ID   A0A3P9D2L0_9CICH        Unreviewed;       639 AA.
AC   A0A3P9D2L0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Protein disulfide-isomerase A4 {ECO:0000256|PIRNR:PIRNR036862};
DE            EC=5.3.4.1 {ECO:0000256|PIRNR:PIRNR036862};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005028447.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005028447.1}
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_004546616.1; XM_004546559.3.
DR   AlphaFoldDB; A0A3P9D2L0; -.
DR   STRING; 106582.ENSMZEP00005028447; -.
DR   Ensembl; ENSMZET00005029351.1; ENSMZEP00005028447.1; ENSMZEG00005021209.1.
DR   GeneID; 101473977; -.
DR   KEGG; mze:101473977; -.
DR   CTD; 9601; -.
DR   GeneTree; ENSGT00940000157738; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000265160; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   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..639
FT                   /note="Protein disulfide-isomerase A4"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5017845068"
FT   DOMAIN          41..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          163..278
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          499..630
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          23..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        200..203
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        549..552
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   639 AA;  71741 MW;  3771FAB1268D3CB4 CRC64;
     MKKLALLLIV LLGVAHFATV SRCEEDVEES KEETDEEDSD DEEDDEDDDT EVKEENGVLV
     LTDNNFDTFI EGKDTVLVEF YAPWCGHCKQ FAPEYEKIAQ TLKENDPPIP VAKVDATVAS
     GLGSRFDVSG YPTIKILKNG EPVDYDGERT EKAIVERVKE VAQPDWKPPP EATLVLTKDN
     FDDTVNNADI ILVEFYAPWC GHCKRLAPEY EKAAKELSQR TPPIPLAKVD ATVESELASR
     FGVTGYPTLK IFRKGKVFEY NGPREKNGIV DYMSEQAGPP SKQVQAAKQI QELIKDGDDA
     VIVGVFSSEQ DAAYDIYVEA CNSLREDFTF RHSFSAEVAK LLKVSPGHVV IVQPEKFRSK
     HEPSSRTFSV KDSTVVSDVQ EFFKKHVIPL VGHRKPSNDA KRYTKRPLVV VYYGVDFSFD
     YRKATQFWRG KVLDVAKDFP EYTFAIADEE DYAEELKGLG LSESGEEVNV GILADGGKKY
     AMEPEEFDSE VLRDFVVAFK KGKLKPIIKS QPVPKNNKGP VKVVVGKTFD DIVMDTQKDV
     LIEFYAPWCG HCKKLEPDYL ALGKKYKGEK NLVIAKMDAT ANDVPSDSYK VEGFPTIYFA
     PSNKKQSPIK FEGGDRTVEG FSKFLEEHAT KLSQKRDEL
//