PDIA6_PONAB
ID PDIA6_PONAB Reviewed; 440 AA.
AC Q5R6T1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein disulfide-isomerase A6;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q15084};
DE Flags: Precursor;
GN Name=PDIA6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a chaperone that inhibits aggregation of
CC misfolded proteins. Negatively regulates the unfolded protein response
CC (UPR) through binding to UPR sensors such as ERN1, which in turn
CC inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3
CC UPR sensor. Plays a role in platelet aggregation and activation by
CC agonists such as convulxin, collagen and thrombin.
CC {ECO:0000250|UniProtKB:Q15084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q15084};
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. Interacts with MICA on the surface of tumor cells, leading to
CC MICA disulfide bond reduction which is required for its release from
CC tumor cells. Interacts with ITGB3 following platelet stimulation.
CC Interacts with ERN1; the interaction is direct. Interacts with EIF2AK3.
CC {ECO:0000250|UniProtKB:Q15084}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q15084}. Cell membrane
CC {ECO:0000250|UniProtKB:Q15084}. Melanosome
CC {ECO:0000250|UniProtKB:Q15084}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; CR860403; CAH92529.1; -; mRNA.
DR RefSeq; NP_001126483.1; NM_001133011.1.
DR AlphaFoldDB; Q5R6T1; -.
DR SMR; Q5R6T1; -.
DR STRING; 9601.ENSPPYP00000014123; -.
DR Ensembl; ENSPPYT00000045108; ENSPPYP00000035740; ENSPPYG00000012651.
DR GeneID; 100173470; -.
DR KEGG; pon:100173470; -.
DR CTD; 10130; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000155646; -.
DR InParanoid; Q5R6T1; -.
DR OrthoDB; 840943at2759; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 3.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Chaperone; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW Membrane; Phosphoprotein; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..440
FT /note="Protein disulfide-isomerase A6"
FT /id="PRO_0000034239"
FT DOMAIN 20..132
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 124..287
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 139..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..440
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15084"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15084"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15084"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15084"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 190..193
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 440 AA; 48110 MW; 34CC8CEEED17B34C CRC64;
MALLVLGLVS CAFFLEVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR
LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT IKIFGSNKNR PEDYQGGRTG
EAIVDAALSA LRQLVKDRLG GQSGGYSSGK QGRSDSSSKK DVIELTDDSF DKNVLDSEDV
WMVEFYAPWC GHCKNLEPEW AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IISEDIAKRT CEEHQLCVVS
VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG IGGFGYPAMA
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GAFPTIVERE PWDGRDGELP
VEDDIDLSDV ELDDLGKDEL
