ERP29_HUMAN
ID ERP29_HUMAN Reviewed; 261 AA.
AC P30040; C9J183; Q3MJC3; Q6FHT4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 4.
DT 03-AUG-2022, entry version 216.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 the
RT protein disulfide isomerase family but lacks a CXXC thioredoxin-box
RT 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., Rifkin L.,
RA Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A.,
RA 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., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., 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., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., 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., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA 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 project:
RT 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 IDENTIFICATION BY 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 complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA 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].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION AT TYR-64 AND TYR-66.
RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M.,
RA Dixon J.E., Yeo C.Y., Whitman M.;
RT "A secreted tyrosine kinase acts in the extracellular environment.";
RL Cell 158:1033-1044(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 (PubMed:12475965). {ECO:0000269|PubMed:12475965}.
CC -!- INTERACTION:
CC P30040; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-946830, EBI-10827839;
CC P30040; O95393: BMP10; NbExp=3; IntAct=EBI-946830, EBI-3922513;
CC P30040; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-946830, EBI-2806959;
CC P30040; Q9P0W2: HMG20B; NbExp=6; IntAct=EBI-946830, EBI-713401;
CC P30040; Q8IXM6: NRM; NbExp=3; IntAct=EBI-946830, EBI-10262547;
CC P30040; O43765: SGTA; NbExp=3; IntAct=EBI-946830, EBI-347996;
CC P30040; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-946830, EBI-744081;
CC P30040; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-946830, EBI-10281213;
CC P30040; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-946830, EBI-10314552;
CC P30040; P55061: TMBIM6; NbExp=3; IntAct=EBI-946830, EBI-1045825;
CC P30040; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-946830, EBI-2548832;
CC P30040; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-946830, EBI-12195249;
CC P30040; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-946830, EBI-10243654;
CC P30040; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-946830, EBI-741480;
CC P30040; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-946830, EBI-947187;
CC PRO_0000021197; P52555: Erp29; Xeno; NbExp=2; IntAct=EBI-8762218, EBI-917740;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC 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 -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in secretory 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 CCDS; CCDS44977.1; -. [P30040-2]
DR CCDS; CCDS9158.1; -. [P30040-1]
DR PIR; T09549; T09549.
DR RefSeq; NP_001029197.1; NM_001034025.1. [P30040-2]
DR RefSeq; NP_006808.1; NM_006817.3. [P30040-1]
DR PDB; 2QC7; X-ray; 2.90 A; A/B=34-261.
DR PDB; 5V8Z; X-ray; 2.10 A; A/C=158-261.
DR PDB; 5V90; X-ray; 3.25 A; A/C=158-261.
DR PDBsum; 2QC7; -.
DR PDBsum; 5V8Z; -.
DR PDBsum; 5V90; -.
DR AlphaFoldDB; P30040; -.
DR BMRB; P30040; -.
DR SMR; P30040; -.
DR BioGRID; 116160; 101.
DR IntAct; P30040; 52.
DR STRING; 9606.ENSP00000261735; -.
DR GlyGen; P30040; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P30040; -.
DR MetOSite; P30040; -.
DR PhosphoSitePlus; P30040; -.
DR SwissPalm; P30040; -.
DR BioMuta; ERP29; -.
DR DMDM; 6015110; -.
DR OGP; P30040; -.
DR REPRODUCTION-2DPAGE; IPI00024911; -.
DR SWISS-2DPAGE; P30040; -.
DR CPTAC; CPTAC-196; -.
DR CPTAC; CPTAC-197; -.
DR EPD; P30040; -.
DR jPOST; P30040; -.
DR MassIVE; P30040; -.
DR MaxQB; P30040; -.
DR PaxDb; P30040; -.
DR PeptideAtlas; P30040; -.
DR PRIDE; P30040; -.
DR ProteomicsDB; 54619; -. [P30040-1]
DR ProteomicsDB; 8041; -.
DR TopDownProteomics; P30040-1; -. [P30040-1]
DR Antibodypedia; 18632; 338 antibodies from 37 providers.
DR DNASU; 10961; -.
DR Ensembl; ENST00000261735.4; ENSP00000261735.3; ENSG00000089248.7. [P30040-1]
DR Ensembl; ENST00000455836.1; ENSP00000412083.1; ENSG00000089248.7. [P30040-2]
DR GeneID; 10961; -.
DR KEGG; hsa:10961; -.
DR MANE-Select; ENST00000261735.4; ENSP00000261735.3; NM_006817.4; NP_006808.1.
DR UCSC; uc001ttl.1; human. [P30040-1]
DR CTD; 10961; -.
DR DisGeNET; 10961; -.
DR GeneCards; ERP29; -.
DR HGNC; HGNC:13799; ERP29.
DR HPA; ENSG00000089248; Low tissue specificity.
DR MIM; 602287; gene.
DR neXtProt; NX_P30040; -.
DR OpenTargets; ENSG00000089248; -.
DR PharmGKB; PA25509; -.
DR VEuPathDB; HostDB:ENSG00000089248; -.
DR eggNOG; ENOG502QSHC; Eukaryota.
DR GeneTree; ENSGT00390000018566; -.
DR HOGENOM; CLU_061309_1_0_1; -.
DR InParanoid; P30040; -.
DR OMA; DGCIKEF; -.
DR PhylomeDB; P30040; -.
DR TreeFam; TF324701; -.
DR PathwayCommons; P30040; -.
DR SignaLink; P30040; -.
DR BioGRID-ORCS; 10961; 15 hits in 1071 CRISPR screens.
DR ChiTaRS; ERP29; human.
DR EvolutionaryTrace; P30040; -.
DR GeneWiki; ERP29; -.
DR GenomeRNAi; 10961; -.
DR Pharos; P30040; Tbio.
DR PRO; PR:P30040; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P30040; protein.
DR Bgee; ENSG00000089248; Expressed in endometrium epithelium and 207 other tissues.
DR ExpressionAtlas; P30040; baseline and differential.
DR Genevisible; P30040; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:ParkinsonsUK-UCL.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030133; C:transport vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; NAS:ParkinsonsUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006457; P:protein folding; NAS:ParkinsonsUK-UCL.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL.
DR GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd03007; PDI_a_ERp29_N; 1.
DR Gene3D; 1.20.1150.12; -; 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; PTHR12211; 1.
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; Direct protein sequencing;
KW Endoplasmic reticulum; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:8313870,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 33..261
FT /note="Endoplasmic reticulum resident protein 29"
FT /id="PRO_0000021197"
FT MOTIF 258..261
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 64
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000269|PubMed:25171405"
FT MOD_RES 66
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000269|PubMed:25171405"
FT VAR_SEQ 49..53
FT /note="VIPKS -> IMVTS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045680"
FT VAR_SEQ 54..261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045681"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2QC7"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2QC7"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2QC7"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2QC7"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:2QC7"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:5V8Z"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:5V8Z"
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
