ID A0A2K6AFY1_MANLE Unreviewed; 643 AA.
AC A0A2K6AFY1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein disulfide-isomerase A4 {ECO:0000256|PIRNR:PIRNR036862};
DE EC=5.3.4.1 {ECO:0000256|PIRNR:PIRNR036862};
DE AltName: Full=Endoplasmic reticulum resident protein 72 {ECO:0000256|PIRNR:PIRNR036862};
GN Name=PDIA4 {ECO:0000313|Ensembl:ENSMLEP00000038976.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038976.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000038976.1}
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 -!- SUBUNIT: Part of a large chaperone multiprotein complex.
CC {ECO:0000256|PIRNR:PIRNR036862}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319, ECO:0000256|PIRNR:PIRNR036862}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}.
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 AlphaFoldDB; A0A2K6AFY1; -.
DR Ensembl; ENSMLET00000062590.1; ENSMLEP00000038976.1; ENSMLEG00000043525.1.
DR GeneTree; ENSGT00940000157738; -.
DR Proteomes; UP000233140; 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; 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:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 19..643
FT /note="Protein disulfide-isomerase A4"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5014209430"
FT DOMAIN 45..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 156..299
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 503..634
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..55
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 553..556
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 643 AA; 72913 MW; E88E7A9BBD632817 CRC64;
SRLSTCFLLV LFWGQADNLF MGVWVFHSDS SNRENAIEDE EEEEEEDDEE EDDLEVKEEN
GVLVLNDANF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE KIANILKDND PPIPVAKIDA
TSASMLASRF DVSGYPTIKI LKKGQAVDYE GSRTQEEIVA KVREVSQPDW TPPPEVTLVL
TKENFDEVVN DADIILVEFY APWCGHCKKL APEYEKAAKE LNKRSPPIPL AKVDATAETD
LAKRFDVSGY PTLKIFRKGR PFDYNGPREK YGIVDYMIEQ SGPPSKEILT LKQVQEFLKD
GDDVIIIGVF KGESDPAYQQ YQDAANNLRE DYKFHHAFST EIAKFLKVSQ GQLVVMQPEK
FQSKYEPRSH VMDVQGSTQD SAIKDFVLKY ALPLVGHRKA SNEAKRYTRR PLVVVYYSVD
FSFDYRAATQ FWRSKVLEVA KDFPEYTFAI ADEEDYAGEV KDLGLSESGE DVNAAILDES
GKKFAMEPEE FDSDTLREFV TAFKKGKLKP VIKSQPVPKN NKGPVKVVVG KTFDSIVMDP
KKDVLIEFYA PWCGHCKQLE PVYSSLAKKY KGQKGLVIAK MDATANDVPS DRYKVEGFPT
IYFAPSGDKK NPVKFEGGDR DLEHLSKFIE EHATKLSRTK EEL
//
