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   24-JAN-2024, entry version 179.
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   jPOST; P52555; -.
DR   PaxDb; 10116-ENSRNOP00000001822; -.
DR   Ensembl; ENSRNOT00000001822.6; ENSRNOP00000001822.3; ENSRNOG00000001348.6.
DR   Ensembl; ENSRNOT00055023659; ENSRNOP00055019263; ENSRNOG00055013763.
DR   Ensembl; ENSRNOT00060003165; ENSRNOP00060002150; ENSRNOG00060002013.
DR   Ensembl; ENSRNOT00065011982; ENSRNOP00065008743; ENSRNOG00065007665.
DR   GeneID; 117030; -.
DR   KEGG; rno:117030; -.
DR   UCSC; RGD:619781; rat.
DR   AGR; RGD:619781; -.
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; KYVLVKF; -.
DR   OrthoDB; 5403558at2759; -.
DR   PhylomeDB; P52555; -.
DR   EvolutionaryTrace; P52555; -.
DR   PRO; PR:P52555; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001348; Expressed in ovary and 20 other cell types or tissues.
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:0042803; F:protein homodimerization activity; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI: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: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; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; ENDOPLASMIC RETICULUM PROTEIN ERP29; 1.
DR   PANTHER; PTHR12211:SF0; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 29; 1.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF07912; ERp29_N; 1.
DR   PIRSF; PIRSF027352; ER_p29; 1.
DR   SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   World-2DPAGE; 0004:P52555; -.
DR   Genevisible; P52555; RN.
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
//