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Database: UniProt
Entry: A0A1I8N351_MUSDO
LinkDB: A0A1I8N351_MUSDO
Original site: A0A1I8N351_MUSDO 
ID   A0A1I8N351_MUSDO        Unreviewed;       489 AA.
AC   A0A1I8N351;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN   Name=101895992 {ECO:0000313|EnsemblMetazoa:MDOA011052-PA};
GN   Synonyms=LOC101895992 {ECO:0000313|RefSeq:XP_005176488.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA011052-PA};
RN   [1] {ECO:0000313|EnsemblMetazoa:MDOA011052-PA}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA011052-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005176488.1}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|RefSeq:XP_005176488.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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         ECO:0000256|RuleBase:RU361130};
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   RefSeq; XP_005176488.1; XM_005176431.3.
DR   STRING; 7370.A0A1I8N351; -.
DR   EnsemblMetazoa; MDOA011052-RA; MDOA011052-PA; MDOA011052.
DR   GeneID; 101895992; -.
DR   KEGG; mde:101895992; -.
DR   VEuPathDB; VectorBase:MDOA011052; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT   CHAIN           20..489
FT                   /note="Protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5041474360"
FT   DOMAIN          5..131
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          344..472
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        51..54
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        394..397
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   489 AA;  55237 MW;  8B815311ABA6F6C3 CRC64;
     MHKALLVLCL AGLAYLSNAA ESDVLELTDD NFLSVLSEHS TTLVMFYAPW CGHCKRLKPE
     YAKAAEIVKD DDPPITLAKV DCTEAGKETC NKFSVSGYPT LKIFKGEEVS QDYNGPREAA
     GIAKYMRAQV GPASKEIKSV EELDKFFTAK ETTIFGYFKD VNSKLAKTFL KFADKNREKY
     RFGHSSNEEV LEKATESDAI VLVRAPHLAN KFEESTVKFD GSSESDLTAF VKENYHGLVG
     HRTQDTVRDF KNPLITAYYG VDYVKNPKGT NYWRNRVLKV AKEFAGKLTF AISAKDDFQH
     ELNEYGYDFV GDKPVILARD AKNLKYALKE EFSVENLRDF AEKLLEGELE PYIKSEPIPE
     DNSAPVKVAV AKNFDEVVMN NDKDTLIEFY APWCGHCKKL APVYDELAEK LQDEDVVIAK
     MDATANDVPP EFNVRGFPTL FWLPKDSKNK PVSYNEGREV DDFLKFISKH ATKELKGFDR
     SGKPKKTEL
//
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