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Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 72)

 H2QVK7_PANTR            Unreviewed;       645 AA.
H2QVK7;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
20-DEC-2017, entry version 57.
RecName: Full=Protein disulfide-isomerase A4 {ECO:0000256|PIRNR:PIRNR036862};
EC=5.3.4.1 {ECO:0000256|PIRNR:PIRNR036862};
AltName: Full=Endoplasmic reticulum resident protein 72 {ECO:0000256|PIRNR:PIRNR036862};
Name=PDIA4 {ECO:0000313|EMBL:JAA31975.1,
ECO:0000313|Ensembl:ENSPTRP00000033973};
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000033973, ECO:0000313|Proteomes:UP000002277};
[1] {ECO:0000313|Ensembl:ENSPTRP00000033973, ECO:0000313|Proteomes:UP000002277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16136131; DOI=10.1038/nature04072;
Chimpanzee sequencing and analysis consortium;
"Initial sequence of the chimpanzee genome and comparison with the
human genome.";
Nature 437:69-87(2005).
[2] {ECO:0000313|Proteomes:UP000002277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16136134; DOI=10.1038/nature04101;
Hughes J.F., Skaletsky H., Pyntikova T., Minx P.J., Graves T.,
Rozen S., Wilson R.K., Page D.C.;
"Conservation of Y-linked genes during human evolution revealed by
comparative sequencing in chimpanzee.";
Nature 437:100-103(2005).
[3] {ECO:0000313|Ensembl:ENSPTRP00000033973}
IDENTIFICATION.
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[4] {ECO:0000313|EMBL:JAA31975.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA34367.1}, and
Skin {ECO:0000313|EMBL:JAA31975.1};
Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
"De novo assembly of the reference chimpanzee transcriptome from
NextGen mRNA sequences.";
Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins. {ECO:0000256|PIRNR:PIRNR036862,
ECO:0000256|RuleBase:RU361130}.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX. {ECO:0000256|PIRNR:PIRNR036862}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000256|PIRNR:PIRNR036862}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000256|PIRNR:PIRNR036862, ECO:0000256|RuleBase:RU004208,
ECO:0000256|SAAS:SAAS00569802}.
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EMBL; AC191230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; GABD01001125; JAA31975.1; -; mRNA.
EMBL; GABE01010372; JAA34367.1; -; mRNA.
EMBL; GABE01010371; JAA34368.1; -; mRNA.
EMBL; GABE01010370; JAA34369.1; -; mRNA.
RefSeq; XP_003318916.1; XM_003318868.3.
RefSeq; XP_016800904.1; XM_016945415.1.
STRING; 9598.ENSPTRP00000033973; -.
Ensembl; ENSPTRT00000036738; ENSPTRP00000033973; ENSPTRG00000019838.
GeneID; 107971647; -.
GeneID; 463822; -.
KEGG; ptr:463822; -.
CTD; 9601; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
KO; K09582; -.
OMA; YRAATQF; -.
OrthoDB; EOG091G05J9; -.
TreeFam; TF106382; -.
Proteomes; UP000002277; Chromosome 7.
Bgee; ENSPTRG00000019838; -.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IEA:Ensembl.
GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR017068; Protein_diS-isomerase_A4.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 3.
PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
SUPFAM; SSF52833; SSF52833; 5.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 3.
PROSITE; PS00194; THIOREDOXIN_1; 3.
PROSITE; PS51352; THIOREDOXIN_2; 3.
2: Evidence at transcript level;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002277};
Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51,
ECO:0000256|SAAS:SAAS00903405};
Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR036862};
Isomerase {ECO:0000256|PIRNR:PIRNR036862,
ECO:0000256|RuleBase:RU361130, ECO:0000313|EMBL:JAA31975.1};
Redox-active center {ECO:0000256|PIRSR:PIRSR605792-51,
ECO:0000256|SAAS:SAAS00903442};
Reference proteome {ECO:0000313|Proteomes:UP000002277};
Repeat {ECO:0000256|SAAS:SAAS00435042};
Signal {ECO:0000256|RuleBase:RU361130}.
SIGNAL 1 24 {ECO:0000256|RuleBase:RU361130}.
CHAIN 25 645 Protein disulfide-isomerase A4.
{ECO:0000256|RuleBase:RU361130}.
/FTId=PRO_5009996879.
DOMAIN 20 156 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
DOMAIN 158 301 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
DOMAIN 505 636 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
COILED 34 62 {ECO:0000256|SAM:Coils}.
DISULFID 206 209 Redox-active.
{ECO:0000256|PIRSR:PIRSR605792-51}.
DISULFID 555 558 Redox-active.
{ECO:0000256|PIRSR:PIRSR605792-51}.
SEQUENCE 645 AA; 72962 MW; D387D4F988F1271D CRC64;
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
EDGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD NDPPIPVAKI
DATSASVLAG RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIIDYMI EQSGPPSKEI LTLKQVQEFL
KDGDDVIIIG VFKGESDRAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
EKFQSRYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KASNDAKRYT RRPLVVVYYS
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL


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