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

 H0V2B9_CAVPO            Unreviewed;       644 AA.
H0V2B9;
22-FEB-2012, integrated into UniProtKB/TrEMBL.
22-NOV-2017, sequence version 2.
23-MAY-2018, entry version 62.
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|Ensembl:ENSCPOP00000003675};
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003675};
[1] {ECO:0000313|Ensembl:ENSCPOP00000003675}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003675};
PubMed=21993624; DOI=10.1038/nature10530;
Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
Pedersen J.S., Lander E.S., Kellis M.;
"A high-resolution map of human evolutionary constraint using 29
mammals.";
Nature 478:476-482(2011).
[2] {ECO:0000313|Ensembl:ENSCPOP00000003675}
IDENTIFICATION.
STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003675};
Ensembl;
Submitted (JAN-2012) to UniProtKB.
-!- 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; AAKN02015288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_003475406.1; XM_003475358.3.
ProteinModelPortal; H0V2B9; -.
STRING; 10141.ENSCPOP00000003675; -.
Ensembl; ENSCPOT00000004118; ENSCPOP00000003675; ENSCPOG00000004073.
GeneID; 100725231; -.
CTD; 9601; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
InParanoid; H0V2B9; -.
OrthoDB; EOG091G05J9; -.
TreeFam; TF106382; -.
Proteomes; UP000005447; Unassembled WGS sequence.
Bgee; ENSCPOG00000004073; -.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
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; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000005447};
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};
Redox-active center {ECO:0000256|PIRSR:PIRSR605792-51,
ECO:0000256|SAAS:SAAS00903442};
Reference proteome {ECO:0000313|Proteomes:UP000005447};
Repeat {ECO:0000256|SAAS:SAAS00435042};
Signal {ECO:0000256|RuleBase:RU361130}.
SIGNAL 1 26 {ECO:0000256|RuleBase:RU361130}.
CHAIN 27 644 Protein disulfide-isomerase A4.
{ECO:0000256|RuleBase:RU361130}.
/FTId=PRO_5011330333.
DOMAIN 13 155 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
DOMAIN 157 301 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
DOMAIN 504 635 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
COILED 41 61 {ECO:0000256|SAM:Coils}.
SEQUENCE 644 AA; 72603 MW; 866E70D80F530D67 CRC64;
MKLRKAFLLL LLLALAQLLA PASVDGADED SPDRENAIED EDEEEDDDDE EEEDLEVKEE
NGVLVLTDAN FDSFVADKDT VLLEFYAPWC GHCKQFAPEY EKIASTLKDN DPPIPVAKID
ATSASMLASR FDVSGYPTIK LLKKGQAVDY EGSRTQEEII AKVREVSQPD WTPPPEVTLV
LTKENFDEVV NDADIILVEF YAPWCGHCKK LAPEYEKAAK ELSKRSPPIP LAKVDATAET
DLAKRFDVSG YPTLKIFRKG RSFDYNGPRE KYGIVDYMIE QSGPPSKEIQ SLKQVQDFLK
DGDDVIIIGV FQGDSDPAYQ QYQDAANNLR EDYKFYHTFN TEITKFLKVS PGKLVVMQPE
KFQSKYEAQH HVLDVQGSTP ASAIKDHVVK HALPLVGHRK TSNDAKRYTK RPLVVVYYTV
DFSFDYRTAT QFWRSKVLEV AKDFPEYTFA IADEEDYATE VKDLGLSESG EDINAAILDE
GGHKFAMEPQ EFDADALRDF VTAFKKGKLK PVIKSQPVPK NNKGPVKVVV GKTFDAIVMD
PKKDVLIEFY APWCGHCKQL EPIYTSLAKK YKGQKSLVIA KMDATANDVP SDRYKVDGFP
TIYFAPSGDK KNPVKFEGGD RDLEHLSKFV EEHSTQWGRT KEEL


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