ID   ERP29_BOVIN             Reviewed;         258 AA.
AC   P81623; Q17QC3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Endoplasmic reticulum resident protein 29;
DE            Short=ERp29;
DE   Flags: Precursor;
GN   Name=ERP29;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 30-50 AND 204-213.
RC   TISSUE=Liver;
RX   PubMed=9738895; DOI=10.1046/j.1432-1327.1998.2550570.x;
RA   Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.;
RT   "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the
RT   protein disulfide isomerase family but lacks a CXXC thioredoxin-box
RT   motif.";
RL   Eur. J. Biochem. 255:570-579(1998).
CC   -!- FUNCTION: Does not seem to be a disulfide isomerase. Plays an important
CC       role in the processing of secretory proteins within the ER (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Part of a large chaperone multiprotein complex
CC       comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB,
CC       SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low
CC       levels, CALR nor CANX (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome
CC       {ECO:0000250}.
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DR   EMBL; BC118440; AAI18441.1; -; mRNA.
DR   RefSeq; NP_001069739.1; NM_001076271.1.
DR   AlphaFoldDB; P81623; -.
DR   SMR; P81623; -.
DR   STRING; 9913.ENSBTAP00000008754; -.
DR   PaxDb; 9913-ENSBTAP00000008754; -.
DR   PeptideAtlas; P81623; -.
DR   Ensembl; ENSBTAT00000008754.4; ENSBTAP00000008754.3; ENSBTAG00000006665.4.
DR   GeneID; 613357; -.
DR   KEGG; bta:613357; -.
DR   CTD; 10961; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006665; -.
DR   VGNC; VGNC:28596; ERP29.
DR   eggNOG; ENOG502QSHC; Eukaryota.
DR   GeneTree; ENSGT00390000018566; -.
DR   HOGENOM; CLU_061309_1_0_1; -.
DR   InParanoid; P81623; -.
DR   OMA; HISANEM; -.
DR   OrthoDB; 5403558at2759; -.
DR   TreeFam; TF324701; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000006665; Expressed in corpus epididymis and 109 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   CDD; cd00238; ERp29c; 1.
DR   CDD; cd03007; PDI_a_ERp29_N; 1.
DR   Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR016855; ERp29.
DR   InterPro; IPR011679; ERp29_C.
DR   InterPro; IPR036356; ERp29_C_sf.
DR   InterPro; IPR012883; ERp29_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12211; ENDOPLASMIC RETICULUM PROTEIN ERP29; 1.
DR   PANTHER; PTHR12211:SF0; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 29; 1.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF07912; ERp29_N; 1.
DR   PIRSF; PIRSF027352; ER_p29; 1.
DR   SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein;
KW   Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:9738895"
FT   CHAIN           30..258
FT                   /note="Endoplasmic reticulum resident protein 29"
FT                   /id="PRO_0000087030"
FT   MOTIF           255..258
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   MOD_RES         61
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000250|UniProtKB:P30040"
FT   MOD_RES         63
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000250|UniProtKB:P30040"
FT   CONFLICT        41
FT                   /note="I -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="D -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  28806 MW;  32A15711043ECDC4 CRC64;
     MAAAIPRAAS LSPLFPLLFL LSAPQDSSGL HTKGALPLDT ITFYKVIPKS KFVLVKFDTQ
     YPYGEKQDEF KRLAENSASS DDLLVAEVGI SDYGDKLNME LSEKYKLDKE NYPIFYLFQD
     GDFENPVLYS GAVKVGAIQR WLKGHGIYLG MPGCLPAYDT LAGEFIRASG VEARQSLLKQ
     GQDNLASVKE TDKKWAEQYL KIMGKILDQG EDFPASEMTR ITKLIEKNKM SDGKKEELQK
     SLNILTAFQK KGGEKEEL
//