ID A0A132AA15_SARSC Unreviewed; 273 AA.
AC A0A132AA15;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein SCO1 -like protein, mitochondrial {ECO:0000313|EMBL:KAF7489067.1};
DE SubName: Full=SCO1-like protein, mitochondrial-like protein {ECO:0000313|EMBL:KPM07425.1};
GN ORFNames=QR98_0059190 {ECO:0000313|EMBL:KPM07425.1}, SSS_3916
GN {ECO:0000313|EMBL:KAF7489067.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM07425.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM07425.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM07425.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
RN [2] {ECO:0000313|Proteomes:UP000070412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33001992;
RA Korhonen P.K., Gasser R.B., Ma G., Wang T., Stroehlein A.J., Young N.D.,
RA Ang C.S., Fernando D.D., Lu H.C., Taylor S., Reynolds S.L., Mofiz E.,
RA Najaraj S.H., Gowda H., Madugundu A., Renuse S., Holt D., Pandey A.,
RA Papenfuss A.T., Fischer K.;
RT "High-quality nuclear genome for Sarcoptes scabiei-A critical resource for
RT a neglected parasite.";
RL PLoS Negl. Trop. Dis. 14:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF7489067.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SSS_KF_BRIS2020 {ECO:0000313|EMBL:KAF7489067.1};
RA Korhonen P.K.K., Guangxu M.G., Wang T.W., Stroehlein A.J.S., Young N.D.,
RA Ang C.-S.A., Fernando D.W.F., Lu H.L., Taylor S.T., Ehtesham M.E.M.,
RA Najaraj S.H.N., Harsha G.H.G., Madugundu A.M., Renuse S.R., Holt D.H.,
RA Pandey A.P., Papenfuss A.P., Gasser R.B.G., Fischer K.F.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblMetazoa:KAF7489067.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-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; WVUK01000065; KAF7489067.1; -; Genomic_DNA.
DR EMBL; JXLN01011566; KPM07425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AA15; -.
DR EnsemblMetazoa; SSS_3916s_mrna; KAF7489067.1; SSS_3916.
DR VEuPathDB; VectorBase:SSCA000040; -.
DR OMA; YYNRMKS; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000070412; Unassembled WGS sequence.
DR Proteomes; UP000616769; 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 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 PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|PIRNR:PIRNR037736};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRNR:PIRNR037736};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037736};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037736};
KW Mitochondrion inner membrane {ECO:0000256|PIRNR:PIRNR037736};
KW Reference proteome {ECO:0000313|Proteomes:UP000070412};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..262
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 136
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 140
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 226
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 136..140
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 273 AA; 31429 MW; D8C6A5A25B5E585C CRC64;
MISFRYLLKF HPINRTLLIQ SISSGIIKPK LLSEISQPLL NHAQVNCFST KPSRKKAQYF
TWKTFLISGA LASFFFYFLK KLKDEKLRKM EKQRKKALGQ AQIGGRFELI DQNGKPFTSH
NLEGKWAMVY FGFTHCPDVC PDELEKIVKA IELLESKKAD PIQPVFISVD PERDSVEAVR
EYIKEFSPKF IGLTGTKEKV EQATRAYRVY YSAGPRDQQN DYIVDHTIIT YLINPEGDLV
DYYGQTKTAE DICSGTLKAM KNYKSLKRKL GFI
//
