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 24-JAN-2024, entry version 153. 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, RC and 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000023550; -. DR PeptideAtlas; Q921X9; -. DR ProteomicsDB; 294049; -. DR Pumba; Q921X9; -. DR Antibodypedia; 32940; 205 antibodies from 27 providers. DR DNASU; 72599; -. DR Ensembl; ENSMUST00000023550.9; ENSMUSP00000023550.8; ENSMUSG00000022844.9. DR GeneID; 72599; -. DR KEGG; mmu:72599; -. DR UCSC; uc007zbl.1; mouse. DR AGR; MGI:1919849; -. 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; 52245at2759; -. DR PhylomeDB; Q921X9; -. DR TreeFam; TF106379; -. DR BioGRID-ORCS; 72599; 0 hits in 77 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 224 other cell types or tissues. 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 Gene3D; 3.40.30.10; Glutaredoxin; 4. 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 PANTHER; PTHR45672:SF2; PROTEIN DISULFIDE-ISOMERASE A5; 1. DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1. DR Pfam; PF00085; Thioredoxin; 3. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 4. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 2. DR PROSITE; PS51352; THIOREDOXIN_2; 3. DR Genevisible; Q921X9; MM. 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 //