ERP27_HUMAN
ID ERP27_HUMAN Reviewed; 273 AA.
AC Q96DN0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, 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; Synonyms=C12orf46; ORFNames=UNQ781/PRO1575;
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 [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP STRUCTURE BY NMR OF 26-141, FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH PDIA3, AND MUTAGENESIS OF MET-168; ILE-196; GLU-231; TRP-232 AND
RP ASP-233.
RX PubMed=16940051; DOI=10.1074/jbc.m604314200;
RA Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H.,
RA Kauppila A., Kellokumpu S., Ruddock L.W.;
RT "ERp27, a new non-catalytic endoplasmic reticulum-located human protein
RT disulfide isomerase family member, interacts with ERp57.";
RL J. Biol. Chem. 281:33727-33738(2006).
RN [5] {ECO:0007744|PDB:4F9Z}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 30-256, FUNCTION, AND INDUCTION.
RX PubMed=23192347; DOI=10.1074/jbc.m112.410522;
RA Kober F.X., Koelmel W., Kuper J., Drechsler J., Mais C., Hermanns H.M.,
RA Schindelin H.;
RT "The crystal structure of the protein-disulfide isomerase family member
RT ERp27 provides insights into its substrate binding capabilities.";
RL J. Biol. Chem. 288:2029-2039(2013).
CC -!- FUNCTION: Specifically binds unfolded proteins and may recruit protein
CC disulfide isomerase PDIA3 to unfolded substrates (PubMed:16940051,
CC PubMed:23192347). Binds protein substrates via a hydrophobic pocket in
CC the C-terminal domain (PubMed:16940051, PubMed:23192347). May play a
CC role in the unfolded stress response (PubMed:23192347).
CC {ECO:0000269|PubMed:16940051, ECO:0000269|PubMed:23192347}.
CC -!- SUBUNIT: Interacts with PDIA3. {ECO:0000269|PubMed:16940051}.
CC -!- INTERACTION:
CC Q96DN0; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-953772, EBI-465872;
CC Q96DN0; Q5U649: C12orf60; NbExp=3; IntAct=EBI-953772, EBI-10488839;
CC Q96DN0; P29692: EEF1D; NbExp=4; IntAct=EBI-953772, EBI-358607;
CC Q96DN0; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-953772, EBI-10181260;
CC Q96DN0; P42858: HTT; NbExp=3; IntAct=EBI-953772, EBI-466029;
CC Q96DN0; Q9H944: MED20; NbExp=3; IntAct=EBI-953772, EBI-394644;
CC Q96DN0; O43765: SGTA; NbExp=7; IntAct=EBI-953772, EBI-347996;
CC Q96DN0; P11441: UBL4A; NbExp=3; IntAct=EBI-953772, EBI-356983;
CC Q96DN0; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-953772, EBI-741480;
CC Q96DN0; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-953772, EBI-10173939;
CC Q96DN0; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-953772, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:16940051}.
CC -!- INDUCTION: Induced by ER stress. {ECO:0000269|PubMed:23192347}.
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; AY358536; AAQ88900.1; -; mRNA.
DR EMBL; AK056677; BAB71251.1; -; mRNA.
DR EMBL; BC030218; AAH30218.1; -; mRNA.
DR CCDS; CCDS8670.1; -.
DR RefSeq; NP_001287713.1; NM_001300784.1.
DR RefSeq; NP_689534.1; NM_152321.3.
DR PDB; 2L4C; NMR; -; A=26-141.
DR PDB; 4F9Z; X-ray; 2.20 A; A/B/C/D/E=30-256.
DR PDBsum; 2L4C; -.
DR PDBsum; 4F9Z; -.
DR AlphaFoldDB; Q96DN0; -.
DR SMR; Q96DN0; -.
DR BioGRID; 125733; 30.
DR IntAct; Q96DN0; 13.
DR MINT; Q96DN0; -.
DR STRING; 9606.ENSP00000266397; -.
DR GlyGen; Q96DN0; 1 site.
DR BioMuta; ERP27; -.
DR DMDM; 74731474; -.
DR MassIVE; Q96DN0; -.
DR MaxQB; Q96DN0; -.
