LIN54_DANRE
ID LIN54_DANRE Reviewed; 771 AA.
AC Q08CM4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein lin-54 homolog;
GN Name=lin54; ORFNames=zgc:152921;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-292 AND SER-308, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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; BC124175; AAI24176.1; -; mRNA.
DR RefSeq; NP_001070035.1; NM_001076567.1.
DR AlphaFoldDB; Q08CM4; -.
DR SMR; Q08CM4; -.
DR STRING; 7955.ENSDARP00000086543; -.
DR iPTMnet; Q08CM4; -.
DR PaxDb; Q08CM4; -.
DR GeneID; 560688; -.
DR KEGG; dre:560688; -.
DR CTD; 132660; -.
DR ZFIN; ZDB-GENE-060929-440; lin54.
DR eggNOG; KOG1171; Eukaryota.
DR InParanoid; Q08CM4; -.
DR OrthoDB; 389707at2759; -.
DR PhylomeDB; Q08CM4; -.
DR Reactome; R-DRE-1538133; G0 and Early G1.
DR PRO; PR:Q08CM4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 1: Evidence at protein level;
KW Activator; Cell cycle; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..771
FT /note="Protein lin-54 homolog"
FT /id="PRO_0000341393"
FT DOMAIN 544..657
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..559
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 606..619
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT REGION 622..635
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT COMPBIAS 68..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 622
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 622
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 559
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 597
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT SITE 633
FT /note="Critical for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q6MZP7"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 771 AA; 81389 MW; 000D69390EBBA9CF CRC64;
MDVVSPELNS LLPDEIMDTE AMDEDPPASH LTPPPQSAPE SAQVPMETEV PEIISICPTT
ASMQAISTNA KSTTSSTTQL LLTPSSSSST TTKNATPTLP KIPSLSVPPN HQLIINKVAA
DGKSPGGAVI KQEGQKLLVA GLSKTGQPIM LALPHAWNKP ATSQGSGDAK SQPTQIKMVT
AMGKPVIAVS SASQLVASST PLQAQHLKTL QITKKPPVST AGPMITKLII TKALNNKVLS
SPGSVSPVVT GRVVSQSTPL TPPRTIAIGE TISTVPQNAA TNSKVAISPL KSPSKLTVVS
VTSQSSNSPQ KSMTLPLNVA LGQQILTVQQ SAVTSPAKAG SSQSTTQTVK PVQTVTVPTS
QFKTIIPLTT PPNVQQIQVP GSRFHYVRLV TATTGSSTVQ TGGSTNTNPS IQPAKPVMMN
AAVRMSVPIV PAQTAKQVVP KPLSSAAQVV TTSQTPQRLI MPATHLPQIQ PNLTNLPPGT
VLAPAHGSGN VGYAVLPAPY VTQIPQPAFV TLTSSSTFST ATPSQAQARL SLNGLSTSEA
NSRPRKPCNC TRSQCLKLYC DCFANGEFCN NCNCVNCFNN LDHESERLKA IKACLDRNPV
AFKPKIGKGK EGESDRRHSK GCNCKKSGCL KNYCECYEAK IMCSSICKCM GCKNFEESPE
RKTLMHLADA AEVRVQQQTA AKTKLSSQIS DLLTRTTPAI TSGGGKLPYT FVTKEVAEAT
CDCLLEQAEQ AELTNQPQAM AERLILEEFG RCLHRIISFA GKAKTDCPIN C
