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   24-JAN-2024, entry version 149.
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   GlyCosmos; Q9D8U3; 2 sites, No reported glycans.
DR   GlyGen; Q9D8U3; 2 sites.
DR   MaxQB; Q9D8U3; -.
DR   PaxDb; 10090-ENSMUSP00000032343; -.
DR   ProteomicsDB; 275800; -.
DR   Antibodypedia; 23696; 127 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000032343.7; ENSMUSP00000032343.7; ENSMUSG00000030219.14.
DR   GeneID; 69187; -.
DR   KEGG; mmu:69187; -.
DR   UCSC; uc009emm.1; mouse.
DR   AGR; MGI:1916437; -.
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; EESHGYK; -.
DR   OrthoDB; 4188393at2759; -.
DR   PhylomeDB; Q9D8U3; -.
DR   TreeFam; TF106381; -.
DR   BioGRID-ORCS; 69187; 2 hits in 78 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 30 other cell types or tissues.
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   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR18929:SF193; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 27; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q9D8U3; MM.
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
//