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}.
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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
//