ID A0A384A3E7_BALAS Unreviewed; 459 AA.
AC A0A384A3E7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 21.
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|RefSeq:XP_007181872.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007181872.1};
RN [1] {ECO:0000313|RefSeq:XP_007181872.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007181872.1};
RG RefSeq;
RL Submitted (JAN-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_007181872.1; XM_007181810.1.
DR AlphaFoldDB; A0A384A3E7; -.
DR GeneID; 103006492; -.
DR CTD; 64714; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000261681; 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; 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; 3.
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; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..459
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017045484"
FT DOMAIN 301..431
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 50996 MW; 10AC411AD841C8D4 CRC64;
MDGQLLPVLL LLLGASGLWG RGPGPEGALE EPPEEEPPEE EPPEEDGILV LSRQTLGLAL
REHPALLVEF CPWEAEGIAE WLRRRVGPRA TGLEDEEGAR ALIDARDVVV IGFFQDLQDK
DVATFLALAQ DALDVSFGLT NQPQLFQKFG LTKDTVVLFK KYDEGRADFP VDEELGLDQG
DLSRFLLTHS MHLVTEFNSQ TSRKIFAARI LNHLLLFVNQ TLAPHRELLA GFREAAPGFL
GQVLFVVVDV GANNDHVLQY FGLKAEEAPT LRFINTETTK KYMPADRGPV TATSVAAFCH
AVLGGEVKPY HLSQEVPPDW DQRPVKTLVG KNFEQVAFDE TKNVFIKFYA PWCTHCKEMA
PAWEALAEKY RDHEDIVIAE LDATANELEA LPVHGFPTLK YFPAGPGRKV IEYKGTRDLE
TFSKFLDSGG ELPAEEPTEV PGAPFPEMPE NTTEPKDEL
//
