Full text data of ERP29
ERP29
(C12orf8, ERP28)
[Confidence: high (present in two of the MS resources)]
Endoplasmic reticulum resident protein 29; ERp29 (Endoplasmic reticulum resident protein 28; ERp28; Endoplasmic reticulum resident protein 31; ERp31; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Endoplasmic reticulum resident protein 29; ERp29 (Endoplasmic reticulum resident protein 28; ERp28; Endoplasmic reticulum resident protein 31; ERp31; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00024911
IPI00024911 Endoplasmic reticulum protein ERp29 precursor Endoplasmic reticulum protein ERp29 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 2 ER lumen n/a found at its expected molecular weight found at molecular weight
IPI00024911 Endoplasmic reticulum protein ERp29 precursor Endoplasmic reticulum protein ERp29 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 2 ER lumen n/a found at its expected molecular weight found at molecular weight
UniProt
P30040
ID ERP29_HUMAN Reviewed; 261 AA.
AC P30040; C9J183; Q3MJC3; Q6FHT4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-1998, sequence version 4.
DT 22-JAN-2014, entry version 145.
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] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=9738895; 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] (ISOFORM 2).
RC TISSUE=Testis;
RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J.,
RA Rifkin L., Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R.,
RA Williamson A., Wohldmann P., Wilson R.;
RT "The WashU-Merck EST project.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 33-52.
RC TISSUE=Liver;
RX 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 [7]
RP PRELIMINARY PROTEIN SEQUENCE OF 33-42.
RC TISSUE=Liver;
RX 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 [8]
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 [9]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RA Hubbard M.J.;
RL Submitted (DEC-1998) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Liver;
RX 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 [11]
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 [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 of 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30040-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30040-2; Sequence=VSP_045680, VSP_045681;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory
CC tissues.
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DR EMBL; X94910; CAA64397.1; -; mRNA.
DR EMBL; AA412124; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR541667; CAG46468.1; -; mRNA.
DR EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101493; AAI01494.1; -; mRNA.
DR EMBL; BC101495; AAI01496.1; -; mRNA.
DR PIR; T09549; T09549.
DR RefSeq; NP_001029197.1; NM_001034025.1.
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; 5.
DR MINT; MINT-5002525; -.
DR STRING; 9606.ENSP00000261735; -.
DR PhosphoSite; P30040; -.
DR DMDM; 6015110; -.
DR OGP; P30040; -.
DR REPRODUCTION-2DPAGE; IPI00024911; -.
DR SWISS-2DPAGE; P30040; -.
DR PaxDb; P30040; -.
DR PeptideAtlas; P30040; -.
DR PRIDE; P30040; -.
DR Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248.
DR Ensembl; ENST00000455836; ENSP00000412083; ENSG00000089248.
DR GeneID; 10961; -.
DR KEGG; hsa:10961; -.
DR UCSC; uc001ttl.1; human.
DR CTD; 10961; -.
DR GeneCards; GC12P112451; -.
DR HGNC; HGNC:13799; ERP29.
DR HPA; HPA039363; -.
DR HPA; HPA039456; -.
DR MIM; 602287; gene.
DR neXtProt; NX_P30040; -.
DR PharmGKB; PA25509; -.
DR eggNOG; NOG82861; -.
DR HOGENOM; HOG000046371; -.
DR HOVERGEN; HBG051508; -.
DR InParanoid; P30040; -.
DR KO; K09586; -.
DR OMA; PYGEKHE; -.
DR OrthoDB; EOG7XH6RH; -.
DR PhylomeDB; P30040; -.
DR ChiTaRS; ERP29; human.
DR EvolutionaryTrace; P30040; -.
DR GeneWiki; ERP29; -.
DR GenomeRNAi; 10961; -.
DR NextBio; 41652; -.
DR PRO; PR:P30040; -.
DR ArrayExpress; P30040; -.
DR Bgee; P30040; -.
DR CleanEx; HS_ERP29; -.
DR Genevestigator; P30040; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
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:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 1.20.1150.12; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR016855; ER_p29.
DR InterPro; IPR011679; ER_p29_C.
DR InterPro; IPR012883; ERp29_N.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Reference proteome;
KW 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 VAR_SEQ 49 53 VIPKS -> IMVTS (in isoform 2).
FT /FTId=VSP_045680.
FT VAR_SEQ 54 261 Missing (in isoform 2).
