DDRGK_DANRE
ID DDRGK_DANRE Reviewed; 300 AA.
AC Q6P0E5;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=DDRGK domain-containing protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=ddrgk1 {ECO:0000303|PubMed:28263186};
GN ORFNames=zgc:56488 {ECO:0000303|Ref.1};
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;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28263186; DOI=10.1172/jci90193;
RA Egunsola A.T., Bae Y., Jiang M.M., Liu D.S., Chen-Evenson Y., Bertin T.,
RA Chen S., Lu J.T., Nevarez L., Magal N., Raas-Rothschild A., Swindell E.C.,
RA Cohn D.H., Gibbs R.A., Campeau P.M., Shohat M., Lee B.H.;
RT "Loss of DDRGK1 modulates SOX9 ubiquitination in spondyloepimetaphyseal
RT dysplasia.";
RL J. Clin. Invest. 127:1475-1484(2017).
CC -!- FUNCTION: Substrate adapter for ufmylation, the covalent attachment of
CC the ubiquitin-like modifier UFM1 to substrate proteins, which plays a
CC key role in reticulophagy (also called ER-phagy) (By similarity). In
CC response to endoplasmic reticulum stress, promotes recruitment of the
CC E3 ufm1-protein ligase ufl1 to the endoplasmic reticulum membrane,
CC leading to ufmylation of target proteins and subsequent reticulophagy
CC of endoplasmic reticulum sheets (By similarity). Plays a role in
CC cartilage development through sox9, inhibiting the ubiquitin-mediated
CC proteasomal degradation of this transcriptional regulator
CC (PubMed:28263186). {ECO:0000250|UniProtKB:Q96HY6,
CC ECO:0000269|PubMed:28263186}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96HY6}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96HY6}. Note=Localizes to the endoplasmic
CC reticulum membrane in response to endoplasmic reticulum stress.
CC {ECO:0000250|UniProtKB:Q96HY6}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown alters craniofacial
CC cartilage development. {ECO:0000269|PubMed:28263186}.
CC -!- SIMILARITY: Belongs to the DDRGK1 family. {ECO:0000305}.
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DR EMBL; BC065652; AAH65652.1; -; mRNA.
DR RefSeq; NP_956587.2; NM_200293.2.
DR AlphaFoldDB; Q6P0E5; -.
DR SMR; Q6P0E5; -.
DR STRING; 7955.ENSDARP00000088891; -.
DR PaxDb; Q6P0E5; -.
DR PRIDE; Q6P0E5; -.
DR GeneID; 393263; -.
DR KEGG; dre:393263; -.
DR CTD; 65992; -.
DR ZFIN; ZDB-GENE-040426-1050; ddrgk1.
DR eggNOG; KOG3054; Eukaryota.
DR InParanoid; Q6P0E5; -.
DR OrthoDB; 1553559at2759; -.
DR PhylomeDB; Q6P0E5; -.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR PRO; PR:Q6P0E5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR019153; DDRGK_dom-contain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF09756; DDRGK; 1.
DR SMART; SM01128; DDRGK; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal;
KW Ubl conjugation pathway.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..300
FT /note="DDRGK domain-containing protein 1"
FT /id="PRO_0000391852"
FT DOMAIN 217..261
FT /note="PCI"
FT REGION 28..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34431 MW; 21FCB7304298DA2C CRC64;
MDVVLYIAAA AILLVLIVFS VKIRGRTQDA DVEDHQNVTA RVSARPQAAP ERAAGMPRRR
RGLHSRVNAQ RAQRASDNED SPVEADEDEE GRNASEERPQ AAGKVGAKKQ RKLEEKQARK
AQREAEQEER EERKRLQELR DQERQKEEEK ERQQEQKQEE ELQRVKEEQE RREEEEYQRL
KESFIIEDQG EAEELTEHES QSLLQEFIQY VQKSKVVLLE DLASQFGLRT QDAIARLQDL
IADGSLTGVI DDRGKFIFIT PEELNAVAQF IKQRGRVSIS ELAQASNTLI NLTPDIHSSA