ID   PDIA5_RAT               Reviewed;         517 AA.
AC   Q5I0H9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Protein disulfide-isomerase A5;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=Pdia5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC088305; AAH88305.1; -; mRNA.
DR   RefSeq; NP_001014147.1; NM_001014125.1.
DR   AlphaFoldDB; Q5I0H9; -.
DR   SMR; Q5I0H9; -.
DR   STRING; 10116.ENSRNOP00000059945; -.
DR   PhosphoSitePlus; Q5I0H9; -.
DR   jPOST; Q5I0H9; -.
DR   PaxDb; 10116-ENSRNOP00000059945; -.
DR   Ensembl; ENSRNOT00000067984.2; ENSRNOP00000059945.3; ENSRNOG00000032327.5.
DR   Ensembl; ENSRNOT00055029595; ENSRNOP00055023760; ENSRNOG00055017496.
DR   Ensembl; ENSRNOT00060029567; ENSRNOP00060023786; ENSRNOG00060017315.
DR   Ensembl; ENSRNOT00065031958; ENSRNOP00065025509; ENSRNOG00065019006.
DR   GeneID; 360722; -.
DR   KEGG; rno:360722; -.
DR   UCSC; RGD:1359236; rat.
DR   AGR; RGD:1359236; -.
DR   CTD; 10954; -.
DR   RGD; 1359236; Pdia5.
DR   eggNOG; KOG0191; Eukaryota.
DR   GeneTree; ENSGT00940000156797; -.
DR   HOGENOM; CLU_021181_1_0_1; -.
DR   InParanoid; Q5I0H9; -.
DR   OMA; RMKPEYE; -.
DR   OrthoDB; 52245at2759; -.
DR   PhylomeDB; Q5I0H9; -.
DR   TreeFam; TF106379; -.
DR   PRO; PR:Q5I0H9; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000032327; Expressed in liver and 18 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:RGD.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; ISO:RGD.
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; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
DR   Genevisible; Q5I0H9; RN.
PE   2: Evidence at transcript 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_0000034235"
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"
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;  59399 MW;  038F0B07E1C15A0A CRC64;
     MARAWGLLLA IGVILPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL YSESEVAAES
     HLKLLSTVAQ AVKGQGTICW VDCGDAESRK LCKKMKVDLS PKDKKIELFH YQDGAFHMQY
     DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD VVHIDSEKDF RRLLKKEEKP LLMMFYAPWC
     SMCKRIMPHF QKAATQVRGH TVLAGMNVYP PEFENIKEEY NVRGYPTICY FEKGRFLFQY
     ENYGSTAEDI VEWLKNPQPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA
     PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATINEA LAERFHISAF PTLKYFKNGE
     QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL VGDNFRETLK KKKHTLVMFY
     APWCPHCKKV IPHFTATADA FKDDRKIACA AVDCVKDKNQ DLCQQESVKA YPTFHYYHYG
     KLVEKYESDR TELGFTSFIR TLREGDLKRL EKRREDL
//