SALL3_MOUSE
ID SALL3_MOUSE Reviewed; 1320 AA.
AC Q62255; Q08EB0; Q52KR5; Q6GQT8; Q8BRD9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sal-like protein 3;
DE AltName: Full=MSal;
DE AltName: Full=Spalt-like protein 3;
GN Name=Sall3; Synonyms=Sal;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1320 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-1320 (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Embryo;
RX PubMed=8798152; DOI=10.1016/0925-4773(96)00516-3;
RA Ott T., Kaestner K.H., Monaghan A.P., Schuetz G.;
RT "The mouse homolog of the region specific homeotic gene spalt of Drosophila
RT is expressed in the developing nervous system and in mesoderm-derived
RT structures.";
RL Mech. Dev. 56:117-128(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 692-1320.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP DOMAIN.
RX PubMed=16545361; DOI=10.1016/j.ydbio.2006.02.009;
RA Sweetman D., Muensterberg A.;
RT "The vertebrate spalt genes in development and disease.";
RL Dev. Biol. 293:285-293(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Probable transcription factor.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62255-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62255-2; Sequence=VSP_006834;
CC -!- TISSUE SPECIFICITY: In adult brain, testis and kidney. In lower levels
CC also in adult ovaries and embryonic stem cells. In embryo in developing
CC neuroectoderm of brain, inner ear and spinal chord. Also weakly and
CC transiently expressed in embryonic branchial arches, notochord, limb
CC buds and heart.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis detected from 7 dpc onward in
CC tissues derived from mesoderm and ectoderm.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks two zinc finger domains (6 and 7) and
CC is the major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC125210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072631; AAH72631.1; -; mRNA.
DR EMBL; AK045051; BAC32197.1; ALT_INIT; mRNA.
DR EMBL; X97581; CAA66196.1; ALT_TERM; mRNA.
DR CCDS; CCDS29371.1; -. [Q62255-2]
DR CCDS; CCDS89289.1; -. [Q62255-1]
DR PIR; T30253; T30253.
DR RefSeq; NP_840064.2; NM_178280.3. [Q62255-2]
DR AlphaFoldDB; Q62255; -.
DR BioGRID; 203420; 18.
DR IntAct; Q62255; 5.
DR MINT; Q62255; -.
DR STRING; 10090.ENSMUSP00000056967; -.
DR iPTMnet; Q62255; -.
DR PhosphoSitePlus; Q62255; -.
DR MaxQB; Q62255; -.
DR PaxDb; Q62255; -.
DR PeptideAtlas; Q62255; -.
DR PRIDE; Q62255; -.
DR ProteomicsDB; 255454; -. [Q62255-1]
DR ProteomicsDB; 255455; -. [Q62255-2]
DR Antibodypedia; 49173; 27 antibodies from 13 providers.
DR DNASU; 20689; -.
DR Ensembl; ENSMUST00000057950; ENSMUSP00000056967; ENSMUSG00000024565. [Q62255-2]
DR GeneID; 20689; -.
DR KEGG; mmu:20689; -.
DR UCSC; uc008ftl.2; mouse. [Q62255-1]
DR UCSC; uc008ftm.1; mouse. [Q62255-2]
DR CTD; 27164; -.
DR MGI; MGI:109295; Sall3.
DR VEuPathDB; HostDB:ENSMUSG00000024565; -.
DR eggNOG; KOG1074; Eukaryota.
DR GeneTree; ENSGT00940000159356; -.
DR HOGENOM; CLU_005740_0_0_1; -.
DR InParanoid; Q62255; -.
DR OrthoDB; 244207at2759; -.
DR PhylomeDB; Q62255; -.
DR TreeFam; TF317003; -.
DR BioGRID-ORCS; 20689; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q62255; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q62255; protein.
DR Bgee; ENSMUSG00000024565; Expressed in spinal cord mantle layer and 113 other tissues.
DR ExpressionAtlas; Q62255; baseline and differential.
DR Genevisible; Q62255; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0035136; P:forelimb morphogenesis; IGI:MGI.
