ERP29_MOUSE
ID ERP29_MOUSE Reviewed; 262 AA.
AC P57759; Q3THW3; Q9CQ42;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Endoplasmic reticulum resident protein 29;
DE Short=ERp29;
DE Flags: Precursor;
GN Name=Erp29;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Lung, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP PROTEIN SEQUENCE OF 115-124, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}. Melanosome {ECO:0000250}.
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; AK004795; BAB23570.1; -; mRNA.
DR EMBL; AK009881; BAB26559.1; -; mRNA.
DR EMBL; AK154539; BAE32664.1; -; mRNA.
DR EMBL; AK168112; BAE40083.1; -; mRNA.
DR EMBL; BC017125; AAH17125.1; -; mRNA.
DR CCDS; CCDS19634.1; -.
DR RefSeq; NP_080405.1; NM_026129.2.
DR AlphaFoldDB; P57759; -.
DR SMR; P57759; -.
DR BioGRID; 212160; 1.
DR IntAct; P57759; 1.
DR STRING; 10090.ENSMUSP00000117347; -.
DR iPTMnet; P57759; -.
DR PhosphoSitePlus; P57759; -.
DR SwissPalm; P57759; -.
DR COMPLUYEAST-2DPAGE; P57759; -.
DR REPRODUCTION-2DPAGE; P57759; -.
DR EPD; P57759; -.
DR jPOST; P57759; -.
DR MaxQB; P57759; -.
DR PaxDb; P57759; -.
DR PeptideAtlas; P57759; -.
DR PRIDE; P57759; -.
DR ProteomicsDB; 275539; -.
DR Antibodypedia; 18632; 338 antibodies from 37 providers.
DR DNASU; 67397; -.
DR Ensembl; ENSMUST00000130451; ENSMUSP00000117347; ENSMUSG00000029616.
DR GeneID; 67397; -.
DR KEGG; mmu:67397; -.
DR UCSC; uc008zjf.1; mouse.
DR CTD; 10961; -.
DR MGI; MGI:1914647; Erp29.
DR VEuPathDB; HostDB:ENSMUSG00000029616; -.
DR eggNOG; ENOG502QSHC; Eukaryota.
DR GeneTree; ENSGT00390000018566; -.
DR HOGENOM; CLU_061309_1_0_1; -.
DR InParanoid; P57759; -.
DR OMA; DGCIKEF; -.
DR OrthoDB; 1535651at2759; -.
DR PhylomeDB; P57759; -.
DR TreeFam; TF324701; -.
DR BioGRID-ORCS; 67397; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Erp29; mouse.
DR PRO; PR:P57759; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P57759; protein.
DR Bgee; ENSMUSG00000029616; Expressed in dorsal pancreas and 266 other tissues.
DR ExpressionAtlas; P57759; baseline and differential.
DR Genevisible; P57759; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; NAS:ParkinsonsUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
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 Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT CHAIN 35..262
FT /note="Endoplasmic reticulum resident protein 29"
FT /id="PRO_0000021198"
FT MOTIF 259..262
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 66
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P30040"
FT MOD_RES 68
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P30040"
SQ SEQUENCE 262 AA; 28823 MW; CA4C83757CA8732B CRC64;
MAAAAGVSGA ASLSPLLSVL LGLLLLFAPH GGSGLHTKGA LPLDTVTFYK VIPKSKFVLV
KFDTQYPYGE KQDEFKRLAE NSASSEELLV AEVGISDYGD KLNMELSEKY KLDKESYPVF
YLFRDGDLEN PVLYNGAVKV GAIQRWLKGQ GVYLGMPGCL PAYDALAGEF IKASSIEARQ
AILKQGQDGL LSVKETEKKW ASQYLKIMGK ILDQGEDFPA SEMARIGKLI ENKMSDSKKE
ELQKSLNILT AFRKKEAEKE EL