FT /FTId=VSP_045681.
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
//
ID ERP29_HUMAN Reviewed; 261 AA.
AC P30040; C9J183; Q3MJC3; Q6FHT4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-1998, sequence version 4.
DT 22-JAN-2014, entry version 145.
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] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=9738895; 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] (ISOFORM 2).
RC TISSUE=Testis;
RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J.,
RA Rifkin L., Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R.,
RA Williamson A., Wohldmann P., Wilson R.;
RT "The WashU-Merck EST project.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 33-52.
RC TISSUE=Liver;
RX 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 [7]
RP PRELIMINARY PROTEIN SEQUENCE OF 33-42.
RC TISSUE=Liver;
RX 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 [8]
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 [9]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RA Hubbard M.J.;
RL Submitted (DEC-1998) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Liver;
RX 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 [11]
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 [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 of 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30040-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30040-2; Sequence=VSP_045680, VSP_045681;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory
CC tissues.
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DR EMBL; X94910; CAA64397.1; -; mRNA.
DR EMBL; AA412124; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR541667; CAG46468.1; -; mRNA.
DR EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101493; AAI01494.1; -; mRNA.
DR EMBL; BC101495; AAI01496.1; -; mRNA.
DR PIR; T09549; T09549.
DR RefSeq; NP_001029197.1; NM_001034025.1.
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; 5.
DR MINT; MINT-5002525; -.
DR STRING; 9606.ENSP00000261735; -.
DR PhosphoSite; P30040; -.
DR DMDM; 6015110; -.
DR OGP; P30040; -.
DR REPRODUCTION-2DPAGE; IPI00024911; -.
DR SWISS-2DPAGE; P30040; -.
DR PaxDb; P30040; -.
DR PeptideAtlas; P30040; -.
DR PRIDE; P30040; -.
DR Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248.
DR Ensembl; ENST00000455836; ENSP00000412083; ENSG00000089248.
DR GeneID; 10961; -.
DR KEGG; hsa:10961; -.
DR UCSC; uc001ttl.1; human.
DR CTD; 10961; -.
DR GeneCards; GC12P112451; -.
DR HGNC; HGNC:13799; ERP29.
DR HPA; HPA039363; -.
DR HPA; HPA039456; -.
DR MIM; 602287; gene.
DR neXtProt; NX_P30040; -.
DR PharmGKB; PA25509; -.
DR eggNOG; NOG82861; -.
DR HOGENOM; HOG000046371; -.
DR HOVERGEN; HBG051508; -.
DR InParanoid; P30040; -.
DR KO; K09586; -.
DR OMA; PYGEKHE; -.
DR OrthoDB; EOG7XH6RH; -.
DR PhylomeDB; P30040; -.
DR ChiTaRS; ERP29; human.
DR EvolutionaryTrace; P30040; -.
DR GeneWiki; ERP29; -.
DR GenomeRNAi; 10961; -.
DR NextBio; 41652; -.
DR PRO; PR:P30040; -.
DR ArrayExpress; P30040; -.
DR Bgee; P30040; -.
DR CleanEx; HS_ERP29; -.
DR Genevestigator; P30040; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
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:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 1.20.1150.12; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR016855; ER_p29.
DR InterPro; IPR011679; ER_p29_C.
DR InterPro; IPR012883; ERp29_N.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Reference proteome;
KW 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 VAR_SEQ 49 53 VIPKS -> IMVTS (in isoform 2).
FT /FTId=VSP_045680.
FT VAR_SEQ 54 261 Missing (in isoform 2).
FT /FTId=VSP_045681.
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
//
MIM
602287
*RECORD*
*FIELD* NO
602287
*FIELD* TI
*602287 ENDOPLASMIC RETICULUM PROTEIN, 29-KD; ERP29
;;CHROMOSOME 12 OPEN READING FRAME 8; C12ORF8;;
read moreERp29;;
ERP28
*FIELD* TX
CLONING
Reticuloplasmins are proteins found in the lumen of the endoplasmic
reticulum (ER). Demmer et al. (1997) cloned ERp29, a 29-kD
reticuloplasmin, from rat enamel cells by microsequencing of the
purified protein followed by RT-PCR. ERp29 has the N-terminal
hydrophobic signal sequence and C-terminal endoplasmic reticulum
retention motif (KEEL) characteristic of reticuloplasmins, but lacks
calcium-binding motifs. Northern blot analysis showed that ERp29 is
widely expressed in rat tissues. A homologous transcript was expressed
in human hepatoma cells.
