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Database: UniProt
Entry: DENR_DANRE
LinkDB: DENR_DANRE
Original site: DENR_DANRE 
ID   DENR_DANRE              Reviewed;         208 AA.
AC   Q6DH65;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Density-regulated protein;
DE            Short=DRP;
GN   Name=denr; ORFNames=zgc:92629;
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=Embryo, and Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   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: May be involved in the translation of target mRNAs by
CC       scanning and recognition of the initiation codon. Involved in
CC       translation initiation; promotes recruitment of aminoacetyled initiator
CC       tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA
CC       and mRNA from recycled 40S subunits following ABCE1-mediated
CC       dissociation of post-termination ribosomal complexes into subunits (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
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DR   EMBL; BC076117; AAH76117.1; -; mRNA.
DR   EMBL; BC095896; AAH95896.1; -; mRNA.
DR   RefSeq; NP_001002697.1; NM_001002697.2.
DR   AlphaFoldDB; Q6DH65; -.
DR   SMR; Q6DH65; -.
DR   STRING; 7955.ENSDARP00000149057; -.
DR   iPTMnet; Q6DH65; -.
DR   PaxDb; 7955-ENSDARP00000054152; -.
DR   GeneID; 436970; -.
DR   KEGG; dre:436970; -.
DR   AGR; ZFIN:ZDB-GENE-040718-450; -.
DR   CTD; 8562; -.
DR   ZFIN; ZDB-GENE-040718-450; denr.
DR   eggNOG; KOG3239; Eukaryota.
DR   HOGENOM; CLU_073511_1_0_1; -.
DR   InParanoid; Q6DH65; -.
DR   OMA; EVFEIDM; -.
DR   PhylomeDB; Q6DH65; -.
DR   TreeFam; TF105912; -.
DR   PRO; PR:Q6DH65; -.
DR   Proteomes; UP000000437; Chromosome 10.
DR   Bgee; ENSDARG00000037229; Expressed in somite and 31 other cell types or tissues.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR   GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR   CDD; cd11607; DENR_C; 1.
DR   Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR   InterPro; IPR046447; DENR_C.
DR   InterPro; IPR005873; DENR_eukaryotes.
DR   InterPro; IPR048517; DENR_N.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   NCBIfam; TIGR01159; DRP1; 1.
DR   PANTHER; PTHR12789:SF0; DENSITY-REGULATED PROTEIN; 1.
DR   PANTHER; PTHR12789; DENSITY-REGULATED PROTEIN HOMOLOG; 1.
DR   Pfam; PF21023; DENR_N; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; eIF1-like; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..208
FT                   /note="Density-regulated protein"
FT                   /id="PRO_0000130604"
FT   DOMAIN          125..192
FT                   /note="SUI1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   208 AA;  22804 MW;  8AD1E48F5E7F9D53 CRC64;
     MATTENAESG SPENKVDRAD PDAKYPLKVL YCGVCSLPAE YCEYMPEPAK CKQWLEKNFP
     DVFAKLTLGT APKQESKGGG GGEDGGGGRG RGEAPPAGEE EEKKKQKRGG RGQIKQKKKT
     VPQKVTIAKI PRAKKKYVTR VCGLATFDIE LKEAQRFFAQ KFSCGASVTA EDEIIIQGDF
     TDDIIDVIQE KWPEVDDDSI DDLGEVKK
//
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