ID A0A1B0DJV4_PHLPP Unreviewed; 254 AA.
AC A0A1B0DJV4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PPAI008528-PA};
OS Phlebotomus papatasi (Sandfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Phlebotomus; Phlebotomus.
OX NCBI_TaxID=29031 {ECO:0000313|EnsemblMetazoa:PPAI008528-PA, ECO:0000313|Proteomes:UP000092462};
RN [1] {ECO:0000313|Proteomes:UP000092462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|Proteomes:UP000092462};
RA Fulton L., Warren W., Minx P., Wilson R., Clifton S., Abrudan J.,
RA Ramalho-Ortigao M., Lawyer P., Kamhawi S., Rowton E., Lehane M., Bates P.,
RA Valenzeula J., Dillon R., Lobo N., Collins F., McDowell M.A.;
RT "Phlebotomus papatasi, whole genome shotgun sequencing project.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:PPAI008528-PA}
RP IDENTIFICATION.
RC STRAIN=Israel {ECO:0000313|EnsemblMetazoa:PPAI008528-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- FUNCTION: Copper metallochaperone essential for the synthesis and
CC maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved
CC in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a
CC thiol-disulfide oxidoreductase to regulate the redox state of the
CC cysteines in SCO1 during maturation of MT-CO2/COX2.
CC {ECO:0000256|PIRNR:PIRNR037736}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037736}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|PIRNR:PIRNR037736}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996, ECO:0000256|PIRNR:PIRNR037736}.
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DR EMBL; AJVK01001125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0DJV4; -.
DR EnsemblMetazoa; PPAI008528-RA; PPAI008528-PA; PPAI008528.
DR VEuPathDB; VectorBase:PPAI008528; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000092462; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:UniProtKB-UniRule.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IEA:InterPro.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|PIRNR:PIRNR037736};
KW Copper {ECO:0000256|PIRNR:PIRNR037736, ECO:0000256|PIRSR:PIRSR037736-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|PIRNR:PIRNR037736};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037736,
KW ECO:0000256|PIRSR:PIRSR037736-1};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037736};
KW Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR037736}.
FT BINDING 116
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 116..120
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 254 AA; 29116 MW; 8C6D81648EF9BFC8 CRC64;
MSRLGRFLFS RTPWARRLPE TLPRRSMATG NQPKKAIGPI TWRSLGIISI AGAGVMGFMY
YLKHEKDMAL LRERKRQLGK AAIGGRWELV DCEGKPRKSE DFRGQWLLIY FGFTHCPDIC
PEELEKMAKV VDQIDETKEV PNIQPLFITV DPERDSKETV GKYVKEFSPK LLGLTGTVEQ
IQKVCKAFRV YYSAGPKDVD DDYIVDHTII IYLVDPNGEF VDYYGQSMQA DQITTSIMVN
MAKFKQLNEK SWFG
//
