ID ERP29_HUMAN Reviewed; 261 AA. AC P30040; Q6FHT4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 4. DT 23-JAN-2007, entry version 71. DE Endoplasmic reticulum protein ERp29 precursor (ERp31) (ERp28). 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; 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 PROTEIN SEQUENCE OF 33-52. RC TISSUE=Liver; RX MEDLINE=94147969; PubMed=8313870; 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 [4] RP PRELIMINARY PROTEIN SEQUENCE OF 33-42. RC TISSUE=Liver; RX MEDLINE=93162045; PubMed=1286669; 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 [5] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RA Hubbard M.J.; RL Submitted (DEC-1998) to Swiss-Prot. RN [6] 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 [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=12643545; 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 [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. 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). 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. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC lumen. Melanosome. Note=Identified by mass spectrometry in CC melanosome fractions from 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 PIR; T09549; T09549. DR UniGene; Hs.75841; -. DR HSSP; P52555; 1G7E. DR SMR; P30040; 33-154, 155-261. DR SWISS-2DPAGE; P30040; HUMAN. DR OGP; P30040; -. DR Siena-2DPAGE; P30040; -. DR Ensembl; ENSG00000089248; Homo sapiens. DR KEGG; hsa:10961; -. DR HGNC; HGNC:13799; ERP29. DR MIM; 602287; gene. DR LinkHub; P30040; -. DR ArrayExpress; P30040; -. DR GermOnline; ENSG00000089248; Homo sapiens. DR RZPD-ProtExp; I0555; -. DR RZPD-ProtExp; RZPDo834E0727; -. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. 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 InterPro; IPR000886; ER_target_S. DR InterPro; IPR011679; ERp29_C. DR InterPro; IPR013331; ERp29_C_type. DR InterPro; IPR012883; ERp29_N. DR InterPro; IPR012336; Thiordxn-like_fd. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:1.20.1150.12; ERp29_C; 1. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF07749; ERp29; 1. DR Pfam; PF07912; ERp29_N; 1. DR PROSITE; PS00014; ER_TARGET; 1. KW Direct protein sequencing; Endoplasmic reticulum; Signal. FT SIGNAL 1 32 FT CHAIN 33 261 Endoplasmic reticulum protein ERp29. FT /FTId=PRO_0000021197. FT MOTIF 258 261 Prevents secretion from ER (By FT similarity). 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 //