ID A0A3B4E4Y9_PYGNA Unreviewed; 641 AA.
AC A0A3B4E4Y9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Protein disulfide-isomerase A4 {ECO:0000256|PIRNR:PIRNR036862};
DE EC=5.3.4.1 {ECO:0000256|PIRNR:PIRNR036862};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000030825.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000030825.1}
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 ECO:0000256|PIRNR:PIRNR036862, ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319, ECO:0000256|PIRNR:PIRNR036862}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|PIRNR:PIRNR036862,
CC ECO:0000256|RuleBase:RU004208}.
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DR RefSeq; XP_017573533.1; XM_017718044.1.
DR AlphaFoldDB; A0A3B4E4Y9; -.
DR STRING; 42514.ENSPNAP00000030825; -.
DR Ensembl; ENSPNAT00000019233.1; ENSPNAP00000030825.1; ENSPNAG00000017785.1.
DR GeneID; 108439576; -.
DR CTD; 9601; -.
DR GeneTree; ENSGT00940000157738; -.
DR OMA; FRSKHEP; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000261440; 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; cd02961; PDI_a_family; 2.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR041866; PDIA4_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
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; 3.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF210; PROTEIN DISULFIDE-ISOMERASE A4; 1.
DR Pfam; PF00085; Thioredoxin; 3.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 5.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR036862};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR036862};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 24..641
FT /note="Protein disulfide-isomerase A4"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5017098787"
FT DOMAIN 33..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 171..296
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 503..633
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 24..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..207
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 552..555
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 641 AA; 72161 MW; 575C5011CB49FCA0 CRC64;
MKKITLLLIV LLGLAHFISL SRCEEDDDVG EKVEEGDDDD DGDDDDDDDD DDSTEVKEEN
GVLVLNDANF DTFMEGKDTV LVEFYAPWCG HCKQFAPEYE KIAQTLKESD PPIPVAKVDA
TKANALASRF EVSGYPTIKI LKTGKPVEYD GDRTEKAIVE RVKEVAKPDW KPPPEATLVL
TKDNFDDVVT NADIILVEFY APWCGHCKRL APEYEKAAKE LSNRTPPIPL AKVDATVEND
IASRFSVTGY PTLKIFRKGK AFEYNGPREK FGIVDYMSEQ AGPPSKQVQA LKQIQELLKD
GDDALIVGVF SSEEDTGYEV YQEACNSLRE DYKFRHTFSS EIAKFLKAKP GQVVVLQPEK
FRSKFEPSSQ AFSIKDSTTA SELQDFFKKH TLPLVGHRKP SNDAKRYTAR PLVVVYYGID
FSFDYRVATQ FWRSKVLEVA KDFPEYTFAI ADEEDYSDEL KSLGLSESGE EVNVGILAEG
GKKYAMEPEE FDSDVLQEFV VAFKKGKLKP IIKSQPIPKN KGPVKVVVGK TFDEIVLDTK
KDVLIEFYAP WCGHCKKLEP DYLALGKKYK NEKNLVIAKM DATANDVPHN SYQVEGFPTI
YFAPSNKKQS PIKFEGGERN VESLSKFIKE HATKLSQKDE L
//
