ID   A0A3B3RHG6_9TELE        Unreviewed;       465 AA.
AC   A0A3B3RHG6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018057.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000018057.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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DR   AlphaFoldDB; A0A3B3RHG6; -.
DR   Ensembl; ENSPKIT00000042584.1; ENSPKIP00000018057.1; ENSPKIG00000003761.1.
DR   GeneTree; ENSGT00930000151022; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03000; PDI_a_TMX3; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..465
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017415042"
FT   DOMAIN          4..119
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          400..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..415
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..456
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  53110 MW;  8D62E91A30D9851D CRC64;
     MLTALLLSLS TAFAHVEDLD DTFKDNRADD IWLVKFYAPW CGYCRKLEPV WHEIGAELKS
     SGSSINVGKM DATAYSSVAS EFGVRGYPTI KLLKGDLAYN YKGPRTKDDI IEFANRVAGP
     VVRSLPSRQM FEHILDRHGV VFVYIGGEST LKEKYIEVAS ELIVYTYFFS ALEDAVPPTV
     TLQELPSVSV FKDGTYFLYD AYQHGELSSW VNKERFRGYL DIDAFTLYEL AETGKLVAIA
     VVDEKVPTEE GARIKMLMQR VATEYRDQFS RDFQFGHMDG NDYINGLIMS EVPVPSIIVL
     NTSNDQYFLP LEQVESHEQM VEFINSVLDG TAQAQGGDSI FQRVKRVFYD ARSTVMSVFR
     SSPLLGCFLF GLPLGIISLM CYGICTAEAD DDSEDLDLLR REEEEEEEEE QRQRAEQQEE
     EEQRLRVEEE EQRQRVEGGE DDKEEEDEEE EEEEEEKSAM DKKVD
//