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Database: UniProt
Entry: A6QNL5_BOVIN
LinkDB: A6QNL5_BOVIN
Original site: A6QNL5_BOVIN 
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
//
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