DR PaxDb; Q96DN0; -.
DR PeptideAtlas; Q96DN0; -.
DR PRIDE; Q96DN0; -.
DR ProteomicsDB; 76296; -.
DR Antibodypedia; 23696; 106 antibodies from 18 providers.
DR DNASU; 121506; -.
DR Ensembl; ENST00000266397.7; ENSP00000266397.2; ENSG00000139055.7.
DR GeneID; 121506; -.
DR KEGG; hsa:121506; -.
DR MANE-Select; ENST00000266397.7; ENSP00000266397.2; NM_152321.4; NP_689534.1.
DR UCSC; uc001rco.4; human.
DR CTD; 121506; -.
DR GeneCards; ERP27; -.
DR HGNC; HGNC:26495; ERP27.
DR HPA; ENSG00000139055; Tissue enriched (pancreas).
DR MIM; 610642; gene.
DR neXtProt; NX_Q96DN0; -.
DR OpenTargets; ENSG00000139055; -.
DR PharmGKB; PA162385401; -.
DR VEuPathDB; HostDB:ENSG00000139055; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00930000151058; -.
DR HOGENOM; CLU_088451_0_0_1; -.
DR InParanoid; Q96DN0; -.
DR OMA; APSRFMF; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q96DN0; -.
DR TreeFam; TF106381; -.
DR BRENDA; 5.3.4.1; 2681.
DR PathwayCommons; Q96DN0; -.
DR SignaLink; Q96DN0; -.
DR BioGRID-ORCS; 121506; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; ERP27; human.
DR GenomeRNAi; 121506; -.
DR Pharos; Q96DN0; Tbio.
DR PRO; PR:Q96DN0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96DN0; protein.
DR Bgee; ENSG00000139055; Expressed in body of pancreas and 121 other tissues.
DR ExpressionAtlas; Q96DN0; baseline and differential.
DR Genevisible; Q96DN0; HS.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Signal; Unfolded protein response.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..273
FT /note="Endoplasmic reticulum resident protein 27"
FT /id="PRO_0000281118"
FT DOMAIN 39..152
FT /note="Thioredoxin"
FT /evidence="ECO:0000305"
FT REGION 230..233
FT /note="PDIA3-binding site"
FT /evidence="ECO:0000269|PubMed:16940051"
FT MOTIF 270..273
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000305|PubMed:16940051"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VARIANT 52
FT /note="F -> L (in dbSNP:rs35030722)"
FT /id="VAR_052582"
FT MUTAGEN 168
FT /note="M->W: Decreases somatostatin-14 binding."
FT /evidence="ECO:0000269|PubMed:16940051"
FT MUTAGEN 196
FT /note="I->A,L,W: Decreases somatostatin-14 binding."
FT /evidence="ECO:0000269|PubMed:16940051"
FT MUTAGEN 196
FT /note="I->W: Conserved PDIA3 binding in vivo and in vitro."
FT /evidence="ECO:0000269|PubMed:16940051"
FT MUTAGEN 231
FT /note="E->K,A: Greatly reduces PDIA3 binding in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:16940051"
FT MUTAGEN 232
FT /note="W->A: Greatly reduces PDIA3 binding in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:16940051"
FT MUTAGEN 233
FT /note="D->G: Greatly reduces PDIA3 binding in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:16940051"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:4F9Z"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4F9Z"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:4F9Z"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:4F9Z"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4F9Z"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:4F9Z"
SQ SEQUENCE 273 AA; 30480 MW; D47280F6F6FDE419 CRC64;
MEAAPSRFMF LLFLLTCELA AEVAAEVEKS SDGPGAAQEP TWLTDVPAAM EFIAATEVAV
IGFFQDLEIP AVPILHSMVQ KFPGVSFGIS TDSEVLTHYN ITGNTICLFR LVDNEQLNLE
DEDIESIDAT KLSRFIEINS LHMVTEYNPV TVIGLFNSVI QIHLLLIMNK ASPEYEENMH
RYQKAAKLFQ GKILFILVDS GMKENGKVIS FFKLKESQLP ALAIYQTLDD EWDTLPTAEV
SVEHVQNFCD GFLSGKLLKE NRESEGKTPK VEL
