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   03-AUG-2022, entry version 88.
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.ENSBTAP00000006649; -.
DR   PaxDb; Q32L47; -.
DR   Ensembl; ENSBTAT00000006649; ENSBTAP00000006649; ENSBTAG00000006036. [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; 462118at2759; -.
DR   TreeFam; TF106381; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000006036; Expressed in dorsal thalamus and 76 other tissues.
DR   ExpressionAtlas; Q32L47; baseline and differential.
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   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