ID ERP29_HUMAN Reviewed; 261 AA. AC P30040; Q3MJC3; Q6FHT4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 4. DT 05-APR-2011, entry version 122. DE RecName: Full=Endoplasmic reticulum resident protein 29; DE Short=ERp29; DE AltName: Full=Endoplasmic reticulum resident protein 28; DE Short=ERp28; DE AltName: Full=Endoplasmic reticulum resident protein 31; DE Short=ERp31; DE Flags: Precursor; GN Name=ERP29; Synonyms=C12orf8, ERP28; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC TISSUE=Liver; RX MEDLINE=98409275; PubMed=9738895; RX DOI=10.1046/j.1432-1327.1998.2550570.x; RA Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.; RT "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of RT the protein disulfide isomerase family but lacks a CXXC thioredoxin- RT box motif."; RL Eur. J. Biochem. 255:570-579(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 PROTEIN SEQUENCE OF 33-52. RC TISSUE=Liver; RX MEDLINE=94147969; PubMed=8313870; DOI=10.1002/elps.11501401181; RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.; RT "Human liver protein map: update 1993."; RL Electrophoresis 14:1216-1222(1993). RN [5] RP PRELIMINARY PROTEIN SEQUENCE OF 33-42. RC TISSUE=Liver; RX MEDLINE=93162045; PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [6] RP PROTEIN SEQUENCE OF 113-122, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [7] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RA Hubbard M.J.; RL Submitted (DEC-1998) to UniProtKB. RN [8] RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Liver; RX MEDLINE=21088920; PubMed=11271497; RX DOI=10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2; RA Hubbard M.J., McHugh N.J.; RT "Human ERp29: isolation, primary structural characterisation and two- RT dimensional gel mapping."; RL Electrophoresis 21:3785-3796(2000). RN [9] 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 RT complexes in endoplasmic reticulum to bind nascent proteins."; RL Mol. Biol. Cell 13:4456-4469(2002). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., RA Hearing V.J., Hunt D.F., Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64 AND TYR-66, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Does not seem to be a disulfide isomerase. Plays an CC important role in the processing of secretory proteins within the CC endoplasmic reticulum (ER), possibly by participating in the CC folding of proteins in the ER. CC -!- SUBUNIT: Homodimer. Part a large chaperone multiprotein complex CC comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, CC PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or CC at very low levels, CALR nor CANX. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory CC tissues. 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; X94910; CAA64397.1; -; mRNA. DR EMBL; CR541667; CAG46468.1; -; mRNA. DR EMBL; BC101493; AAI01494.1; -; mRNA. DR EMBL; BC101495; AAI01496.1; -; mRNA. DR IPI; IPI00024911; -. DR PIR; T09549; T09549. DR RefSeq; NP_006808.1; NM_006817.3. DR UniGene; Hs.75841; -. DR PDB; 2QC7; X-ray; 2.90 A; A/B=34-261. DR PDBsum; 2QC7; -. DR ProteinModelPortal; P30040; -. DR SMR; P30040; 33-256. DR IntAct; P30040; 8. DR MINT; MINT-5002525; -. DR STRING; P30040; -. DR PhosphoSite; P30040; -. DR SWISS-2DPAGE; P30040; -. DR OGP; P30040; -. DR REPRODUCTION-2DPAGE; IPI00024911; -. DR Siena-2DPAGE; P30040; -. DR PeptideAtlas; P30040; -. DR PRIDE; P30040; -. DR Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248. DR GeneID; 10961; -. DR KEGG; hsa:10961; -. DR UCSC; uc001ttk.1; human. DR CTD; 10961; -. DR GeneCards; GC12P109464; -. DR H-InvDB; HIX0036837; -. DR HGNC; HGNC:13799; ERP29. DR MIM; 602287; gene. DR neXtProt; NX_P30040; -. DR eggNOG; prNOG12363; -. DR GeneTree; ENSGT00390000018566; -. DR HOGENOM; HBG278228; -. DR HOVERGEN; HBG051508; -. DR InParanoid; P30040; -. DR OMA; KIMGKVL; -. DR OrthoDB; EOG45QHF1; -. DR PhylomeDB; P30040; -. DR NextBio; 41652; -. DR ArrayExpress; P30040; -. DR Bgee; P30040; -. DR CleanEx; HS_ERP29; -. DR Genevestigator; P30040; -. DR GermOnline; ENSG00000089248; Homo sapiens. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0006457; P:protein folding; TAS:ProtInc. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR016855; ER_p29. DR InterPro; IPR011679; ER_p29_C. DR InterPro; IPR012883; ERp29_N. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:1.20.1150.12; ERp29_C_type; 1. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF07749; ERp29; 1. DR Pfam; PF07912; ERp29_N; 1. DR PIRSF; PIRSF027352; ER_p29; 1. DR SUPFAM; SSF47933; ERP29_C; 1. DR SUPFAM; SSF52833; Thiordxn-like_fd; 1. DR PROSITE; PS00014; ER_TARGET; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Phosphoprotein; Signal. FT SIGNAL 1 32 FT CHAIN 33 261 Endoplasmic reticulum resident protein FT 29. FT /FTId=PRO_0000021197. FT MOTIF 258 261 Prevents secretion from ER (By FT similarity). FT MOD_RES 64 64 Phosphotyrosine. FT MOD_RES 66 66 Phosphotyrosine. FT HELIX 45 49 FT HELIX 50 52 FT STRAND 54 60 FT HELIX 68 80 FT STRAND 86 91 FT STRAND 96 98 FT HELIX 102 107 FT HELIX 112 114 FT STRAND 116 122 FT HELIX 138 147 FT HELIX 159 170 FT HELIX 174 180 FT HELIX 183 187 FT HELIX 193 211 FT HELIX 217 230 FT HELIX 235 248 SQ SEQUENCE 261 AA; 28993 MW; 76145006433A1983 CRC64; MAAAVPRAAF LSPLLPLLLG FLLLSAPHGG SGLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYTGAVKVGA IQRWLKGQGV YLGMPGCLPV YDALAGEFIR ASGVEARQAL LKQGQDNLSS VKETQKKWAE QYLKIMGKIL DQGEDFPASE MTRIARLIEK NKMSDGKKEE LQKSLNILTA FQKKGAEKEE L //