PDIA5_HUMAN
ID PDIA5_HUMAN Reviewed; 519 AA.
AC Q14554; D3DN95; Q9BV43;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7556671; DOI=10.1016/0014-5793(95)00996-m;
RA Hayano T., Kikuchi M.;
RT "Molecular cloning of the cDNA encoding a novel protein disulfide
RT isomerase-related protein (PDIR).";
RL FEBS Lett. 372:210-214(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-150, DISULFIDE BOND, AND
RP INTERACTION WITH CALR.
RX PubMed=23614004; DOI=10.1371/journal.pone.0062021;
RA Vinaik R., Kozlov G., Gehring K.;
RT "Structure of the non-catalytic domain of the protein disulfide isomerase-
RT related protein (PDIR) reveals function in protein binding.";
RL PLoS ONE 8:E62021-E62021(2013).
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:0000269|PubMed:23614004}.
CC -!- INTERACTION:
CC Q14554; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-953879, EBI-10172290;
CC Q14554; Q99750: MDFI; NbExp=3; IntAct=EBI-953879, EBI-724076;
CC Q14554-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-12094562, EBI-11749135;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14554-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14554-2; Sequence=VSP_056536, VSP_056537;
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; D49490; BAA08451.1; -; mRNA.
DR EMBL; AC063922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79452.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79453.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79454.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79456.1; -; Genomic_DNA.
DR EMBL; BC001625; AAH01625.1; -; mRNA.
DR CCDS; CCDS3020.1; -. [Q14554-1]
DR PIR; S66673; S66673.
DR RefSeq; NP_006801.1; NM_006810.3. [Q14554-1]
DR PDB; 4I6X; X-ray; 1.50 A; A=29-150.
DR PDBsum; 4I6X; -.
DR AlphaFoldDB; Q14554; -.
DR SMR; Q14554; -.
DR BioGRID; 116154; 128.
DR IntAct; Q14554; 31.
DR STRING; 9606.ENSP00000323313; -.
DR GlyGen; Q14554; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q14554; -.
DR PhosphoSitePlus; Q14554; -.
DR SwissPalm; Q14554; -.
DR BioMuta; PDIA5; -.
DR DMDM; 2501208; -.
DR EPD; Q14554; -.
DR jPOST; Q14554; -.
DR MassIVE; Q14554; -.
DR MaxQB; Q14554; -.
DR PaxDb; Q14554; -.
DR PeptideAtlas; Q14554; -.
DR PRIDE; Q14554; -.
DR ProteomicsDB; 60041; -. [Q14554-1]
DR ProteomicsDB; 79167; -.
DR Antibodypedia; 32940; 192 antibodies from 27 providers.
DR DNASU; 10954; -.
DR Ensembl; ENST00000316218.12; ENSP00000323313.7; ENSG00000065485.20. [Q14554-1]
DR Ensembl; ENST00000489923.5; ENSP00000417520.1; ENSG00000065485.20. [Q14554-2]
DR GeneID; 10954; -.
DR KEGG; hsa:10954; -.
DR MANE-Select; ENST00000316218.12; ENSP00000323313.7; NM_006810.4; NP_006801.1.
DR UCSC; uc003egc.3; human. [Q14554-1]
DR CTD; 10954; -.
DR DisGeNET; 10954; -.
DR GeneCards; PDIA5; -.
DR HGNC; HGNC:24811; PDIA5.
DR HPA; ENSG00000065485; Tissue enhanced (liver).
DR neXtProt; NX_Q14554; -.
DR OpenTargets; ENSG00000065485; -.
DR PharmGKB; PA142671191; -.
DR VEuPathDB; HostDB:ENSG00000065485; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000156797; -.
DR HOGENOM; CLU_1061567_0_0_1; -.
DR InParanoid; Q14554; -.
DR OMA; RMKPEYE; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q14554; -.
DR TreeFam; TF106379; -.
DR PathwayCommons; Q14554; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q14554; -.
DR BioGRID-ORCS; 10954; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; PDIA5; human.
DR GenomeRNAi; 10954; -.
DR Pharos; Q14554; Tbio.
DR PRO; PR:Q14554; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14554; protein.
DR Bgee; ENSG00000065485; Expressed in liver and 182 other tissues.
DR ExpressionAtlas; Q14554; baseline and differential.
DR Genevisible; Q14554; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:FlyBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; TAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
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 3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..519
FT /note="Protein disulfide-isomerase A5"
FT /id="PRO_0000034233"
FT DOMAIN 134..261
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 270..384
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 378..506
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 516..519
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 85..94
FT /evidence="ECO:0000269|PubMed:23614004,
FT ECO:0007744|PDB:4I6X"
FT DISULFID 182..185
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 305..308
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 426..429
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 258..261
FT /note="NPQP -> KVWP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056536"
FT VAR_SEQ 262..518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056537"
FT VARIANT 391
FT /note="T -> M (in dbSNP:rs2292661)"
FT /id="VAR_052581"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:4I6X"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:4I6X"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:4I6X"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:4I6X"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4I6X"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:4I6X"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:4I6X"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4I6X"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4I6X"
SQ SEQUENCE 519 AA; 59594 MW; 6083FBEB8C019658 CRC64;
MARAGPAWLL LAIWVVLPSW LSSAKVSSLI ERISDPKDLK KLLRTRNNVL VLYSKSEVAA
ENHLRLLSTV AQAVKGQGTI CWVDCGDAES RKLCKKMKVD LSPKDKKVEL FHYQDGAFHT
EYNRAVTFKS IVAFLKDPKG PPLWEEDPGA KDVVHLDSEK DFRRLLKKEE KPLLIMFYAP
WCSMCKRMMP HFQKAATQLR GHAVLAGMNV YSSEFENIKE EYSVRGFPTI CYFEKGRFLF
QYDNYGSTAE DIVEWLKNPQ PPQPQVPETP WADEGGSVYH LTDEDFDQFV KEHSSVLVMF
HAPWCGHCKK MKPEFEKAAE ALHGEADSSG VLAAVDATVN KALAERFHIS EFPTLKYFKN
GEKYAVPVLR TKKKFLEWMQ NPEAPPPPEP TWEEQQTSVL HLVGDNFRET LKKKKHTLVM
FYAPWCPHCK KVIPHFTATA DAFKDDRKIA CAAVDCVKDK NQDLCQQEAV KGYPTFHYYH
YGKFAEKYDS DRTELGFTNY IRALREGDHE RLGKKKEEL
