ID H0X009_OTOGA Unreviewed; 645 AA.
AC H0X009;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 86.
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:ENSOGAP00000008218.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000008218.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000008218.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAQR03087342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03087343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03087344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03087345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03087346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0X009; -.
DR STRING; 30611.ENSOGAP00000008218; -.
DR Ensembl; ENSOGAT00000009167.2; ENSOGAP00000008218.2; ENSOGAG00000009163.2.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000157738; -.
DR HOGENOM; CLU_025879_6_2_1; -.
DR InParanoid; H0X009; -.
DR OMA; FRSKHEP; -.
DR TreeFam; TF106382; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
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:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 25..645
FT /note="Protein disulfide-isomerase A4"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005133475"
FT DOMAIN 13..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 168..300
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 505..636
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 24..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 205..208
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 555..558
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 645 AA; 72640 MW; A651BCD46EC64B99 CRC64;
MRARKACLLV LLLALAQLLV AASAQGTDED SPDSENAVED EEEEEEEDDE EEDDLEVKEE
NGVLVLNDAN FDNFVADKDT VLLEFYAPWC GHCKQFAPEY EKIAGVLKDN DPPIAVAKID
ATSASMLASR FDVSGYPTIK ILKKGQAVDY EGSRTQEEIV AKVREVSQPN WTPPPEVTLV
LTKENFDEVV NDADIILVEF YAPWCGHCKK LAPEYEKAAK ELSKRSPPIP LAKVDATTET
DLAKRFDVSG YPTLKIFRKG RPFDYNGPRE KYGIVDYMVE QSGPPSKEIL SLKQVQDFLK
DGDDVIIIGV FKGESDPAYQ QYQDAANNLR EDYKFHHTFS TEIAKFLKVS PGKLVVMQPE
KFQSKYEPKS NVMDIQQGST EGSAIKDYVV NHALPLVGHR KTANDAKRYS KRPLVVVYYS
VDFSFDYRAA TQFWRNKVLE VAKDFPEYTF AIADEEDYST EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDVLRE FVTAFKKGKL KPIIKSQPVP KNNKGPVKVV VGKTFDSIMM
DPKNDVLIEF YAPWCGHCKQ LEPVYTSLAK KYKGQKGLVI AKMDATANDI TSDRYKVEGF
PTIYFAPRGD KKNPIKFEGG DRDLEHLSKF VEEHATKLSR TKEEL
//
