ID   DENR_PONAB              Reviewed;         198 AA.
AC   Q5RFP5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Density-regulated protein;
DE            Short=DRP;
GN   Name=DENR;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Interacts with MCTS1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR857108; CAH89412.1; -; mRNA.
DR   RefSeq; NP_001124595.1; NM_001131123.1.
DR   AlphaFoldDB; Q5RFP5; -.
DR   SMR; Q5RFP5; -.
DR   STRING; 9601.ENSPPYP00000005779; -.
DR   GeneID; 100171431; -.
DR   KEGG; pon:100171431; -.
DR   CTD; 8562; -.
DR   eggNOG; KOG3239; Eukaryota.
DR   InParanoid; Q5RFP5; -.
DR   OrthoDB; 1490022at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005873; DENR_eukaryotes.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   CHAIN           2..198
FT                   /note="Density-regulated protein"
FT                   /id="PRO_0000130602"
FT   DOMAIN          115..182
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          72..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQJ6"
SQ   SEQUENCE   198 AA;  22062 MW;  004A7297A26FB258 CRC64;
     MAADISESSG ADCNGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
     FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
     PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
     KWPEVVDDSI EDLGEVKK