ID   DDRGK_MOUSE             Reviewed;         315 AA.
AC   Q80WW9; Q14BT4; Q9CT52;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   16-SEP-2015, entry version 97.
DE   RecName: Full=DDRGK domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=UFM1-binding and PCI domain-containing protein 1 {ECO:0000303|PubMed:21494687};
DE   Flags: Precursor;
GN   Name=Ddrgk1 {ECO:0000312|MGI:MGI:1924256};
GN   Synonyms=Ufbp1 {ECO:0000303|PubMed:21494687};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-171.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=20228063; DOI=10.1074/jbc.M110.110619;
RA   Wu J., Lei G., Mei M., Tang Y., Li H.;
RT   "A novel C53/LZAP-interacting protein regulates stability of C53/LZAP
RT   and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB
RT   signaling.";
RL   J. Biol. Chem. 285:15126-15136(2010).
RN   [7]
RP   FUNCTION, UFMYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21494687; DOI=10.1371/journal.pone.0018517;
RA   Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E.,
RA   Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.;
RT   "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect
RT   pancreatic beta cells from ER stress-induced apoptosis.";
RL   PLoS ONE 6:E18517-E18517(2011).
RN   [8]
RP   STRUCTURE BY NMR OF 216-274.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PCI domain from mouse hypothetical protein
RT   AAH51541.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Protein which interacts with the E3 UFM1-protein ligase
CC       UFL1 and one of its substrates TRIP4 and is required for TRIP4
CC       ufmylation. Through TRIP4 ufmylation may regulate nuclear
CC       receptors-mediated transcription. May play a role in NF-kappa-B-
CC       mediated transcription through regulation of the phosphorylation
CC       and the degradation of NFKBIB, the inhibitor of NF-kappa-B (By
CC       similarity). May also play a role in the cellular response to
CC       endoplasmic reticulum stress (PubMed:21494687).
CC       {ECO:0000250|UniProtKB:Q96HY6, ECO:0000269|PubMed:21494687}.
CC   -!- SUBUNIT: Interacts with TRIP4; the interaction with TRIP4 is
CC       direct. Interacts with UFL1. Interacts with NFKBIB. Interacts with
CC       CDK5RAP3. {ECO:0000250|UniProtKB:Q96HY6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:21494687}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:20228063).
CC       Higher expression in pancreatic islets, pancreatic acini and
CC       testis (at protein level) (PubMed:21494687).
CC       {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21494687}.
CC   -!- PTM: Ufmylated. Conjugated to ubiquitin-like protein UFM1,
CC       probably at Lys-268. {ECO:0000269|PubMed:21494687}.
CC   -!- PTM: Ubiquitinated. Ubiquitination probably triggers proteasomal
CC       degradation and is negatively regulated by UFL1, the enzyme
CC       involved in the ufmylation of DDRGK1.
CC       {ECO:0000250|UniProtKB:Q96HY6}.
CC   -!- SIMILARITY: Belongs to the DDRGK1 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PCI domain. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51541.1; Type=Erroneous initiation; Evidence={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; AL731707; CAM13264.1; -; Genomic_DNA.
DR   EMBL; AL772162; CAM13264.1; JOINED; Genomic_DNA.
DR   EMBL; AL772162; CAM16448.1; -; Genomic_DNA.
DR   EMBL; AL731707; CAM16448.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL28284.1; -; Genomic_DNA.
DR   EMBL; BC115616; AAI15617.1; -; mRNA.
DR   EMBL; BC115617; AAI15618.1; -; mRNA.
DR   EMBL; BC051541; AAH51541.1; ALT_INIT; mRNA.
DR   EMBL; AK011170; BAB27444.1; -; mRNA.
DR   CCDS; CCDS38243.1; -.
DR   RefSeq; NP_084108.1; NM_029832.2.
DR   UniGene; Mm.440063; -.
DR   PDB; 1WI9; NMR; -; A=216-274.
DR   PDBsum; 1WI9; -.
