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   03-AUG-2022, entry version 105.
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}.
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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; Q2KIL5; -.
DR   PRIDE; Q2KIL5; -.
DR   Ensembl; ENSBTAT00000025128; ENSBTAP00000025128; ENSBTAG00000018877.
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; 522268at2759; -.
DR   TreeFam; TF106379; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000018877; Expressed in spermatocyte and 106 other 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:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
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   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; 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