ID A6QNL5_BOVIN Unreviewed; 453 AA.
AC A6QNL5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Protein disulfide-isomerase A6 {ECO:0000256|ARBA:ARBA00024139};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
DE Flags: Fragment;
GN Name=PDIA6 {ECO:0000313|EMBL:AAI48887.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI48887.1};
RN [1] {ECO:0000313|EMBL:AAI48887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI48887.1};
RC TISSUE=Hypothalamus {ECO:0000313|EMBL:AAI48887.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 EMBL; BC148886; AAI48887.1; -; mRNA.
DR RefSeq; NP_001193274.1; NM_001206345.1.
DR AlphaFoldDB; A6QNL5; -.
DR SMR; A6QNL5; -.
DR IntAct; A6QNL5; 1.
DR GeneID; 613927; -.
DR KEGG; bta:613927; -.
DR CTD; 10130; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_030311_0_0_1; -.
DR OrthoDB; 52245at2759; -.
DR TreeFam; TF315231; -.
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 2: Evidence at transcript level;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 15..146
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 167..300
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 154..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAI48887.1"
SQ SEQUENCE 453 AA; 49624 MW; 96EF71550E86D496 CRC64;
RRRLECVAAR ALSMARLVLG LMSCTLFITV NGLYSSSDDV IELTPSNFNR EVIQSDSLWL
VEFYAPWCGH CQRLTPEWKK AATALKDVVK VGAVDADKHQ SLGGQYGVQG FPTIKIFGSN
KNKPEDYQGG RTGEAIVDAA LSALRQLVKD RLGGRGSGYS SGKQGRGDSS SKKDVIELTD
DNFDKNVLDS EDVWMVEFYA PWCGHCKNLE PEWAAAATEV KEQTKGKVKL AAVDATVNQV
LASRYGIRGF PTIKIFQKGE SPVDYDGGRT RSDIVSRALD LFSDNAPPPE LLEIINEDVA
KKTCEEHQLC VVAVLPHILD TGAAGRNSYL EVLLKLADKY KKKMWGWLWT EAGAQSELEN
ALGIGGFGYP AMAAINARKM KFALLKGSFS EQGINEFLRE LSFGRGSTAP VGGGAFPTIS
TREPWDGKDG ELPVEDDIDL SDVELDDLEK DEL
//