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Endoplasmic reticulum resident protein 29 (ERp29) (Endoplasmic reticulum resident protein 28) (ERp28) (Endoplasmic reticulum resident protein 31) (ERp31)

 ERP29_HUMAN             Reviewed;         261 AA.
P30040; C9J183; Q3MJC3; Q6FHT4;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 4.
25-OCT-2017, entry version 184.
RecName: Full=Endoplasmic reticulum resident protein 29;
Short=ERp29;
AltName: Full=Endoplasmic reticulum resident protein 28;
Short=ERp28;
AltName: Full=Endoplasmic reticulum resident protein 31;
Short=ERp31;
Flags: Precursor;
Name=ERP29; Synonyms=C12orf8, ERP28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=9738895; DOI=10.1046/j.1432-1327.1998.2550570.x;
Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling 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.";
Eur. J. Biochem. 255:570-579(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J.,
Rifkin L., Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R.,
Williamson A., Wohldmann P., Wilson R.;
"The WashU-Merck EST project.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 33-52.
TISSUE=Liver;
PubMed=8313870; DOI=10.1002/elps.11501401181;
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
"Human liver protein map: update 1993.";
Electrophoresis 14:1216-1222(1993).
[7]
PRELIMINARY PROTEIN SEQUENCE OF 33-42.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[8]
PROTEIN SEQUENCE OF 113-122, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[9]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
Hubbard M.J.;
Submitted (DEC-1998) to UniProtKB.
[10]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=11271497;
DOI=10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2;
Hubbard M.J., McHugh N.J.;
"Human ERp29: isolation, primary structural characterisation and two-
dimensional gel mapping.";
Electrophoresis 21:3785-3796(2000).
[11]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION AT TYR-64 AND TYR-66.
PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L.,
Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.;
"A secreted tyrosine kinase acts in the extracellular environment.";
Cell 158:1033-1044(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-32, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Does not seem to be a disulfide isomerase. Plays an
important role in the processing of secretory proteins within the
endoplasmic reticulum (ER), possibly by participating in the
folding of proteins in the ER.
-!- SUBUNIT: Homodimer. Part of a large chaperone multiprotein complex
comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4,
PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or
at very low levels, CALR nor CANX.
-!- INTERACTION:
P52555:Erp29 (xeno); NbExp=2; IntAct=EBI-8762218, EBI-917740;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-946830, EBI-741480;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P30040-1; Sequence=Displayed;
Name=2;
IsoId=P30040-2; Sequence=VSP_045680, VSP_045681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory
tissues.
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EMBL; X94910; CAA64397.1; -; mRNA.
EMBL; AA412124; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR541667; CAG46468.1; -; mRNA.
EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC101493; AAI01494.1; -; mRNA.
EMBL; BC101495; AAI01496.1; -; mRNA.
CCDS; CCDS44977.1; -. [P30040-2]
CCDS; CCDS9158.1; -. [P30040-1]
PIR; T09549; T09549.
RefSeq; NP_001029197.1; NM_001034025.1. [P30040-2]
RefSeq; NP_006808.1; NM_006817.3. [P30040-1]
UniGene; Hs.75841; -.
PDB; 2QC7; X-ray; 2.90 A; A/B=34-261.
PDB; 5V8Z; X-ray; 2.10 A; A/C=158-261.
PDB; 5V90; X-ray; 3.25 A; A/C=158-261.
PDBsum; 2QC7; -.
PDBsum; 5V8Z; -.
PDBsum; 5V90; -.
ProteinModelPortal; P30040; -.
SMR; P30040; -.
BioGrid; 116160; 18.
