ID A0A3L6RUN9_PANMI Unreviewed; 416 AA.
AC A0A3L6RUN9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Protein disulfide isomerase-like 5-3 {ECO:0000313|EMBL:RLN09499.1};
GN ORFNames=C2845_PM11G07550 {ECO:0000313|EMBL:RLN09499.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN09499.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN09499.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQIB02000007; RLN09499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6RUN9; -.
DR STRING; 4540.A0A3L6RUN9; -.
DR Proteomes; UP000275267; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF167; PROTEIN DISULFIDE ISOMERASE-LIKE 5-3; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:RLN09499.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..416
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018025319"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..148
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 416 AA; 46222 MW; 393DED99195AB5B0 CRC64;
MALRRLLLPL VLLFGLLPPG RVASGGGDGG ELAEFEIPRD GTVVELDESN FDAAVRAVDY
LFVDFYAPWC GHCKRLAPQL DEAAPVLAGL GTPIIIAKVN ADKYRKLGSK YGVDGFPTLM
LFDHGVPSEY TGSRKADLLI ENLKKLVAPD VSVLESDSSI KSFVEAAGIN FPLFIGFGVD
ESLIAEYGAK YKKKAWFSTA KDFSEDMMVL YDFDKFPALV SVNPKYNEQS VFYGPFEGTF
LEDFIRQSLL PLTVPTNRET VKLLKDDGRK VVLTILEDEL DENAPQLIKV LRSAANANHD
LVFGFVGVKQ WEEFTETFDV KGSQLPKIIV WDTKEEYEVV EGSERLEEGD YGSQVSRFLE
GYRSGKTIKK NVGRGSPTLL GLNAIYILIF LVAILVALMY FSGQGEEEQR PRTHQD
//
