ID M3XVY3_MUSPF Unreviewed; 1337 AA.
AC M3XVY3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Spalt like transcription factor 1 {ECO:0000313|Ensembl:ENSMPUP00000003233.1};
GN Name=SALL1 {ECO:0000313|Ensembl:ENSMPUP00000003233.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003233.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003233.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000256|ARBA:ARBA00038474}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEYP01015332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004744231.1; XM_004744174.2.
DR STRING; 9669.ENSMPUP00000003233; -.
DR Ensembl; ENSMPUT00000003298.1; ENSMPUP00000003233.1; ENSMPUG00000003265.1.
DR KEGG; mpuf:101691183; -.
DR eggNOG; KOG1074; Eukaryota.
DR GeneTree; ENSGT00940000155938; -.
DR HOGENOM; CLU_005740_0_0_1; -.
DR InParanoid; M3XVY3; -.
DR OMA; QELHKSP; -.
DR OrthoDB; 2880677at2759; -.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0008406; P:gonad development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEA:Ensembl.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR CDD; cd20908; SUF4-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR PANTHER; PTHR23233:SF51; SAL-LIKE PROTEIN 1; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1337
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004044178"
FT DOMAIN 460..487
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 488..515
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 719..746
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 747..774
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 779..806
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1014..1041
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1042..1069
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1147..1174
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1175..1202
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 105..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 141221 MW; 023E023E7315348D CRC64;
MIIAFLFGVC VCVCVCVCDA FFSVFSRVLS GPKDLLLMWQ KCDCHRSALA QILGDAEKVQ
PSRTTKSKDA HVCGRCCAEF FELSDLLLHK KNCTKNQLVL IVNESPASPP ETFSPTPPPE
HPDEQMNDPV LKTDQAKGGD LPEHRGRHRE ESMEVEAPGA NKGGGGAPGD GGSGVPSTGT
SAITTSLPQL GDLTTLGNFS VINSNVIIEN LQSTKVAVAQ FSQEARCGGA SGGKLAVPAL
MEQLLALQQQ QIHQLQLIEQ IRHQILLLAS QNADLPTSSS PSPGTLRTSA NPLSTLSSHL
SQQLAAAAGL AQSLASQSAC ISSVKQLPPT QLPQSGSGHT IVPPNSGSSP NINVLAAAGS
TPSSEKAASS AGAVHASLPA ASVSSSPAFA ISSLLNPASN PLLPQPAPAN PVFPSPLPNI
GTTAEDLNSL SALAQQRKSK PPNVPAFEAK STSDEAFFKH KCRFCAKVFG SDSALQIHLR
SHTGERPFKC NICGNRFSTK GNLKVHFQRH KEKYPHIQMN PYPVPEHLDN IPTSTGIPYG
MSIPPEKPVT SWLDTKPVLP TLTTSVGLPL PPTLPSLAPF IKTEEPAPIP ISHSATSPPP
GSVKSDSGAP EPATRNPGGL ADEAEESAGP PSGGRSEESG TAPGSAPAAG GGSGSLSWGG
ADGGPSSAAA FPNPLLPLMS EQFKAKFPFG GLLDSAQASE TSKLQQLVEN IDKKAADPNE
CIICHRVLSC QSALKMHYRT HTGERPFKCK ICGRAFTTKG NLKTHYSVHR AVPPLRVQHS
CPICQKKFTN AVVLQQHIRM HMGGQIPNTP VPDSYPESME SDTGSFDEKN FDDLDTFSDE
NMEDCPEGSI PDTPKSADAS QDSLSSSPLP LEMSSIAALE NQMKMINAGL AEQLQASLKS
VENGSVEGDV LTNDSSSVGG DMESQSAGSP AISESTSSMQ ALSPSNSTQE LHKSPSVEEK
PQRAVPSEFA NGLSPTPVNG GALDLTSSHA EKIIKEDSLG ILFPFRDRGK FKNTACDICG
KTFACQSALD IHYRSHTKER PFICTVCNRG FSTKGNLKQH MLTHQMRDLP SQLFEPSSNL
GPNQNSAVIP ANSLSSLIKT EVNGFVHVTP QDSKDTSTGH VPSGPLSSSA TSPVLLPALP
RRTPKQHYCN TCGKTFSSSS ALQIHERTHT GEKPFACTIC GRAFTTKGNL KVHMGTHMWN
SAPARRGRRL SVDGPMTFLG GNPVKFPEMF QKDLAARSGS GDPSSFWNQY AAALSNGLAM
KANEISVIQN GGIPPIPGSL GSGSSSPISG LTGNLEKLQN SEPSAPLAGL EKMASSENGT
NFRFTRFVED SKEIVTS
//