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   16-JUN-2009, entry version 31.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 3 thioredoxin domains.
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DR   EMBL; BC112593; AAI12594.1; -; mRNA.
DR   IPI; IPI00717336; -.
DR   RefSeq; NP_001039556.1; -.
DR   UniGene; Bt.6804; -.
DR   Ensembl; ENSBTAG00000018877; Bos taurus.
DR   GeneID; 511603; -.
DR   KEGG; bta:511603; -.
DR   HOVERGEN; Q2KIL5; -.
DR   OMA; Q2KIL5; KNPQPPQ.
DR   BRENDA; 5.3.4.1; 251.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR006662; Thioredoxin-like_subdom.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 3.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   PRINTS; PR00421; THIOREDOXIN.
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   Repeat; Signal.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    521       Protein disulfide-isomerase A5.
FT                                /FTId=PRO_0000244882.
FT   DOMAIN      136    263       Thioredoxin 1.
FT   DOMAIN      274    386       Thioredoxin 2.
FT   DOMAIN      387    508       Thioredoxin 3.
FT   MOTIF       518    521       Prevents secretion from ER (Potential).
FT   COMPBIAS    387    392       Poly-Pro.
FT   DISULFID    184    187       Redox-active (By similarity).
FT   DISULFID    307    310       Redox-active (By similarity).
FT   DISULFID    428    431       Redox-active (By similarity).
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
//