ID A0A2K6KUY6_RHIBE Unreviewed; 490 AA.
AC A0A2K6KUY6;
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 A6 {ECO:0000256|ARBA:ARBA00024139};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=PDIA6 {ECO:0000313|Ensembl:ENSRBIP00000015077.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000015077.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000015077.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000015077.1}
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR AlphaFoldDB; A0A2K6KUY6; -.
DR Ensembl; ENSRBIT00000038917.1; ENSRBIP00000015077.1; ENSRBIG00000031454.1.
DR GeneTree; ENSGT00940000155646; -.
DR Proteomes; UP000233180; 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; cd02983; P5_C; 1.
DR CDD; cd03001; PDI_a_P5; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01126; pdi_dom; 2.
DR PANTHER; PTHR45815; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR PANTHER; PTHR45815:SF3; PROTEIN DISULFIDE-ISOMERASE A6; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 47..181
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 202..335
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 53687 MW; 63EE5A28F0A9ED6E CRC64;
MRIITAPASK VSRGSNEFMI PVRRSDHGKS SSPAHSLSRK SPIRYPSTTT ANAPSLVSCA
FFLAVNGLYS SSDDVIELTP SNFNREVIQS DSLWLVEFYA PWCGHCQRLT PEWKKAATAL
KDVVKVGAVD ADKHQSLGGQ YGVQGFPTIK IFGSNKNRPE DYQGGRTGEA IVDAALSALR
QLVKDRLGGR SGGYSSGKQG RSDSSSKKDV IELTDDSFDE NVLDSEDVWM VEFYAPWCGH
CKNLEPEWAA AASEVKEQTK GKVKLAAVDA TVNQVLASRY GIRGFPTIKI FQKGESPVDY
DGGRTRSDIV SRALDLFSDN APPPELLEII NEDIAKRTCE EHQLCVVAVL PHILDTGAAG
RNSYLEVLLK MADKYKRKFW FSRWLWTEAG AQSELETALG IGGFGYPAMA AINARKMKFA
LLKGSFSEQG INEFLRELSF GRGSTAPVGG GAFPTIVERE PWDGRDGELP VEDDIDLSDV
ELDDLGKDEL
//
