ID   PDIA4_BOVIN             Reviewed;         643 AA.
AC   Q29RV1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Protein disulfide-isomerase A4;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=PDIA4;
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 (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBUNIT: Part a large chaperone multiprotein complex comprising
CC       CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1,
CC       UGT1A1 and very small amounts of ERP29, but not, or at very low
CC       levels, CALR nor CANX.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC       Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 3 thioredoxin domains.
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DR   EMBL; BC114004; AAI14005.1; -; mRNA.
DR   IPI; IPI00706136; -.
DR   RefSeq; NP_001039344.1; -.
DR   UniGene; Bt.23128; -.
DR   SMR; Q29RV1; 55-178, 177-283, 521-643.
DR   Ensembl; ENSBTAG00000017143; Bos taurus.
DR   GeneID; 415110; -.
DR   KEGG; bta:415110; -.
DR   HOVERGEN; Q29RV1; -.
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:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017068; Protein_diS-isomerase_A4.
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   PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
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     20       Potential.
FT   CHAIN        21    643       Protein disulfide-isomerase A4.
FT                                /FTId=PRO_0000240338.
FT   DOMAIN       21    168       Thioredoxin 1.
FT   DOMAIN      170    300       Thioredoxin 2.
FT   DOMAIN      503    634       Thioredoxin 3.
FT   MOTIF       640    643       Prevents secretion from ER (By
FT                                similarity).
FT   COMPBIAS     39     54       Asp/Glu-rich (acidic).
FT   DISULFID     90     93       Redox-active (By similarity).
FT   DISULFID    205    208       Redox-active (By similarity).
FT   DISULFID    553    556       Redox-active (By similarity).
SQ   SEQUENCE   643 AA;  72526 MW;  EFBBB755DE97A35E CRC64;
     MRPRKAWMLV LLLALVQLLA VASAGAPDED STDKEDAIEE DEEEDEDDDD DDDDLEVKEE
     NGVLILNDAN FDNFVADKDT VLLEFYAPWC GHCKQFAPEY EKIAATLKEN DPPIPVAKID
     ATSESALASR FDVSGYPTIK ILKKGQEVDY EGSRTQEEIV AKVKEVSQPN WTPPPEVTLV
     LTKDNFDEVV NDADIILVEF YAPWCGHCKK LAPEYEKAAK ELSKSSPPIP LAKVDAIAET
     DLAKRFDVSS YPTLKIFRKG KAFSYNGPRE KYGIVDYMME QSGPPSKQIL ALKQVQEFLK
     DGDDVIIIGV FKSESDPAYQ LYQDAANSLR EDYKFHHTFS TEIAKFLKVS LGKLVVMQPE
     KFQSKYEPKS YVMDIKDSTE AAAITEHVVK HTLPLVGHRK AADAKRYTRR PLVVVYYSVD
     FSFDYRAATQ FWRNKVLEVA KDFPEYTFAV ADEEDFATEL KDLGLSESGE EVNAAILDEG
     GRRFAMEPDD FDADALRDFV TAFKKGKLKP VIKSQPVPKN NKGPVKVVVG KTFDSIVMDP
     KKDVLIEFYA PWCGHCKQLE PVYTSLGKKY KGHKNLVIAK MDATANDVTS DRYKVEGFPT
     IYFAPSGDKK KPIKFEDGNR DLEHLSKFIE EHATKLSRTK EEL
//