ID   Q658S9_HUMAN            Unreviewed;       392 AA.
AC   Q658S9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
DE   Flags: Fragment;
GN   Name=DKFZp666I134 {ECO:0000313|EMBL:CAH56286.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAH56286.1};
RN   [1] {ECO:0000313|EMBL:CAH56286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Stomach {ECO:0000313|EMBL:CAH56286.1};
RG   The German cDNA Consortium;
RA   Ansorge W., Krieger S., Regiert T., Rittmueller C., Schwager B.,
RA   Mewes H.W., Weil B., Amid C., Osanger A., Fobo G., Han M., Wiemann S.;
RL   Submitted (SEP-2004) 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; Evidence={ECO:0000256|ARBA:ARBA00001182};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; AL833008; CAH56286.1; -; mRNA.
DR   AlphaFoldDB; Q658S9; -.
DR   SMR; Q658S9; -.
DR   IntAct; Q658S9; 1.
DR   PeptideAtlas; Q658S9; -.
DR   PharmGKB; PA134992492; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR   CDD; cd03005; PDI_a_ERp46; 3.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 1.
DR   PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR   PANTHER; PTHR45672:SF3; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   2: Evidence at transcript level;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..129
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          130..255
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          264..389
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAH56286.1"
SQ   SEQUENCE   392 AA;  43505 MW;  05F3B811E9C91B0F CRC64;
     AAAAAADGPP AADGEDGQDP HSKHLYTADM FTHGIQSAAH FVMFFAPWCG HCQRLQPTWN
     DLGDKYNSME DAKVYVAKVD CTAHSDVCSA QGVRGYPTLK LFKPGQEAVK YQGPRDFQTL
     ENWMLQTLNE EPVTPEPEVE PPSAPELKQG LYELSASNFE LHVAQGDHFI KFFAPWCGHC
     KALAPTWEQL ALGLEHSETV KIGKVDCTQH YELCSGNQVR GYPTLLWFRD GKKVDQYKGK
     RDLESLREYV ESQLQRTETG ATETVTPSEA PVLAAEPEAD KGTVLALTEN NFDDTIAEGI
     TFIKFYAPWC GHCKTLAPTW EELSKKEFPG LAGVKIAEVD CTAERNICSK YSVRGYPTLL
     LFRGGKKVSE HSGGRDLDSL HRFVLSQAKD EL
//