ID   A0A8C4LTV9_EQUAS        Unreviewed;      1197 AA.
AC   A0A8C4LTV9;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   02-SEP-2026, entry version 23.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|RuleBase:RU361130};
GN   Name=PDIA4 {ECO:0000313|Ensembl:ENSEASP00005012888.2};
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005012888.2, ECO:0000313|Proteomes:UP000694387};
RN   [1] {ECO:0000313|Ensembl:ENSEASP00005012888.2, ECO:0000313|Proteomes:UP000694387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33293529;
RA   Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA   Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA   C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA   J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA   Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA   Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA   S., Zhou, X. and Zhong, J.;
RT   "Donkey genomes provide new insights into domestication and selection for
RT   coat color.";
RL   Nat. Commun. 11:6014-6014(2020).
RN   [2] {ECO:0000313|Ensembl:ENSEASP00005012888.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) 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   -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC       and very small amounts of ERP29, but not, or at very low levels, CALR
CC       nor CANX. Component of a complex containing at least CRELD2, MANF,
CC       MATN3 and PDIA4. {ECO:0000256|ARBA:ARBA00066008}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000256|ARBA:ARBA00006991}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   AlphaFoldDB; A0A8C4LTV9; -.
DR   Ensembl; ENSEAST00005014006.2; ENSEASP00005012888.2; ENSEASG00005009014.2.
DR   GeneTree; ENSGT00940000157738; -.
DR   Proteomes; UP000694387; Chromosome 1.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:TreeGrafter.
DR   CDD; cd07765; KRAB_A-box; 1.
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   FunFam; 3.30.160.60:FF:000065; B-cell CLL/lymphoma 6, member B; 1.
DR   FunFam; 3.40.30.10:FF:000017; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000067; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000076; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000084; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000126; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.30.160.60:FF:000151; Zinc finger and SCAN domain-containing 21; 3.
DR   FunFam; 3.30.160.60:FF:001064; Zinc finger protein 425; 1.
DR   FunFam; 3.30.160.60:FF:000562; Zinc finger protein 786; 2.
DR   FunFam; 3.30.160.60:FF:003276; Zinc finger protein 786; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR041866; PDIA4_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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
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; PF01352; KRAB; 1.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694387};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          9..80
FT                   /note="KRAB"
FT                   /evidence="ECO:0000259|PROSITE:PS50805"
FT   DOMAIN          196..223
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          251..278
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          307..334
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          384..411
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          412..439
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          440..467
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          468..495
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          496..523
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          524..551
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          552..579
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          590..721
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          723..853
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          1057..1188
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          167..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..245
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..610
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        643..646
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00691"
FT   DISULFID        758..761
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU00691"
FT   DISULFID        1107..1110
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   1197 AA;  136199 MW;  E425F73D3629058A CRC64;
     MAEPARLPLT FEDVAIYFSE QEWQKLEAWQ KELYKHVMRT TYDIFVSLDD GIPKPELISW
     IEQGRELFRN WGESQKSGNI ICFSADLHFD PVIERQPFWV SGSQQAVNSG ETQCHFQVDP
     LQSHCSSEPL LGKSEDISFR PDQGITLMNP HRHDTRALIP VVHSVREPTQ RGRIQSPKTL
     GLPGSQEVPS WEAPQHHCPV CGKSFWKKNH LEKHQTSHSK DQPHRAWKKF NGQADPQPQR
     SSPQGRGRRR FRCQECGRSF RLKRYFLRHL ATHAGKSAPQ GPECKVCFCH KRTLLSDHFL
     HKGETAPQCP TCDKSFLLKN SMPAHQGQPS GEGPVSRRVG DKESKLTSVH SGEKPDLRPA
     CGEHCLLKGD GDALQHGPAG EGPHCCTECG QHFPTRSKLA SHIRVHTGEK PFQCLQCDKS
     FQVSSLLQVH LRMHRGERPF SCSQCGRGFT HHCKLRDHLR VHSGERPFQC PECNRSFRLK
     GMLKVHQHTH SQERPFSCGE CGKGFTRQCR LAEHFRLHSG EKPFQCSSCD RSFRLKEQLL
     SHQRLHTGKR PFQCPECDKS YSVKADMKAH QLLHSGEMPF SYSSDKEDAL EEEDEEEDDD
     DEEEEDDLEV KEENGVLVLK DANFDNFVAD KDTVLLEFYA PWCGHCKQFA PEYEKIASTL
     KENDPPIPVA KIDATSESAL ASRFGVSGYP TLKILKKGQA VDYEGSRTQE EIVAKVKEIS
     QPNWTPPPEV TLVLTKDNFD EVVNDADIIL VEFYAPWCGH CKKLAPEYEK AAKELSKRSP
     PIPLAKVDAT AETDLAKRFD VSGYPTLKIF RKGKPFDYNG PREKYGIIDY MIEQSGPPSK
     EIQALKQVQE FLKDGDDVII IGVFKAESDP AYQQYQDAAN NLREDYKFHH TFSTEIAKFL
     KVSPGKLVVM QPEKFQSKYE PRSNVLDIQG STEGSAIKDH VLKHSLPLVG HRKTSNDAKR
     YTRRPLVVVY YSVDFGFDYR AATQFWRNKV LEVAKDFPEY TFAVADEDDF ATEVKDLGLS
     ESGEDVNAAI LDESGRKFAM EPDEFDSDTL REFVTAFKKG KLKPVIKSQP VPKNNKGPVK
     VVVGKTFDSI VMDPKKDVLI EFYAPWCGHC KQLEPVYTAL GKKYKSHKNL VIAKMDATAN
     DVTNDRYKVE GFPTIYFAPR GDKKNPIKFE DGDRDLEHLS KFIEEHARKL SRTREEL
//