PDIA5_MOUSE
ID PDIA5_MOUSE Reviewed; 517 AA.
AC Q921X9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein disulfide-isomerase A5;
DE EC=5.3.4.1;
DE AltName: Full=Protein disulfide isomerase-related protein;
DE Flags: Precursor;
GN Name=Pdia5; Synonyms=Pdir;
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=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Interacts with CALR (via P-domain).
CC {ECO:0000250|UniProtKB:Q14554}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; BC009151; AAH09151.1; -; mRNA.
DR CCDS; CCDS37323.1; -.
DR RefSeq; NP_082571.1; NM_028295.1.
DR AlphaFoldDB; Q921X9; -.
DR SMR; Q921X9; -.
DR BioGRID; 215462; 5.
DR STRING; 10090.ENSMUSP00000023550; -.
DR iPTMnet; Q921X9; -.
DR PhosphoSitePlus; Q921X9; -.
DR SwissPalm; Q921X9; -.
DR EPD; Q921X9; -.
DR jPOST; Q921X9; -.
DR MaxQB; Q921X9; -.
DR PaxDb; Q921X9; -.
DR PeptideAtlas; Q921X9; -.
DR PRIDE; Q921X9; -.
DR ProteomicsDB; 294049; -.
DR Antibodypedia; 32940; 192 antibodies from 27 providers.
DR DNASU; 72599; -.
DR Ensembl; ENSMUST00000023550; ENSMUSP00000023550; ENSMUSG00000022844.
DR GeneID; 72599; -.
DR KEGG; mmu:72599; -.
DR UCSC; uc007zbl.1; mouse.
DR CTD; 10954; -.
DR MGI; MGI:1919849; Pdia5.
DR VEuPathDB; HostDB:ENSMUSG00000022844; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000156797; -.
DR HOGENOM; CLU_021181_1_0_1; -.
DR InParanoid; Q921X9; -.
DR OMA; RMKPEYE; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q921X9; -.
DR TreeFam; TF106379; -.
DR BioGRID-ORCS; 72599; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Pdia5; mouse.
DR PRO; PR:Q921X9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q921X9; protein.
DR Bgee; ENSMUSG00000022844; Expressed in placenta labyrinth and 220 other tissues.
DR Genevisible; Q921X9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR CDD; cd02997; PDI_a_PDIR; 3.
DR CDD; cd03067; PDI_b_PDIR_N; 1.
DR InterPro; IPR046374; PDI_a_PDIR.
DR InterPro; IPR041865; PDI_b_PDIR_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR SUPFAM; SSF52833; SSF52833; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..517
FT /note="Protein disulfide-isomerase A5"
FT /id="PRO_0000034234"
FT DOMAIN 132..259
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 268..382
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 376..504
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 514..517
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 83..92
FT /evidence="ECO:0000250|UniProtKB:Q14554"
FT DISULFID 180..183
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 303..306
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 424..427
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 517 AA; 59267 MW; 6702B9C5EF9F1C84 CRC64;
MARAWGLLLA IGVVLPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL YSESEVAAES
HLKLLSTVAQ AVKGQGTVCW VDCGDAESRK LCKKMKVDLS PKDKKIELFH YQDGAFHMQY
DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD VVHIDSEKDF RRLLKREEKP LLMMFYAPWC
SMCKRIMPHF QKAATQVRGH IVLAGMNVYP SEFENIKEEY NVRGYPTICY FEKGRFLFPY
ENYGSTAEDI VEWLKNPLPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA
PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATVNEA LAGRFHISAF PTLKYFKNGE
QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL VGDNFRDTLK KKKHTLVMFY
APWCPHCKKV IPHFTATADA FKEDRKIACA AVDCVKDKNQ DLCQQEAVKA YPTFHYYHYG
KLVEKYESDR TELGFTSFIR TLREGDLKRL EKRREEL