IntAct; P30040; 15.
MINT; MINT-5002525; -.
STRING; 9606.ENSP00000261735; -.
iPTMnet; P30040; -.
PhosphoSitePlus; P30040; -.
SwissPalm; P30040; -.
BioMuta; ERP29; -.
DMDM; 6015110; -.
OGP; P30040; -.
REPRODUCTION-2DPAGE; IPI00024911; -.
SWISS-2DPAGE; P30040; -.
EPD; P30040; -.
PaxDb; P30040; -.
PeptideAtlas; P30040; -.
PRIDE; P30040; -.
TopDownProteomics; P30040-1; -. [P30040-1]
Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1]
Ensembl; ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2]
GeneID; 10961; -.
KEGG; hsa:10961; -.
UCSC; uc001ttl.1; human. [P30040-1]
CTD; 10961; -.
DisGeNET; 10961; -.
EuPathDB; HostDB:ENSG00000089248.6; -.
GeneCards; ERP29; -.
HGNC; HGNC:13799; ERP29.
HPA; HPA039363; -.
HPA; HPA039456; -.
MIM; 602287; gene.
neXtProt; NX_P30040; -.
OpenTargets; ENSG00000089248; -.
PharmGKB; PA25509; -.
eggNOG; ENOG410IX2F; Eukaryota.
eggNOG; ENOG4111I8S; LUCA.
GeneTree; ENSGT00390000018566; -.
HOGENOM; HOG000169611; -.
HOVERGEN; HBG051508; -.
InParanoid; P30040; -.
KO; K09586; -.
OMA; DGCIKEF; -.
OrthoDB; EOG091G0NH4; -.
PhylomeDB; P30040; -.
TreeFam; TF324701; -.
ChiTaRS; ERP29; human.
EvolutionaryTrace; P30040; -.
GeneWiki; ERP29; -.
GenomeRNAi; 10961; -.
PRO; PR:P30040; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000089248; -.
CleanEx; HS_ERP29; -.
ExpressionAtlas; P30040; baseline and differential.
Genevisible; P30040; HS.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL.
GO; GO:0030133; C:transport vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISS:ParkinsonsUK-UCL.
GO; GO:0000187; P:activation of MAPK activity; IDA:ParkinsonsUK-UCL.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL.
GO; GO:0050709; P:negative regulation of protein secretion; IDA:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0009306; P:protein secretion; IEA:InterPro.
GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL.
GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
CDD; cd00238; ERp29c; 1.
Gene3D; 1.20.1150.12; -; 1.
InterPro; IPR016855; ERp29.
InterPro; IPR011679; ERp29_C.
InterPro; IPR036356; ERp29_C_sf.
InterPro; IPR012883; ERp29_N.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF07749; ERp29; 1.
Pfam; PF07912; ERp29_N; 1.
PIRSF; PIRSF027352; ER_p29; 1.
SUPFAM; SSF47933; SSF47933; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00014; ER_TARGET; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein;
Reference proteome; Signal.
SIGNAL 1 32 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:8313870}.
CHAIN 33 261 Endoplasmic reticulum resident protein
29.
/FTId=PRO_0000021197.
MOTIF 258 261 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
MOD_RES 64 64 Phosphotyrosine; by PKDCC.
{ECO:0000269|PubMed:25171405}.
MOD_RES 66 66 Phosphotyrosine; by PKDCC.
{ECO:0000269|PubMed:25171405}.
VAR_SEQ 49 53 VIPKS -> IMVTS (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_045680.
VAR_SEQ 54 261 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_045681.
HELIX 45 49 {ECO:0000244|PDB:2QC7}.
HELIX 50 52 {ECO:0000244|PDB:2QC7}.
STRAND 54 60 {ECO:0000244|PDB:2QC7}.
HELIX 68 80 {ECO:0000244|PDB:2QC7}.
STRAND 86 91 {ECO:0000244|PDB:2QC7}.
STRAND 96 98 {ECO:0000244|PDB:2QC7}.
HELIX 102 107 {ECO:0000244|PDB:2QC7}.
HELIX 112 114 {ECO:0000244|PDB:2QC7}.
STRAND 116 122 {ECO:0000244|PDB:2QC7}.
HELIX 138 147 {ECO:0000244|PDB:2QC7}.
HELIX 159 170 {ECO:0000244|PDB:2QC7}.
HELIX 174 180 {ECO:0000244|PDB:2QC7}.
HELIX 183 187 {ECO:0000244|PDB:2QC7}.
HELIX 193 211 {ECO:0000244|PDB:2QC7}.
HELIX 217 230 {ECO:0000244|PDB:2QC7}.
HELIX 235 248 {ECO:0000244|PDB:2QC7}.
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


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CSB-EL007800CH Chicken Endoplasmic reticulum resident protein 29(ERP29) ELISA kit SpeciesChicken 96T


 

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