LIN54_XENTR
ID LIN54_XENTR Reviewed; 741 AA.
AC Q0IHV2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protein lin-54 homolog;
GN Name=lin54;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the DREAM complex, a multiprotein complex that
CC can both act as a transcription activator or repressor depending on the
CC context. Specifically recognizes the consensus motif 5'-TTYRAA-3' in
CC target DNA. {ECO:0000250|UniProtKB:Q6MZP7}.
CC -!- SUBUNIT: Component of the DREAM complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The CRC domain mediates DNA-binding. It contains two CXC
CC subdomains (joined by a flexible linker) which are both required for
CC efficient association with target DNA. Each CXC subdomain coordinates
CC three Zn(2+) ions. {ECO:0000250|UniProtKB:Q6MZP7}.
CC -!- SIMILARITY: Belongs to the lin-54 family. {ECO:0000305}.
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DR EMBL; BC122957; AAI22958.1; -; mRNA.
DR RefSeq; NP_001072590.1; NM_001079122.1.
DR RefSeq; XP_012821023.1; XM_012965569.2.
DR RefSeq; XP_012821025.1; XM_012965571.2.
DR RefSeq; XP_017950024.1; XM_018094535.1.
DR AlphaFoldDB; Q0IHV2; -.
DR SMR; Q0IHV2; -.
DR STRING; 8364.ENSXETP00000000785; -.
DR PaxDb; Q0IHV2; -.
DR DNASU; 780045; -.
DR Ensembl; ENSXETT00000000785; ENSXETP00000000785; ENSXETG00000000369.
DR GeneID; 780045; -.
DR KEGG; xtr:780045; -.
DR CTD; 132660; -.
DR Xenbase; XB-GENE-5752559; lin54.
DR eggNOG; KOG1171; Eukaryota.
DR HOGENOM; CLU_024128_0_0_1; -.
DR InParanoid; Q0IHV2; -.
DR OMA; MFFIVIC; -.
DR OrthoDB; 389707at2759; -.
DR TreeFam; TF313189; -.
DR Reactome; R-XTR-1538133; G0 and Early G1.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000369; Expressed in ovary and 13 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR005172; CRC.
DR InterPro; IPR028307; Lin-54_fam.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR12446; PTHR12446; 1.
DR Pfam; PF03638; TCR; 2.
DR SMART; SM01114; CXC; 2.
DR PROSITE; PS51634; CRC; 1.
PE 2: Evidence at transcript level;
KW Activator; Cell cycle; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..741
FT /note="Protein lin-54 homolog"
FT /id="PRO_0000341394"
FT DOMAIN 513..626
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 515..528
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 575..588
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 591..604
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 528
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 566
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 602
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
SQ SEQUENCE 741 AA; 78222 MW; D81A201B234F9D25 CRC64;
MDVVSTDVNN VLPDEIMETG ISLVDDDSIE AITISSPMVD EAPMETELER IVEVSSSGEC
VSTAVVKEAV ASTSNNAGHL AVVSVASKPE SGPSAAAMKT VLQTHFHKLA TPISGQVVLN
KVSQASDLTA GSHVVKQEGQ KLIVTTLGKS SHPIVLTLPQ SHIGNAQTPV THVQRIESKV
TPQQIKLVTI GGNRSDGNPV LGMSALTSAQ IISPSTKSPV LQTQQIKTLQ IAKKAPTSSG
PVITKLIIAK PLNSKPLTEQ TTQIASSFAG GPALSQTNPG TPPKALNIAD IGVIGTPSAK
TTNKIAISPL KSPSKGVKSS VGGINTPQFK TIIPLAAAPN VQQIQVPGSK FHYVRLVTAS
TASNTTPSSQ IQSTSTQPLQ QAKPVVVNAT PVRMSVPIIP AQTVKQVVPK PLNAASQIVT
TSQPQQRLLM PATPLAQIQP SLTNLPAGTV LASAPGTGNV GYAVLPAQYV TQLQQSSYVS
IASNAGLSGT TAAQNQPRGP LNGIISSESA SRPRKPCNCT KSLCLKLYCD CFANGEFCNN
CNCTNCYNNL EHENERQKAI KACLDRNPEA FKPKIGKGKE GESDRRHSKG CNCKRSGCLK
NYCECYEAKI MCSSICKCIG CKNFEESPER KTLMHLADAA EVRVQQQTAA KTKLSSQISD
LLTRPAPPMN SGGGKLPFTF VTKEVAEATC ECLLAQAEQA EKQLKSKAAT ERMILEEFGR
CLMRVINSAG KAKTDPCPMS C