Ferrari et al. (1998) cloned ERP29, which they designated ERP28, from a
human liver cDNA library. The deduced 229-amino acid protein has a
calculated molecular mass of 24.8 kD and contains the KEEL ER retention
signal. The purified protein migrates as a dimer under nondenaturing
conditions and as a 28-kD monomer by SDS-PAGE. The same apparent masses
are seen with recombinant protein and protein purified from human
hepatocellular carcinoma cells or from bovine liver, indicating lack of
glycosylation. Ferrari et al. (1998) found that ERP29 shares 92%
sequence identity with the rat homolog. It shows low but significant
similarity with members of the protein disulfide isomerase family (see
176790), but does not contain a reactive thioredoxin-box motif.
Immunofluorescence and subcellular fractionation studies showed
colocalization of ERP29 with calreticulin (109091) in the ER.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ERP29
gene to chromosome 12 (TMAP SGC31784).
*FIELD* RF
1. Demmer, J.; Zhou, C.; Hubbard, M. J.: Molecular cloning of ERp29,
a novel and widely expressed resident of the endoplasmic reticulum. FEBS
Lett. 402: 145-150, 1997.
2. Ferrari, D. M.; Nguyen Van, P.; Kratzin, H. D.; Soling, H.-D.:
ERp28, a human endoplasmic-reticulum-lumenal protein, is a member
of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box
motif. Europ. J. Biochem. 255: 570-579, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 4/5/2002
*FIELD* CD
Rebekah S. Rasooly: 1/27/1998
*FIELD* ED
wwang: 10/12/2007
terry: 5/23/2007
carol: 4/5/2002
terry: 3/27/2002
carol: 2/4/1998
*RECORD*
*FIELD* NO
602287
*FIELD* TI
*602287 ENDOPLASMIC RETICULUM PROTEIN, 29-KD; ERP29
;;CHROMOSOME 12 OPEN READING FRAME 8; C12ORF8;;
read moreERp29;;
ERP28
*FIELD* TX
CLONING
Reticuloplasmins are proteins found in the lumen of the endoplasmic
reticulum (ER). Demmer et al. (1997) cloned ERp29, a 29-kD
reticuloplasmin, from rat enamel cells by microsequencing of the
purified protein followed by RT-PCR. ERp29 has the N-terminal
hydrophobic signal sequence and C-terminal endoplasmic reticulum
retention motif (KEEL) characteristic of reticuloplasmins, but lacks
calcium-binding motifs. Northern blot analysis showed that ERp29 is
widely expressed in rat tissues. A homologous transcript was expressed
in human hepatoma cells.
Ferrari et al. (1998) cloned ERP29, which they designated ERP28, from a
human liver cDNA library. The deduced 229-amino acid protein has a
calculated molecular mass of 24.8 kD and contains the KEEL ER retention
signal. The purified protein migrates as a dimer under nondenaturing
conditions and as a 28-kD monomer by SDS-PAGE. The same apparent masses
are seen with recombinant protein and protein purified from human
hepatocellular carcinoma cells or from bovine liver, indicating lack of
glycosylation. Ferrari et al. (1998) found that ERP29 shares 92%
sequence identity with the rat homolog. It shows low but significant
similarity with members of the protein disulfide isomerase family (see
176790), but does not contain a reactive thioredoxin-box motif.
Immunofluorescence and subcellular fractionation studies showed
colocalization of ERP29 with calreticulin (109091) in the ER.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ERP29
gene to chromosome 12 (TMAP SGC31784).
*FIELD* RF
1. Demmer, J.; Zhou, C.; Hubbard, M. J.: Molecular cloning of ERp29,
a novel and widely expressed resident of the endoplasmic reticulum. FEBS
Lett. 402: 145-150, 1997.
2. Ferrari, D. M.; Nguyen Van, P.; Kratzin, H. D.; Soling, H.-D.:
ERp28, a human endoplasmic-reticulum-lumenal protein, is a member
of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box
motif. Europ. J. Biochem. 255: 570-579, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 4/5/2002
*FIELD* CD
Rebekah S. Rasooly: 1/27/1998
*FIELD* ED
wwang: 10/12/2007
terry: 5/23/2007
carol: 4/5/2002
terry: 3/27/2002
carol: 2/4/1998