR EMBL; AJ844915; CAH59970.1; -; mRNA.
DR EMBL; AL954713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139398; AAI39399.1; -; mRNA.
DR EMBL; BC139407; AAI39408.1; -; mRNA.
DR CCDS; CCDS16126.1; -. [Q64HY3-1]
DR RefSeq; NP_001005343.1; NM_001005343.2. [Q64HY3-1]
DR AlphaFoldDB; Q64HY3; -.
DR SMR; Q64HY3; -.
DR STRING; 10090.ENSMUSP00000088322; -.
DR iPTMnet; Q64HY3; -.
DR PhosphoSitePlus; Q64HY3; -.
DR MaxQB; Q64HY3; -.
DR PaxDb; Q64HY3; -.
DR PRIDE; Q64HY3; -.
DR ProteomicsDB; 263300; -. [Q64HY3-1]
DR ProteomicsDB; 263301; -. [Q64HY3-2]
DR Antibodypedia; 57975; 19 antibodies from 7 providers.
DR DNASU; 381373; -.
DR Ensembl; ENSMUST00000090813; ENSMUSP00000088322; ENSMUSG00000068859. [Q64HY3-1]
DR GeneID; 381373; -.
DR KEGG; mmu:381373; -.
DR UCSC; uc008kcj.2; mouse. [Q64HY3-1]
DR CTD; 100131390; -.
DR MGI; MGI:3574660; Sp9.
DR VEuPathDB; HostDB:ENSMUSG00000068859; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162304; -.
DR HOGENOM; CLU_019484_4_1_1; -.
DR InParanoid; Q64HY3; -.
DR OMA; HHHATSV; -.
DR OrthoDB; 664813at2759; -.
DR PhylomeDB; Q64HY3; -.
DR TreeFam; TF350150; -.
DR BioGRID-ORCS; 381373; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q64HY3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64HY3; protein.
DR Bgee; ENSMUSG00000068859; Expressed in olfactory bulb and 27 other tissues.
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: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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..484
FT /note="Transcription factor Sp9"
FT /id="PRO_0000395451"
FT ZN_FING 332..356
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..386
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 409..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..186
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000250|UniProtKB:P0CG40"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_039467"
FT CONFLICT 273
FT /note="A -> S (in Ref. 2; CAH59970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 48959 MW; 57ADE8A82E9B12E7 CRC64;
MATSILGEEP RFGTTPLAML AATCNKIGNT SPLTTLPESS AFAKGGFHPW KRSSSSCNLG
SSLSGFAVAT GGRGSGSLAG GSGAANSAFC LASTSPTSSA FSSDYGGLFS NSAAAAAAAA
GVSPQEAGGQ SAFISKVHTT AADGLYPRVG MAHPYESWYK SGFHSTLAAG EVTNGAASSW
WDVHSSPGSW LEVQNPAGGL QSSLHSGAPQ ASLHSQLGTY NPDFSSLTHS AFSSTGLGSS
AAAASHLLST SQHLLAQDGF KPVLPSYSDS SAAVAAAAAS AMISGAAAAA AGGSSARSAR
RYSGRATCDC PNCQEAERLG PAGASLRRKG LHSCHIPGCG KVYGKTSHLK AHLRWHTGER
PFVCNWLFCG KRFTRSDELQ RHLRTHTGEK RFACPVCNKR FMRSDHLSKH IKTHNGGGGG
KKGSDSDTDA SNLETPRSES PDLILHDSGV SAARAAAAAA AAAAAAAAAA SAGGKEAATG
PNDS
