SALL2_MOUSE
ID SALL2_MOUSE Reviewed; 1004 AA.
AC Q9QX96; Q5U3X1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Sal-like protein 2;
DE AltName: Full=Spalt-like protein 2;
DE AltName: Full=Zinc finger protein Spalt-2;
DE Short=Sal-2;
DE Short=mSal-2;
GN Name=Sall2; Synonyms=Sal2;
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 TISSUE=Brain;
RX PubMed=10602995; DOI=10.1007/s003350010012;
RA Kohlhase J., Altmann M., Archangelo L., Dixkens C., Engel W.;
RT "Genomic cloning, chromosomal mapping, and expression analysis of Msal-2.";
RL Mamm. Genome 11:64-68(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24412933; DOI=10.1093/hmg/ddt643;
RA Kelberman D., Islam L., Lakowski J., Bacchelli C., Chanudet E., Lescai F.,
RA Patel A., Stupka E., Buck A., Wolf S., Beales P.L., Jacques T.S.,
RA Bitner-Glindzicz M., Liasis A., Lehmann O.J., Kohlhase J., Nischal K.K.,
RA Sowden J.C.;
RT "Mutation of SALL2 causes recessive ocular coloboma in humans and mice.";
RL Hum. Mol. Genet. 23:2511-2526(2014).
CC -!- FUNCTION: Probable transcription factor that plays a role in eye
CC development before, during, and after optic fissure closure.
CC {ECO:0000269|PubMed:24412933}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed throughout embryonic development. In
CC adult predominantly in brain.
CC -!- DISRUPTION PHENOTYPE: No overt phenotypic abnormalities. Histologic
CC analysis of the eyes reveales a colobomatous phenotype, with delayed
CC apposition of the optic fissure margins and persistence of an anterior
CC retinal coloboma phenotype after birth. Deficient embryos display
CC correct posterior closure toward the optic nerve head, and upon contact
CC of the fissure margins, dissolution of the basal lamina occurs and
CC PAX2, known to be critical for this process, is expressed normally.
CC Anterior closure is disrupted with the fissure margins failing to meet,
CC or in some cases misaligning leading to a retinal lesion.
CC {ECO:0000269|PubMed:24412933}.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AJ007396; CAB65274.1; -; mRNA.
DR EMBL; BC085361; AAH85361.1; -; mRNA.
DR CCDS; CCDS27054.1; -.
DR RefSeq; NP_001231845.1; NM_001244916.1.
DR RefSeq; NP_056587.2; NM_015772.3.
DR AlphaFoldDB; Q9QX96; -.
DR BioGRID; 206051; 2.
DR IntAct; Q9QX96; 3.
DR MINT; Q9QX96; -.
DR STRING; 10090.ENSMUSP00000056401; -.
DR iPTMnet; Q9QX96; -.
DR PhosphoSitePlus; Q9QX96; -.
DR jPOST; Q9QX96; -.
DR MaxQB; Q9QX96; -.
DR PaxDb; Q9QX96; -.
DR PRIDE; Q9QX96; -.
DR ProteomicsDB; 256829; -.
DR Antibodypedia; 22191; 100 antibodies from 20 providers.
DR DNASU; 50524; -.
DR Ensembl; ENSMUST00000058326; ENSMUSP00000056401; ENSMUSG00000049532.
DR GeneID; 50524; -.
DR KEGG; mmu:50524; -.
DR UCSC; uc007tpf.2; mouse.
DR CTD; 6297; -.
DR MGI; MGI:1354373; Sall2.
DR VEuPathDB; HostDB:ENSMUSG00000049532; -.
DR eggNOG; KOG1074; Eukaryota.
DR GeneTree; ENSGT00940000162245; -.
DR HOGENOM; CLU_013111_0_0_1; -.
DR InParanoid; Q9QX96; -.
DR OMA; ENGSEQC; -.
DR OrthoDB; 244207at2759; -.
DR TreeFam; TF317003; -.
DR BioGRID-ORCS; 50524; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Sall2; mouse.
DR PRO; PR:Q9QX96; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QX96; protein.
DR Bgee; ENSMUSG00000049532; Expressed in vestibular epithelium and 211 other tissues.
DR ExpressionAtlas; Q9QX96; baseline and differential.
DR Genevisible; Q9QX96; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO: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: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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
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:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1004
FT /note="Sal-like protein 2"
FT /id="PRO_0000047023"
FT ZN_FING 34..56
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000303|PubMed:16545361"
FT ZN_FING 372..394
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 629..651
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 657..679
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 689..711
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 908..930
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 937..961
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..777
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y467"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y467"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y467"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT CROSSLNK 908
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y467"
FT CONFLICT 8
FT /note="R -> K (in Ref. 1; CAB65274)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="D -> H (in Ref. 1; CAB65274)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> P (in Ref. 1; CAB65274)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="E -> K (in Ref. 1; CAB65274)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="T -> I (in Ref. 1; CAB65274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 104944 MW; AEEBBDEE04DDE5FF CRC64;
MSRRKQRRPQ QLISDCEGPS ASENGDASEE DHPQVCAKCC AQFSDPTEFL AHQNSCCTDP
PVMVIIGGQE NPSNSSASSA PRPEGHSRSQ VMDTEHSNPP DSGSSGAPDP TWGPERRGEE
SSGQFLVAAT GTAAGGGGGL ILASPKLGAT PLPPESTPAP PPPPPPPPPP GVGSGHLNIP
LILEELRVLQ QRQIHQMQMT EQICRQVLLL GSLGQTVGAP ASPSELPGTG AASSTKPLLP
LFSPIKPAQT GKTLASSSSS SSSSGAEPPK QAFFHLYHPL GSQHPFSVGG VGRSHKPTPA
PSPALPGSTD QLIASPHLAF PGTTGLLAAQ CLGAARGLEA AASPGLLKPK NGSGELGYGE
VISSLEKPGG RHKCRFCAKV FGSDSALQIH LRSHTGERPY KCNVCGNRFT TRGNLKVHFH
RHREKYPHVQ MNPHPVPEHL DYVITSSGLP YGMSVPPEKA EEEAGTPGGG VERKPLVAST
TALSATESLT LLSTGTSTAV APGLPTFNKF VLMKAVEPKS KADENTPPGS EGSAIAGVAD
SGSATRMQLS KLVTSLPSWA LLTNHLKSTG SFPFPYVLEP LGASPSETSK LQQLVEKIDR
QGAVAVASTA SGAPTTSAPA PSSSASGPNQ CVICLRVLSC PRALRLHYGQ HGGERPFKCK
VCGRAFSTRG NLRAHFVGHK TSPAARAQNS CPICQKKFTN AVTLQQHVRM HLGGQIPNGG
SALSEGGGAA QENSSEQSTA SGPGSFPQPQ SQQPSPEEEM SEEEEEDEEE EEDVTDEDSL
AGRGSESGGE KAISVRGDSE EVSGAEEEVA TSVAAPTTVK EMDSNEKAPQ HTLPPPPPPP
DNLDHPQPME QGTSDVSGAM EEEAKLEGTS SPMAALTQEG EGTSTPLVEE LNLPEAMKKD
PGESSGRKAC EVCGQSFPTQ TALEEHQKTH PKDGPLFTCV FCRQGFLDRA TLKKHMLLAH
HQVPPFAPHG PQNIATLSLV PGCSSSIPSP GLSPFPRKDD PTMP
