ERP27_MOUSE
ID ERP27_MOUSE Reviewed; 272 AA.
AC Q9D8U3; Q3SX97;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Endoplasmic reticulum resident protein 27;
DE Short=ER protein 27;
DE Short=ERp27;
DE AltName: Full=Inactive protein disulfide-isomerase 27 {ECO:0000305};
DE Flags: Precursor;
GN Name=Erp27;
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=C57BL/6J; TISSUE=Pancreas;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
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: Specifically binds unfolded proteins and may recruit protein
CC disulfide isomerase PDIA3 to unfolded substrates. Binds protein
CC substrates via a hydrophobic pocket in the C-terminal domain. May play
CC a role in the unfolded stress response. {ECO:0000250|UniProtKB:Q96DN0}.
CC -!- SUBUNIT: Interacts with PDIA3. {ECO:0000250|UniProtKB:Q96DN0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q96DN0}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: Does not contain a CXXC active site motif indicating that it
CC is a catalytically redox-inactive member of the protein disulfide
CC isomerase family. {ECO:0000305}.
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DR EMBL; AK007684; BAB25188.1; -; mRNA.
DR EMBL; AK131830; BAE20822.1; -; mRNA.
DR EMBL; BC104406; AAI04407.1; -; mRNA.
DR EMBL; BC104407; AAI04408.1; -; mRNA.
DR CCDS; CCDS20660.1; -.
DR RefSeq; NP_081259.1; NM_026983.2.
DR AlphaFoldDB; Q9D8U3; -.
DR SMR; Q9D8U3; -.
DR STRING; 10090.ENSMUSP00000032343; -.
DR GlyGen; Q9D8U3; 2 sites.
DR MaxQB; Q9D8U3; -.
DR PaxDb; Q9D8U3; -.
DR PRIDE; Q9D8U3; -.
DR ProteomicsDB; 275800; -.
DR Antibodypedia; 23696; 106 antibodies from 18 providers.
DR Ensembl; ENSMUST00000032343; ENSMUSP00000032343; ENSMUSG00000030219.
DR GeneID; 69187; -.
DR KEGG; mmu:69187; -.
DR UCSC; uc009emm.1; mouse.
DR CTD; 121506; -.
DR MGI; MGI:1916437; Erp27.
DR VEuPathDB; HostDB:ENSMUSG00000030219; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00930000151058; -.
DR HOGENOM; CLU_088451_0_0_1; -.
DR InParanoid; Q9D8U3; -.
DR OMA; APSRFMF; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q9D8U3; -.
DR TreeFam; TF106381; -.
DR BioGRID-ORCS; 69187; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Erp27; mouse.
DR PRO; PR:Q9D8U3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D8U3; protein.
DR Bgee; ENSMUSG00000030219; Expressed in pancreas and 29 other tissues.
DR Genevisible; Q9D8U3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW Unfolded protein response.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..272
FT /note="Endoplasmic reticulum resident protein 27"
FT /id="PRO_0000281119"
FT DOMAIN 39..152
FT /note="Thioredoxin"
FT /evidence="ECO:0000305"
FT REGION 230..233
FT /note="PDIA3-binding site"
FT /evidence="ECO:0000250|UniProtKB:Q96DN0"
FT MOTIF 269..272
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250|UniProtKB:Q96DN0"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 104
FT /note="N -> S (in Ref. 2; AAI04407/AAI04408)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="V -> M (in Ref. 2; AAI04407/AAI04408)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="H -> L (in Ref. 2; AAI04407/AAI04408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30693 MW; B4BC442A4C54E60C CRC64;
MKITRSRCLI LSFVLVCGLV PEVTADVEEA TDGLSTTQEP IWLTDVPATV ELIAAAEVAV
IGFFQDLEIP IVSVFRSMAR QFQDVSFGIS NHSEVLTHYN VTSNSICLFR LVDDQQLHLN
AEDIENLDAA KLSRFIHVNN LHWVTEYSPM IAAGLFNTMV QTHLLLMMKK TSPEYEESMR
RYREAAKLFQ GQILFVLVDS GKRENGKVMS YFKLKESQLP ALAIYESVDD KWDTLPIAEV
TVEKVRGFCE GFLKGLLQRD HEAEGDSGKE EL
