ID   PDIA6_CAEEL             Reviewed;         440 AA.
AC   Q11067;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Probable protein disulfide-isomerase A6;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=tag-320; ORFNames=B0403.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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 2 thioredoxin domains.
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DR   EMBL; U40411; AAC47065.1; -; Genomic_DNA.
DR   PIR; T15352; T15352.
DR   RefSeq; NP_509190.1; -.
DR   UniGene; Cel.6685; -.
DR   HSSP; P07237; 1MEK.
DR   Ensembl; B0403.4; Caenorhabditis elegans.
DR   GeneID; 180974; -.
DR   KEGG; cel:B0403.4; -.
DR   NMPDR; fig|6239.3.peg.23679; -.
DR   WormBase; WBGene00015168; tag-320.
DR   WormPep; B0403.4; CE03880.
DR   OMA; Q11067; LEPEWAA.
DR   BRENDA; 5.3.4.1; 672.
DR   NextBio; 911804; -.
DR   ArrayExpress; Q11067; -.
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   GO; GO:0040007; P:growth; IMP:WormBase.
DR   GO; GO:0040011; P:locomotion; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   InterPro; IPR005788; Disulphide_isomerase.
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; 2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW   Redox-active center; Repeat; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    440       Probable protein disulfide-isomerase A6.
FT                                /FTId=PRO_0000034241.
FT   DOMAIN       19    131       Thioredoxin 1.
FT   DOMAIN      127    273       Thioredoxin 2.
FT   MOTIF       437    440       Prevents secretion from ER (By
FT                                similarity).
FT   COMPBIAS    142    152       Poly-Ser.
FT   COMPBIAS    158    163       Poly-Gly.
FT   COMPBIAS    425    436       Asp/Glu-rich (acidic).
FT   ACT_SITE     54     54       Nucleophile (By similarity).
FT   ACT_SITE     57     57       Nucleophile (By similarity).
FT   ACT_SITE    194    194       Nucleophile (By similarity).
FT   ACT_SITE    197    197       Nucleophile (By similarity).
FT   SITE         55     55       Contributes to redox potential value (By
FT                                similarity).
FT   SITE         56     56       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        117    117       Lowers pKa of C-terminal Cys of first
FT                                active site (By similarity).
FT   SITE        195    195       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        196    196       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        259    259       Lowers pKa of C-terminal Cys of second
FT                                active site (By similarity).
FT   DISULFID     54     57       Redox-active (By similarity).
FT   DISULFID    194    197       Redox-active (By similarity).
SQ   SEQUENCE   440 AA;  47728 MW;  608785076B159578 CRC64;
     MALIKLLLAS LAITSVCGMY SKKDDVVELT EANFQSKVIN SDDIWIVEFY APWCGHCKSL
     VPEYKKAASA LKGVAKVGAV DMTQHQSVGG PYNVQGFPTL KIFGADKKKP TDYNGQRTAQ
     AIADSVLAEA KKAVSARLGG KSSGSSSSGS GSGSGKRGGG GSGNEVVELT DANFEDLVLN
     SKDIWLVEFF APWCGHCKSL EPQWKAAASE LKGKVRLGAL DATVHTVVAN KFAIRGFPTI
     KYFAPGSDVS DAQDYDGGRQ SSDIVAWASA RAQENMPAPE VFEGINQQVV EDACKEKQLC
     IFAFLPHILD CQSECRNNYL AMLKEQSEKF KKNLWGWIWV EGAAQPALEE SFEVGGFGYP
     AMTALNFRKN KYAVLKGSFG KDGIHEFLRD LSYGKGRTSS LRGDGFPKIQ KTEKWDGKDG
     ALPAEDDIDL SDIDLDKTEL
//