ELP5_DANRE
ID ELP5_DANRE Reviewed; 296 AA.
AC A1A5V9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Elongator complex protein 5;
DE AltName: Full=Dermal papilla-derived protein 6 homolog;
DE AltName: Full=Retinoic acid-induced protein 12;
GN Name=elp5; Synonyms=derp6, Rai12; ORFNames=zgc:158278, zgc:158285;
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].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC catalyzes the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (By similarity). {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SUBUNIT: Component of the elongator complex.
CC {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TE02}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SIMILARITY: Belongs to the ELP5 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}.
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DR EMBL; BC128832; AAI28833.1; -; mRNA.
DR EMBL; BC128833; AAI28834.1; -; mRNA.
DR RefSeq; NP_001073536.1; NM_001080067.2.
DR AlphaFoldDB; A1A5V9; -.
DR SMR; A1A5V9; -.
DR STRING; 7955.ENSDARP00000088643; -.
DR PaxDb; A1A5V9; -.
DR PeptideAtlas; A1A5V9; -.
DR PRIDE; A1A5V9; -.
DR GeneID; 790921; -.
DR KEGG; dre:790921; -.
DR CTD; 23587; -.
DR ZFIN; ZDB-GENE-061215-33; elp5.
DR eggNOG; ENOG502QQ2R; Eukaryota.
DR InParanoid; A1A5V9; -.
DR OrthoDB; 805928at2759; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:A1A5V9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR019519; Elp5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15641; PTHR15641; 1.
DR Pfam; PF10483; Elong_Iki1; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..296
FT /note="Elongator complex protein 5"
FT /id="PRO_0000280820"
FT REGION 203..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32739 MW; 092D3BFDB2ACFCA0 CRC64;
MLLEVLQAAE AGGFILIQDS VQCCGRGILR CCINAALKRD EDVHVLGFES PETEVCAGLD
SSFAQKLHFH KGFPDPLGWR GKSSFTVQQF TSQHITQLIR DSQPAKASVL VVDSLSLVLR
HHDPVIVCQS LQELRKGGVV KTIIGLLHSD LHLQGIVGIV CHLASTVISV APTNNERHAV
ATTTRRTKSG KVMQEEEYFS VSEDATLSVQ SKPRQHDRVE KEQDSAEVDP ASNLTFNLRL
SEEERRAKEK VALPFVFSQE KKSALLRPTP GSGRIMYEPD ANDDFDEEDP DDDLDV