ID A0A078I5A8_BRANA Unreviewed; 332 AA.
AC A0A078I5A8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=(rape) hypothetical protein {ECO:0000313|EMBL:CAF2102556.1};
DE SubName: Full=BnaA05g29370D protein {ECO:0000313|EMBL:CDY44669.1};
GN Name=BnaA05g29370D {ECO:0000313|EMBL:CDY44669.1};
GN ORFNames=DARMORV10_A05P39890.1 {ECO:0000313|EMBL:CAF2102556.1},
GN GSBRNA2T00080645001 {ECO:0000313|EMBL:CDY44669.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY44669.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY44669.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2] {ECO:0000313|EMBL:CDY44669.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAF2102556.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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; HG994359; CAF2102556.1; -; Genomic_DNA.
DR EMBL; LK032599; CDY44669.1; -; Genomic_DNA.
DR RefSeq; XP_013693356.1; XM_013837902.1.
DR STRING; 3708.A0A078I5A8; -.
DR PaxDb; 3708-A0A078I5A8; -.
DR EnsemblPlants; CDY44669; CDY44669; GSBRNA2T00080645001.
DR GeneID; 106397319; -.
DR Gramene; CDY44669; CDY44669; GSBRNA2T00080645001.
DR KEGG; bna:106397319; -.
DR OMA; FITIDPW; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 164..329
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 68..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 208
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 293
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 204..208
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 332 AA; 36722 MW; 984E2FBF6934A45E CRC64;
MASALCRTAS RLRPVQLCYR FRAVSDLLSP SSPSPACISD HGDFSLHRSF FSLSGGIERL
KMDQRRLLST SASGTTSKPS SGESEAKSSG ENEKSGGSEG SDGGGSDQKS DRASGKHARG
APVSWMSFFL LFATGAGLVY YYDREKKRHI EDINTNSKAV KEGPSAGKAA IGGPFSLVRD
DGKRITEKDL MGKWTILYFG FTHCPDICPD ELIKLAAAID KIKEKAGVDV VPVFISVDPE
RDTVQQVHEY VKEFHPKLIG LTGTPEEIKS VARSYRVYYM KTEEEDSDYL VDHSIVMYLM
SPEMNFVKFY GKNHDVDSLT DGVVKEIRQY RK
//
