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Database: UniProt
Entry: A0A384B8P6_BALAS
LinkDB: A0A384B8P6_BALAS
Original site: A0A384B8P6_BALAS 
ID   A0A384B8P6_BALAS        Unreviewed;       505 AA.
AC   A0A384B8P6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|RuleBase:RU361130};
GN   Name=PDIA3 {ECO:0000313|RefSeq:XP_007196050.1};
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_007196050.1};
RN   [1] {ECO:0000313|RefSeq:XP_007196050.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007196050.1};
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         ECO:0000256|RuleBase:RU361130};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}.
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_007196050.1; XM_007195988.2.
DR   AlphaFoldDB; A0A384B8P6; -.
DR   STRING; 310752.A0A384B8P6; -.
DR   GeneID; 103002005; -.
DR   KEGG; bacu:103002005; -.
DR   CTD; 2923; -.
DR   InParanoid; A0A384B8P6; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; 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; cd03073; PDI_b'_ERp72_ERp57; 1.
DR   CDD; cd03069; PDI_b_ERp57; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR041868; PDIA3_PDI_b.
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; 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, ECO:0000256|RuleBase:RU361130};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT   CHAIN           25..505
FT                   /note="Protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5016478532"
FT   DOMAIN          19..133
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          343..485
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          486..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        57..60
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        406..409
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   505 AA;  56906 MW;  D77CB59EA8CC66D7 CRC64;
     MRLRRLALFP GLALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV EFFAPWCGHC
     KKLAPEYEAA AARLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT
     ADGIVSHLKK QAGPASVPLR TEEEFEKFIS DKDASVVGFF KDLFSDTHSE FLKAASNLRD
     NYRFAHTNVE SLVNKYDDDG EGITLFRPSH LMNKFEDRTV AYTEQKMTSG KIKKFIQENI
     FGICPHMTED NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGKKLNFA
     VASRKTFSHE LSDFGLESTT GEIAVVAIRT AKGEKFVMQE EFSRDGKALE RFLQDYFDGN
     LKRYLKSEPI PESNDGPVKV VVAENFDEIV NDENKDVLIE FYAPWCGHCK NLEPKYKELG
     EKLRKDPNII IAKMDATAND VPSPYEVRGF PTIYFSPANK KLNPKKYEGG RELSDFISYL
     KREATNPPVI QEEKPKKKKK AQEDL
//
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