GenomeNet

Database: UniProt
Entry: A0A2K6H0T2_PROCO
LinkDB: A0A2K6H0T2_PROCO
Original site: A0A2K6H0T2_PROCO 
ID   A0A2K6H0T2_PROCO        Unreviewed;       525 AA.
AC   A0A2K6H0T2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   Name=PDIA2 {ECO:0000313|Ensembl:ENSPCOP00000032131.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000032131.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000032131.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_012515037.1; XM_012659583.1.
DR   AlphaFoldDB; A0A2K6H0T2; -.
DR   STRING; 379532.ENSPCOP00000032131; -.
DR   Ensembl; ENSPCOT00000043092.1; ENSPCOP00000032131.1; ENSPCOG00000028851.1.
DR   GeneID; 105822582; -.
DR   KEGG; pcoq:105822582; -.
DR   CTD; 64714; -.
DR   GeneTree; ENSGT00940000161859; -.
DR   OMA; REDYVWS; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000233160; 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   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR   GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
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   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF93; PROTEIN DISULFIDE-ISOMERASE A2; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
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};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..525
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014386914"
FT   DOMAIN          28..153
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          368..497
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          20..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        72..75
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        419..422
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   525 AA;  57773 MW;  90A19F797DBE9EE1 CRC64;
     MDSQLLPVLL LLGALGPWGQ GQGPEGSSEE LLEEPPEEVP REDGILVLSR HNLGLALREH
     PALLVEFYAP WCAHCKALAP KYHKAATLLA AASIPATLAK VDGPAEPELA EEFGVTEYPT
     LKFFRDGNRT HPEEYTGPRE AEGITEWLRR RVGPSATRLE DEAGVQALVG AHDVVVIGFF
     QDLQDEDVAT FLALAQDALD MTFGLTDQPQ LFQKFDLTND TVVLLKKFDE GRADFPVDKK
     RGLDLVNLSR FLVTHSMHLV TEFNSQTHPK IFAARILNHL LLFVNQTLAP HRELLTGFGE
     AAPPFRGQVL FVVVDVAADN DHVLRYFGLK AEAAPTLRLV NIETAKKYAP VDGEPVTAAS
     VAAFCRAVLT GHVQPYLLSQ EVPPDWDRRP VKTLVSKNFE QVAFDETKNV FVKFYAPWCA
     HCREMAPAWE ALAEKYKDHA DIVIAELDAT ANELEGLAVP GFPTLKYFPA GPGRKVIEYK
     GTRDLETLSK FLDHGGELPT EPTEEPGAPV PESPANSTAG SKEEL
//
DBGET integrated database retrieval system