ID ERP27_BOVIN Reviewed; 272 AA.
AC Q32L47; A0A3Q1M4B2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 24-JAN-2024, entry version 93.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32L47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32L47-2; Sequence=VSP_060299;
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; BC109770; AAI09771.1; -; mRNA.
DR RefSeq; NP_001033130.1; NM_001038041.2. [Q32L47-2]
DR AlphaFoldDB; Q32L47; -.
DR SMR; Q32L47; -.
DR STRING; 9913.ENSBTAP00000065033; -.
DR GlyCosmos; Q32L47; 1 site, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000006649; -.
DR Ensembl; ENSBTAT00000006649.4; ENSBTAP00000006649.3; ENSBTAG00000006036.5. [Q32L47-2]
DR GeneID; 505855; -.
DR KEGG; bta:505855; -.
DR CTD; 121506; -.
DR VEuPathDB; HostDB:ENSBTAG00000006036; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00930000151058; -.
DR HOGENOM; CLU_088451_0_0_1; -.
DR InParanoid; Q32L47; -.
DR OrthoDB; 4188393at2759; -.
DR TreeFam; TF106381; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000006036; Expressed in dorsal thalamus and 76 other cell types or tissues.
DR ExpressionAtlas; Q32L47; baseline.
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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal; 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_0000281117"
FT DOMAIN 38..151
FT /note="Thioredoxin"
FT /evidence="ECO:0000305"
FT REGION 229..232
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 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 192..257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060299"
SQ SEQUENCE 272 AA; 30399 MW; F7F5D51738C01428 CRC64;
MEAMPSRCLF LLFLSTCKLS PEVVAEVQES SDGPGAQEPM RLTDVQAAME FIAAAEVAVI
GFFQDSEVPA VSLIHSVVQN FQDVSFGIST ASEVLAYYNI TGNTISLFRL VDNKQLDLKG
EDFESMDATK LSRFIESNNL RLVTEYNAIT AIGLFNSMIP IHLLLIMNKA SSEFEENLHR
FQEAAKLFQG RILFILVDSG VKQNEKAISF FKLKMAELPA LAIYQTLDDK WDTLPITEVL
VEQVQNFCDG FLKGKGLRQN HEAKEKTSKV EL
//
