ID PDIA5_BOVIN Reviewed; 521 AA. AC Q2KIL5; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 24-JAN-2024, entry version 110. DE RecName: Full=Protein disulfide-isomerase A5; DE EC=5.3.4.1; DE Flags: Precursor; GN Name=PDIA5; 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=Testis; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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: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; BC112593; AAI12594.1; -; mRNA. DR RefSeq; NP_001039556.1; NM_001046091.2. DR AlphaFoldDB; Q2KIL5; -. DR SMR; Q2KIL5; -. DR STRING; 9913.ENSBTAP00000025128; -. DR PaxDb; 9913-ENSBTAP00000025128; -. DR Ensembl; ENSBTAT00000025128.4; ENSBTAP00000025128.3; ENSBTAG00000018877.4. DR GeneID; 511603; -. DR KEGG; bta:511603; -. DR CTD; 10954; -. DR VEuPathDB; HostDB:ENSBTAG00000018877; -. DR VGNC; VGNC:32699; PDIA5. DR eggNOG; KOG0191; Eukaryota. DR GeneTree; ENSGT00940000156797; -. DR HOGENOM; CLU_021181_1_0_1; -. DR InParanoid; Q2KIL5; -. DR OMA; RMKPEYE; -. DR OrthoDB; 52245at2759; -. DR TreeFam; TF106379; -. DR Proteomes; UP000009136; Chromosome 1. DR Bgee; ENSBTAG00000018877; Expressed in spermatocyte and 106 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; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. 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; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 3. PE 2: Evidence at transcript level; KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..521 FT /note="Protein disulfide-isomerase A5" FT /id="PRO_0000244882" FT DOMAIN 136..263 FT /note="Thioredoxin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DOMAIN 274..386 FT /note="Thioredoxin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DOMAIN 387..508 FT /note="Thioredoxin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT MOTIF 518..521 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT DISULFID 184..187 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DISULFID 307..310 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DISULFID 428..431 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" SQ SEQUENCE 521 AA; 59673 MW; A05A85EB4EEA2BEA CRC64; MARVVPAWLL LPLAVWVVLP TWLSSAKFSS LIERISDPKD LKKLLRTRNN VLVLYSKSEA AAESHLKLLS TVAQAVKGQG TICWVDCGDA ESRKLCKKMK VDLSAKDKKV ELFHYQDGAF HTEYNRAVTF KSIVAFLKDP KGPPLWEEDP GAKDVVHIDN EKDFRRLLKK EEKPILMMFY APWCSVCKRI MPHFQKAATQ LRGQFVLAGM NVYPSEFENI KEEYSVRGYP TICYFEKGRF LFQYDSYGST AEDIVEWLKN PQPPQPQVPE TPWADEGGSV YHLSDEDFDQ FVKEHSSVLV MFHAPWCGHC KKMKPEFESA AEVLHGEGDS SGVLAAVDAT VNKALAERFH IAEFPTLKYF KNGEKYAVPA LRTKKSFIEW MRNPESPPPP DPAWEEQQTS VLHLSGDNFR ETLKRKKHAL VMFYAPWCPH CKKAIPHFTA AADAFKDDRK IACAAIDCVK ENNKDLCQQE AVKAYPTFHY YHYGKFVEKY DTNPTELGFT SFIRTLREGD HERLGKKKEE L //