ID A0A287BPF3_PIG Unreviewed; 312 AA.
AC A0A287BPF3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DDRGK domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018218};
GN Name=DDRGK1 {ECO:0000313|Ensembl:ENSSSCP00000057985.1,
GN ECO:0000313|VGNC:VGNC:103933};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000057985.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000057985.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000057985.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDC36617.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000057985.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DDRGK1 family.
CC {ECO:0000256|ARBA:ARBA00009829}.
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DR EMBL; DQIR01281139; HDC36617.1; -; Transcribed_RNA.
DR RefSeq; NP_001177141.1; NM_001190212.1.
DR STRING; 9823.ENSSSCP00000057985; -.
DR PaxDb; 9823-ENSSSCP00000007622; -.
DR Ensembl; ENSSSCT00000060030.3; ENSSSCP00000057985.1; ENSSSCG00000007160.5.
DR GeneID; 100155894; -.
DR KEGG; ssc:100155894; -.
DR CTD; 65992; -.
DR VGNC; VGNC:103933; DDRGK1.
DR eggNOG; KOG3054; Eukaryota.
DR GeneTree; ENSGT00390000017193; -.
DR OrthoDB; 197573at2759; -.
DR Reactome; R-SSC-8980692; RHOA GTPase cycle.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007160; Expressed in longissimus lumborum muscle and 47 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0071569; P:protein ufmylation; IEA:Ensembl.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0061709; P:reticulophagy; IEA:Ensembl.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR019153; DDRGK_dom-contain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR48176; DDRGK DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR48176:SF1; DDRGK DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF09756; DDRGK; 1.
DR SMART; SM01128; DDRGK; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287BPF3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 35765 MW; 99E4C6B7953D78E5 CRC64;
MVAPVVYLVV AALLVGFILF LTRRRGRAAA AGREPLNNEE ELGVAGRVAQ PELDEQRAGG
RPRRRRDLGS RLQAQRRAQR VAWAEVDEDE EEVIIPALEE EIIEKPVETH LSGKIGAKKL
RKLEEKQARK AQREAEEAER EERKRLESQR EAEWKKEEER LRLEEEQKEE EERRAREEQA
QREHEEYLKL KESFVVEEEG VGETMTEEES HSFLTEFINY IKQSKVVLLE DLASQVGLRT
QDTINRIQDL LAEGTLTGVI DDRGKFIYIT PEELAAVANF IRQRGRVSIT ELAQASNSLI
AWGREPPAQA PA
//