DR GO; GO:0035137; P:hindlimb morphogenesis; IGI:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0021891; P:olfactory bulb interneuron development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
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..1320
FT /note="Sal-like protein 3"
FT /id="PRO_0000047025"
FT ZN_FING 51..73
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000303|PubMed:16545361"
FT ZN_FING 427..449
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..714
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..742
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 752..774
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 997..1019
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1025..1047
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1133..1155
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1161..1183
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA9"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA9"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA9"
FT VAR_SEQ 993..1064
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8798152"
FT /id="VSP_006834"
FT CONFLICT 131..132
FT /note="EP -> S (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="A -> G (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..256
FT /note="TA -> NT (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="C -> CC (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 497..498
FT /note="NV -> KC (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="A -> G (in Ref. 3; CAA66196)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="V -> I (in Ref. 4; BAC32197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1320 AA; 138760 MW; 33A19F56C69D5EEB CRC64;
MSRRKQAKPQ HLKSDEELPP QDGASEHGVP GDGAEDADSG SESRSGSEET SVCEKCCAEF
FKWADFLQHK KTCTKNPLVL IVHDDEPAPP SEDFPEPSPA SSPSDRTESE VAEEVAPTEG
SEVKAATKEA EPMDVEVSTD KGPPGPSVPP PPPALPPQPE PAAFSMPSTN VTLETLLSTK
VAVAQFSQGA RAGGTTGAGG SVGAVAIPMI LEQLVALQQQ QIHQLQLIEQ IRSQVALMSR
QPGPPLKPSA SAPGTASVQL QGLTPHAALQ LSAGPATASA GSGSTLPAAF DGPQHLSQPA
SGTSTPCSTS AAPPDSGAHP ACSTGPAPGA VAAASSTVGN AVQPQNASTP PALGPGPLLS
SASNLPNPLL PQTSSSSVIF PNPLVSIAAT ANALDPLSAL MKHRKGKPPN VSVFEPKASA
EDPFFKHKCR FCAKVFGSDS ALQIHLRSHT GERPFKCNIC GNRFSTKGNL KVHFQRHKEK
YPHIQMNPYP VPEYLDNVPT CSGIPYGMSL PPEKPVTTWL DSKPVLPTVP TSVGLQLPPT
VPGTHNYTDS PSITPVSRSP QRPSPASSEC TSLSPGLNNT ESGITVRPES PQPLLGGPSL
TKAEPVSLPC TSTRTGDAPV VGGQVSGLPT SAATAVTDSA CTSLGSPGLP AVSDQFKAQF
PFGGLLDSMQ TSETSKLQQL VENIDKKMTD PNQCVICHRV LSCQSALKMH YRTHTGERPF
KCKICGRAFT TKGNLKTHFG VHRAKPPLRV QHSCPICQKK FTNAVVLQQH IRMHMGGQIP
NTPLPEGLQE AMDADLPFDE KNAETLSSFD DDIDENSMEE DSELKDTASD SSKPLLSYSG
SCPPSPPSVI SSIAALENQM KMIDSVMNCQ QLANLKSVEN GSGESDRLSN DSSSAVGDLE
SRSAGSPALS ESSSSQALSP AHSNGESFRS KSPGLGHQED PQEIPLKTER LDSPPPGPGN
GGALDLTAGH PGRPLIKEEA PFSLLFLSRE RGKCASTVCG VCGKPFACKS ALEIHYRSHT
KERRFVCTVC RRGCSTMGNL KQHLLTHKLK ELPSQVFDPN FTLGPSHSTP SLASSPAPTM
IKMEVNGHSK AIALGEGPAL PAGVQVPTGP QTVMSPGLAP MLAPPPRRTP KQHNCQSCGK
TFSSASALQI HERTHTGEKP FGCTICGRAF TTKGNLKVHM GTHMWNNAPA RRGRRLSVEN
PMALLGGDAL KFSEMFQKDL AARAMNVDPS FWNQYAAAIT NGLAMKNNEI SVIQNGGIPQ
LPVSLGGGAI PPLGAMASGV DKARTGSSPP IVSLDKASSE TGASRPFARF IEDNKEIGIN
