SALL1_MOUSE
ID SALL1_MOUSE Reviewed; 1322 AA.
AC Q9ER74; Q920R5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sal-like protein 1;
DE AltName: Full=Zinc finger protein Spalt-3;
DE Short=Sal-3;
DE Short=mSal-3;
GN Name=Sall1; Synonyms=Sal3;
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 [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=10965108; DOI=10.1159/000015598;
RA Buck A., Archangelo L., Dixkens C., Kohlhase J.;
RT "Molecular cloning, chromosomal localization, and expression of the murine
RT SALL1 ortholog Sall-1.";
RL Cytogenet. Cell Genet. 89:150-153(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11688560; DOI=10.1242/dev.128.16.3105;
RA Nishinakamura R., Matsumoto Y., Nakao K., Nakamura K., Sato A.,
RA Copeland N.G., Gilbert D.J., Jenkins N.A., Scully S., Lacey D.L.,
RA Katsuki M., Asashima M., Yokota T.;
RT "Murine homolog of SALL1 is essential for ureteric bud invasion in kidney
RT development.";
RL Development 128:3105-3115(2001).
RN [3]
RP FUNCTION, INTERACTION WITH HDAC1; HDAC2; RBBP4; RBPP7; MTA1 AND MTA2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11836251; DOI=10.1074/jbc.m200052200;
RA Kiefer S.M., McDill B.W., Yang J., Rauchman M.;
RT "Murine sall1 represses transcription by recruiting a histone deacetylase
RT complex.";
RL J. Biol. Chem. 277:14869-14876(2002).
RN [4]
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 [5]
RP INTERACTION WITH NSD2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19483677; DOI=10.1038/nature08086;
RA Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J.,
RA Kaneda Y.;
RT "A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-
RT Hirschhorn syndrome.";
RL Nature 460:287-291(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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: Transcriptional repressor involved in organogenesis
CC (PubMed:11688560, PubMed:11836251). Plays an essential role in ureteric
CC bud invasion during kidney development (PubMed:11688560).
CC {ECO:0000269|PubMed:11688560, ECO:0000269|PubMed:11836251}.
CC -!- SUBUNIT: May associate with NuRD histone deacetylase complex (HDAC)
CC (PubMed:11836251). Interacts with components of HDAC complex including
CC HDAC1, HDAC2, RBBP4, RBPP7, MTA1 and MTA2 (PubMed:11836251). Interacts
CC with CCNQ (By similarity). Interacts with NSD2 (via PHD-type zinc
CC fingers 1, 2 and 3) (PubMed:19483677). {ECO:0000250|UniProtKB:Q9NSC2,
CC ECO:0000269|PubMed:11836251, ECO:0000269|PubMed:19483677}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11836251,
CC ECO:0000269|PubMed:19483677}.
CC -!- TISSUE SPECIFICITY: Expressed in the metanephric mesenchyme surrounding
CC ureteric bud. {ECO:0000269|PubMed:11688560}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic heart (at protein level)
CC (PubMed:19483677). At 11.5 dpc expressed in limb buds, ventromedial
CC parts of otic vesicles, endocardium, and weakly in the spinal cord and
CC the brain (PubMed:11688560). At 14.5 dpc expressed in limb buds,
CC anorectal region, developing olfactory bulb, nose and eye. At 10.5 dpc,
CC expressed in the nephrogenic primordium (PubMed:11688560). At 11.5 dpc,
CC expressed in mesonephric tubules and Wolffian ducts, and in the
CC metanephric mesenchyme surrounding the ureteric bud (PubMed:11688560).
CC At 14.5 dpc, expressed in the mesenchyme around the ureteric buds and
CC weakly in comma-shaped bodies of metanephric tubules, but not in
CC glomeruli, in the cortical regions of the developing kidney
CC (PubMed:11688560). {ECO:0000269|PubMed:11688560,
CC ECO:0000269|PubMed:19483677}.
CC -!- DISRUPTION PHENOTYPE: Death at P1 stage (PubMed:11688560). Newborns
CC have either no kidneys or ureters, only one kidney or ureter, or two
CC small kidneys (PubMed:11688560). The remnant kidneys have disorganized
CC cortical structure, shrunken glomeruli, necrotic proximal tubules and
CC multiple cysts (PubMed:11688560). At day 11.5, embryos have an
CC incomplete ureteric bud outgrowth, fail to form tubules in the
CC mesenchyme and show apoptosis of the mesenchyme (PubMed:11688560).
CC {ECO:0000269|PubMed:11688560}.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AJ271914; CAC09602.1; -; Genomic_DNA.
DR EMBL; AJ271915; CAC09602.1; JOINED; Genomic_DNA.
DR EMBL; AB051409; BAB55673.1; -; mRNA.
DR AlphaFoldDB; Q9ER74; -.
DR DIP; DIP-54906N; -.
DR IntAct; Q9ER74; 11.
DR STRING; 10090.ENSMUSP00000034090; -.
DR iPTMnet; Q9ER74; -.
DR PhosphoSitePlus; Q9ER74; -.
DR MaxQB; Q9ER74; -.
DR PaxDb; Q9ER74; -.
DR PRIDE; Q9ER74; -.
DR ProteomicsDB; 255453; -.
DR MGI; MGI:1889585; Sall1.
DR eggNOG; KOG1074; Eukaryota.