DR   ProteinModelPortal; Q80WW9; -.
DR   SMR; Q80WW9; 213-274.
DR   BioGrid; 218455; 1.
DR   STRING; 10090.ENSMUSP00000086988; -.
DR   PhosphoSite; Q80WW9; -.
DR   MaxQB; Q80WW9; -.
DR   PaxDb; Q80WW9; -.
DR   PRIDE; Q80WW9; -.
DR   Ensembl; ENSMUST00000089559; ENSMUSP00000086988; ENSMUSG00000068290.
DR   GeneID; 77006; -.
DR   KEGG; mmu:77006; -.
DR   UCSC; uc008mjs.1; mouse.
DR   CTD; 65992; -.
DR   MGI; MGI:1924256; Ddrgk1.
DR   eggNOG; NOG296076; -.
DR   GeneTree; ENSGT00390000017193; -.
DR   HOGENOM; HOG000005758; -.
DR   HOVERGEN; HBG051191; -.
DR   InParanoid; Q80WW9; -.
DR   OMA; EERGAGM; -.
DR   OrthoDB; EOG7SV0WW; -.
DR   PhylomeDB; Q80WW9; -.
DR   TreeFam; TF314645; -.
DR   EvolutionaryTrace; Q80WW9; -.
DR   NextBio; 346288; -.
DR   PRO; PR:Q80WW9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; Q80WW9; -.
DR   ExpressionAtlas; Q80WW9; baseline and differential.
DR   Genevisible; Q80WW9; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISS:UniProtKB.
DR   GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR   GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   InterPro; IPR019153; DDRGK_dom-contain.
DR   Pfam; PF09756; DDRGK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Endoplasmic reticulum;
KW   Isopeptide bond; Reference proteome; Signal; Ubl conjugation.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    315       DDRGK domain-containing protein 1.
FT                                /FTId=PRO_0000021034.
FT   DOMAIN      230    274       PCI.
FT   REGION        1    115       Mediates interaction with CDK5RAP3.
FT                                {ECO:0000250|UniProtKB:Q96HY6}.
FT   REGION      119    217       Mediates interaction with TRIP4.
FT                                {ECO:0000250|UniProtKB:Q96HY6}.
FT   REGION      217    315       Mediates interaction with UFL1.
FT                                {ECO:0000250|UniProtKB:Q96HY6}.
FT   CROSSLNK    268    268       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in UFM1).
FT                                {ECO:0000250|UniProtKB:Q96HY6}.
FT   HELIX       216    226       {ECO:0000244|PDB:1WI9}.
FT   STRAND      228    230       {ECO:0000244|PDB:1WI9}.
FT   HELIX       232    239       {ECO:0000244|PDB:1WI9}.
FT   HELIX       243    256       {ECO:0000244|PDB:1WI9}.
FT   STRAND      257    259       {ECO:0000244|PDB:1WI9}.
FT   STRAND      261    263       {ECO:0000244|PDB:1WI9}.
FT   STRAND      269    271       {ECO:0000244|PDB:1WI9}.
SQ   SEQUENCE   315 AA;  35977 MW;  D973B9AFBE265562 CRC64;
     MVGPWVYLVA AVLLIGLILF LTRSRGRAAA ADGEPLHNEE ERAGAGQVGR SLPQESEEQR
     TGSRPRRRRD LGSRLQAQRR AQRVAWEDGD ENVGQTVIPA QEEEGIEKPA EVHPTGKIGA
     KKLRKLEEKQ ARKAQREAEE AEREERKRLE SQREAEWKKE EERLRLKEEQ KEEEERKAQE
     EQARREHEEY LKLKEAFVVE EEGVSETMTE EQSHSFLTEF INYIKKSKVV LLEDLAFQMG
     LRTQDAINRI QDLLTEGTLT GVIDDRGKFI YITPEELAAV ANFIRQRGRV SITELAQASN
     SLISWGQDLP AQASA
//