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Database: UniProt
Entry: A0A2T7F7N2_9POAL
LinkDB: A0A2T7F7N2_9POAL
Original site: A0A2T7F7N2_9POAL 
ID   A0A2T7F7N2_9POAL        Unreviewed;       512 AA.
AC   A0A2T7F7N2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN   ORFNames=GQ55_1G261900 {ECO:0000313|EMBL:PUZ76078.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ76078.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ76078.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336}, and HAL2
RC   {ECO:0000313|EMBL:PUZ76078.1};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) 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         ECO:0000256|RuleBase:RU361130};
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; CM009749; PUZ76078.1; -; Genomic_DNA.
DR   EMBL; CM009749; PUZ76079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7F7N2; -.
DR   STRING; 1504633.A0A2T7F7N2; -.
DR   EnsemblPlants; PUZ76078; PUZ76078; GQ55_1G261900.
DR   EnsemblPlants; PUZ76079; PUZ76079; GQ55_1G261900.
DR   Gramene; PUZ76078; PUZ76078; GQ55_1G261900.
DR   Gramene; PUZ76079; PUZ76079; GQ55_1G261900.
DR   Proteomes; UP000244336; Chromosome 1.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF206; PROTEIN DISULFIDE ISOMERASE-LIKE 1-3; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244336};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT   CHAIN           28..512
FT                   /note="Protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5033850994"
FT   DOMAIN          21..141
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          353..480
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          479..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        59..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        403..406
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   512 AA;  56326 MW;  8C6AD418452A43A9 CRC64;
     MATCSRIPFA FLVALLLLLS SSSTASAEEE AVLTLDAGNF SEVVAAHQFI VVEFYAPWCG
     HCKQLAPEYE KAASILSKHD PPVVLAKVDA SDEKNKDLSG KYDVQGFPTI KILRSQGDNA
     QEYNGPRDAD GIVEYLKKQV GPASVEIRSV EDATDLIGDK GVVVVGVFPA FGGSEYDNFM
     AVAEEMRNDY DFLHTLDGSI LPRGDKAVKG PAVRLFKPFD ELYADSQVFD KDTLEKFIEV
     SGFPTVVTFD TNPTNHKYLL KYFENDGTKA MLFLSFDDDR IEAFKSQFHE AAKQYGEKNI
     SFLIGDVTDA QGAFQYFGLK ESEVPLLFIQ ASTAKYIKPT VEPDQILPWL KEYSDGTLLP
     HVKSDPIPVV NDQPVNVVVA DNLNDVVFNS GKNVLLEFYA PWCGHCQKLA PILDEVAVSL
     QNDEDVIIAK MDATTNDIPP DFAVEGYPTM YFYSSAGNLL SYEGGRTAEE IINFIKKNKG
     SKPGEGAVGD DAAETDAMEE QELALESVKD EL
//
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