DR InParanoid; Q9ER74; -.
DR PhylomeDB; Q9ER74; -.
DR ChiTaRS; Sall1; mouse.
DR PRO; PR:Q9ER74; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ER74; protein.
DR GO; GO:0010369; C:chromocenter; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0048566; P:embryonic digestive tract development; ISO:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
DR GO; GO:0035136; P:forelimb morphogenesis; IGI:MGI.
DR GO; GO:0097154; P:GABAergic neuron differentiation; IMP:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0035137; P:hindlimb morphogenesis; IGI:MGI.
DR GO; GO:0031129; P:inductive cell-cell signaling; IMP:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0072073; P:kidney epithelium development; IMP:UniProtKB.
DR GO; GO:0060173; P:limb development; ISO:MGI.
DR GO; GO:0072309; P:mesenchymal stem cell maintenance involved in metanephric nephron morphogenesis; IMP:MGI.
DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IMP:UniProtKB.
DR GO; GO:2000384; P:negative regulation of ectoderm development; IMP:BHF-UCL.
DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IMP:MGI.
DR GO; GO:2000381; P:negative regulation of mesoderm development; IMP:BHF-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0021915; P:neural tube development; IGI:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0021889; P:olfactory bulb interneuron differentiation; IMP:UniProtKB.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; ISO:MGI.
DR GO; GO:0021553; P:olfactory nerve development; IMP:UniProtKB.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; 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 GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR GO; GO:0072092; P:ureteric bud invasion; IMP:UniProtKB.
DR GO; GO:0003281; P:ventricular septum development; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
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; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1322
FT /note="Sal-like protein 1"
FT /id="PRO_0000047021"
FT ZN_FING 43..65
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000303|PubMed:16545361"
FT ZN_FING 450..472
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 478..500
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 705..727
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 733..755
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..787
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1000..1022
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1028..1050
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..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 672
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 946
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 981
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 1085
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 1218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 1297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CROSSLNK 1317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NSC2"
FT CONFLICT 165
FT /note="C -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="S -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="S -> SS (in Ref. 2; BAB55673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1322 AA; 140230 MW; DF4FEF7FEA0B9F5C CRC64;
MSRRKQAKPQ HFQSDPEVAS LPRRDGDTEK GQPSRPTKSK DAHVCGRCCA EFFELSDLLL
HKKSCTKNQL VLIVNESPAS PAKTFPPGPS LNDPDDQMKD AANKADQEDC SDLSEPKGLD
REESMEVEVP VATTTTTTTG GSGGSGGSTL SGVTNITTPS CHSGCSSGTS AITTSLPQLG
DLTTLGNFSV INSNVIIENL QSTKVAVAQF SQEARCGGAS GGKLLISTLM EQLLALQQQQ
IHQLQLIEQI RHQILLLASQ SADLPAAPSI PSQGTLRTSA NPLTTLSSHL SQQLAVAAGL
AQSLASQSAN ISGVKQLPHV QLPQSSSGTS IVPPSGGTSP NMSIVTAAVP TPSSEKVASN
AGASHVSSPA VSASSSPAFA ISSLLSPESN PLLPQPTPAN AVFPTPLPNI ATTAEDLNSL
SALAQQRKSK PPNVTAFEAK STSDEAFFKH KCRFCAKVFG SDSALQIHLR SHTGERPFKC
NICGNRFSTK GNLKVHFQRH KEKYPHIQMN PYPVPEHLDN VPTSTGIPYG MSIPSEKPVT
SWLDTKPVLP TLTTSVGLPL PPTLPSLTPF IKTEEPAPIP ISHSAASPQG SVKSDSGAPD
LATRNPSGVP EEVEGSAVPP FGGKGEESNM ASSAVPTAGN STLNSPVADG GPGGTTFTNP
LLPLMSEQFK AKFPFGGLLD SAQASETSKL QQLVENIDKK ATDPNECIIC HRVLSCQSAL
KMHYRTHTGE RPFKCKICGR AFTTKGNLKT HYSVHRAMPP LRVQHSCPIC QKKFTNAVVL
QQHIRMHMGG QIPNTPVPDN YPESMESDTG SFDEKNFDDL DNFSDENMEE CPEGSIPDTP
KSADASQDSL SSSPLPLEMS SIAALENQMK MINAGLAEQL QASLKSVENG SMEGDVLTND
SSSVGGDMES QSAGSPAISE STSSMQALSP SNSTQEFHKS PGMEEKPQRV GPGEFANGLS
PTPVNGGALD LTSSHAEKII KEDSLGILFP FRDRGKFKNT ACDICGKTFA CQSALDIHYR
SHTKERPFIC TVCNRGFSTK GNLKQHMLTH QMRDLPSQLF EPSSNLGPNQ NSAVIPANSL
SSLIKTEVNG FVHVSPQDSK DAPTSHVPQG PLSSSATSPV LLPALPRRTP KQHYCNTCGK
TFSSSSALQI HERTHTGEKP FACTICGRAF TTKGNLKVHM GTHMWNSTPA RRGRRLSVDG
PMTFLGGNPV KFPEMFQKDL AARSGSGDPS SFWNQYTAAL SNGLAMKANE ISVIQNGGIP
PIPGSLGSGS SPISGLTGNV EKLGNSEPSA PLAGLEKMAS SENGTNFRFT RFVEDSKEIV
TS
