ERP29_RAT
ID ERP29_RAT Reviewed; 260 AA.
AC P52555; P80749; Q5BKC2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Endoplasmic reticulum resident protein 29;
DE Short=ERp29;
DE AltName: Full=Endoplasmic reticulum resident protein 31;
DE Short=ERp31;
DE Flags: Precursor;
GN Name=Erp29;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9492298; DOI=10.1046/j.1432-1327.1998.2510304.x;
RA Mkrtchian S., Fang C., Hellman U., Ingelman-Sundberg M.;
RT "A stress-inducible rat liver endoplasmic reticulum protein, ERp29.";
RL Eur. J. Biochem. 251:304-313(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Enamel epithelium, and Liver;
RX PubMed=9037184; DOI=10.1016/s0014-5793(96)01513-x;
RA Demmer J., Zhou C.M., Hubbard M.J.;
RT "Molecular cloning of ERp29, a novel and widely expressed resident of the
RT endoplasmic reticulum.";
RL FEBS Lett. 402:145-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mkrtchian S., Baryshev M., Sharipo A., Ingelman-Sundberg M.;
RT "Genomic organization of the gene encoding rat endoplasmic reticulum
RT protein ERp29.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 113-122 AND 209-223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Chen W.-Q., Afjehi-Sadat L.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Dental pulp, and Enamel epithelium;
RX PubMed=10727933; DOI=10.1046/j.1432-1327.2000.01193.x;
RA Hubbard M.J., McHugh N.J., Carne D.L.;
RT "Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel
RT cells evidence for a unique role in secretory-protein synthesis.";
RL Eur. J. Biochem. 267:1945-1957(2000).
RN [7]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [8]
RP MUTAGENESIS OF CYS-157.
RX PubMed=15572350; DOI=10.1074/jbc.m410889200;
RA Hermann V.M., Cutfield J.F., Hubbard M.J.;
RT "Biophysical characterization of ERp29: evidence for a key structural role
RT of cysteine-125.";
RL J. Biol. Chem. 280:13529-13537(2005).
RN [9]
RP STRUCTURE BY NMR OF 33-260, AND SUBUNIT.
RX PubMed=11435111; DOI=10.1016/s0969-2126(01)00607-4;
RA Liepinsh E., Baryshev M., Sharipo A., Ingelman-Sundberg M., Otting G.,
RA Mkrtchian S.;
RT "Thioredoxin fold as homodimerization module in the putative chaperone
RT ERp29: NMR structures of the domains and experimental model of the 51 kDa
RT dimer.";
RL Structure 9:457-471(2001).
CC -!- FUNCTION: Does not seem to be a disulfide isomerase. Plays an important
CC role in the processing of secretory proteins within the endoplasmic
CC reticulum (ER), possibly by participating in the folding of proteins in
CC the ER.
CC -!- SUBUNIT: Homodimer. Part of a large chaperone multiprotein complex
CC comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB,
CC SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P52555; PRO_0000021197 [P30040]: ERP29; Xeno; NbExp=2; IntAct=EBI-917740, EBI-8762218;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory tissues.
CC -!- INDUCTION: By stress.
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DR EMBL; U36482; AAC15239.1; -; mRNA.
DR EMBL; Y10264; CAA71313.1; -; mRNA.
DR EMBL; AY004254; AAF93170.1; -; Genomic_DNA.
DR EMBL; BC091129; AAH91129.1; -; mRNA.
DR RefSeq; NP_446413.1; NM_053961.2.
DR PDB; 1G7D; NMR; -; A=155-260.
DR PDB; 1G7E; NMR; -; A=33-154.
DR PDB; 2M66; NMR; -; A=155-260.
DR PDB; 6O6I; NMR; -; A=155-260.
DR PDBsum; 1G7D; -.
DR PDBsum; 1G7E; -.
DR PDBsum; 2M66; -.
DR PDBsum; 6O6I; -.
DR AlphaFoldDB; P52555; -.
DR BMRB; P52555; -.
DR SMR; P52555; -.
DR CORUM; P52555; -.
DR IntAct; P52555; 9.
DR STRING; 10116.ENSRNOP00000001822; -.
DR iPTMnet; P52555; -.
DR PhosphoSitePlus; P52555; -.
DR SwissPalm; P52555; -.
DR World-2DPAGE; 0004:P52555; -.
DR jPOST; P52555; -.
DR PaxDb; P52555; -.
DR PRIDE; P52555; -.
DR Ensembl; ENSRNOT00000001822; ENSRNOP00000001822; ENSRNOG00000001348.
DR GeneID; 117030; -.
DR KEGG; rno:117030; -.
DR UCSC; RGD:619781; rat.
DR CTD; 10961; -.
DR RGD; 619781; Erp29.
DR eggNOG; ENOG502QSHC; Eukaryota.
DR GeneTree; ENSGT00390000018566; -.
DR HOGENOM; CLU_061309_1_0_1; -.
DR InParanoid; P52555; -.
DR OMA; DGCIKEF; -.
DR OrthoDB; 1535651at2759; -.
DR PhylomeDB; P52555; -.
DR EvolutionaryTrace; P52555; -.
DR PRO; PR:P52555; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001348; Expressed in ovary and 20 other tissues.
DR Genevisible; P52555; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; TAS:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0006457; P:protein folding; TAS:RGD.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; NAS:ParkinsonsUK-UCL.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd03007; PDI_a_ERp29_N; 1.
DR Gene3D; 1.20.1150.12; -; 1.
DR InterPro; IPR016855; ERp29.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR012883; ERp29_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12211; PTHR12211; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF07912; ERp29_N; 1.
DR PIRSF; PIRSF027352; ER_p29; 1.
DR SUPFAM; SSF47933; SSF47933; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Phosphoprotein; Reference proteome; Signal; Stress response.
FT SIGNAL 1..32
FT CHAIN 33..260
FT /note="Endoplasmic reticulum resident protein 29"
FT /id="PRO_0000021199"
FT MOTIF 257..260
FT /note="Prevents secretion from ER"
FT MOD_RES 64
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P30040"
FT MOD_RES 66
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P30040"
FT MUTAGEN 157
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:15572350"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1G7E"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:1G7E"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1G7E"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1G7E"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1G7E"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:1G7E"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:1G7E"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1G7D"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1G7D"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1G7D"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1G7D"
FT HELIX 196..211
FT /evidence="ECO:0007829|PDB:1G7D"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:1G7D"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1G7D"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:1G7D"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1G7D"
SQ SEQUENCE 260 AA; 28575 MW; 8D9EBAA756ED6CA2 CRC64;
MAAAVPGAVS LSPLLSVLLG LLLLSAPHGA SGLHTKGALP LDTVTFYKVI PKSKFVLVKF
DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL
FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGCLPA YDALAGQFIE ASSREARQAI
LKQGQDGLSG VKETDKKWAS QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL
QRSLNILTAF RKKGAEKEEL
