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Database: UniProt
Entry: A0A1U7QDR2_MESAU
LinkDB: A0A1U7QDR2_MESAU
Original site: A0A1U7QDR2_MESAU 
ID   A0A1U7QDR2_MESAU        Unreviewed;      1320 AA.
AC   A0A1U7QDR2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Sal-like protein 3 isoform X1 {ECO:0000313|RefSeq:XP_005065467.1};
GN   Name=Sall3 {ECO:0000313|RefSeq:XP_005065467.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005065467.1};
RN   [1] {ECO:0000313|RefSeq:XP_005065467.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_005065467.1; XM_005065410.3.
DR   STRING; 10036.ENSMAUP00000011148; -.
DR   GeneID; 101823776; -.
DR   KEGG; maua:101823776; -.
DR   CTD; 27164; -.
DR   eggNOG; KOG1074; Eukaryota.
DR   OrthoDB; 2880677at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF84; FI23031P1-RELATED; 1.
DR   PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
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; 8.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   DOMAIN          427..454
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          455..482
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          692..719
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          720..747
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          752..779
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          997..1024
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1133..1160
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1161..1188
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..50
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..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..599
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          877..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1305
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        533..587
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        877..937
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1320 AA;  138628 MW;  42FFB145D8DCD580 CRC64;
     MSRRKQAKPQ HLKSDEELPP QDGASEHGVP GDGAEDAESG SESRSGSEET SVCEKCCAEF
     FKWTDFLQHK KTCTKNPLVL IVHDDEPAPP SEDFPEPSPA SSPSDRTESE VAEEVAPTEG
     SEVKAAAKEA EPMDVEASAD KGPPGPGVPP PPPALPPQPE PAAFSMPSTN VTLETLLSTK
     VAVAQFSQGA RAGGATGAGS TVGAVAIPMI LEQLVALQQQ QIHQLQLIEQ IRSQVALMSR
     QPGPPLKPSA GAPATASVQL QGLAPHTALQ LSTGPATASA GSGSALPAAF DGPQHLSQPA
     SGTSTPCSTS AGPAESGAHP ACSTGPAPGA VAAAASAVGN TVQPQNASTP PALGPGPLLS
     SASNLPNPLL PQTSSSSVIF PNPLVSIAAT ANALDPLSAL MKHRKGKPPN VSVFEPKASA
     EDPFFKHKCR FCAKVFGSDS ALQIHLRSHT GERPFKCNIC GNRFSTKGNL KVHFQRHKEK
     YPHIQMNPYP VPEYLDNVPT CSGIPYGMSL PPEKPVTTWL DSKPVLPTVP TSVGLQLPPT
     VPGTHNYTDS PSVTPISRSP QRPSPASSEC TSLSPGLNNT ESGITVRPES PQPLLGGPSL
     AKTEPVSLPC ASTRTGDAPV VGGQVSGLPT PTATSVTDSA CTSLGSPGLP AVSDQFKAQF
     PFGGLLDSMQ TSETSKLQQL VENIDKKITD PNQCVICHRV LSCQSALKMH YRTHTGERPF
     KCKICGRAFT TKGNLKTHFG VHRAKPPLRV QHSCPICQKK FTNAVVLQQH IRMHMGGQIP
     NTPLPEGLQE AMDAELPFDE KNAETLSSFD DDIDENSMEE DSELKDTASD SSKPLLSYSG
     SCPPSPPSVI SSIAALENQM KMIDSVMNCQ QLTSLKSVEN GSGESDRLSN DSSSAVGDLE
     SRSAGSPALS ESSSSQALSP THSNGESFRS KSPGLSHQED PQEIPLKTER LDSPPPGPGN
     GGALDLTAGH PGRPLIKEEA PFSLLFLSRE RGKCASTVCG VCGKPFACKS ALEIHHRSHT
     KERPFVCTVC RRGCSTMGNL KQHLLTHKLK ELPSQVFDSD FTLGPSHSTP SLASSPAPTM
     IKMEVNGHSK AIALGEGPAL PAGVQVPTGP QTVMSPGLAP MLAPPPRRTP KQHNCQSCGK
     TFSSASALQI HERTHTGEKP FGCTICGRAF TTKGNLKVHM GTHMWNNAPA RRGRRLSVEN
     PMALLGGDAL KFSEMFQKDL AARAMNVDPS FWNQYAAAIT NGLAMKNNEI SVIQNGGIPQ
     LPVSLGGGAI PPLGAIAGGV EKTRTGSSPP IVSLDKASSE TGAGRPFTRF IEDNKEIGIN
//
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