ID G1PGD9_MYOLU Unreviewed; 266 AA.
AC G1PGD9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=SCO cytochrome c oxidase assembly protein 2 {ECO:0000313|Ensembl:ENSMLUP00000009699.2};
GN Name=SCO2 {ECO:0000313|Ensembl:ENSMLUP00000009699.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009699.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009699.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000009699.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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; AAPE02053877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PGD9; -.
DR STRING; 59463.ENSMLUP00000009699; -.
DR Ensembl; ENSMLUT00000010639.2; ENSMLUP00000009699.2; ENSMLUG00000010645.2.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; G1PGD9; -.
DR OMA; YYNRMKS; -.
DR TreeFam; TF313752; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:UniProtKB-UniRule.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IEA:Ensembl.
DR GO; GO:0003012; P:muscle system process; IEA:Ensembl.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR PANTHER; PTHR12151:SF2; PROTEIN SCO2 HOMOLOG, MITOCHONDRIAL; 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|PIRNR:PIRNR037736};
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:UP000001074}.
FT DOMAIN 95..259
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 133
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT DISULFID 133..137
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 266 AA; 29537 MW; 4FA9AADF6CB13D0C CRC64;
VLLLAQLPKA QHGLSQLKAS TLLKTPGGEA LHVRCRLLSR QGPAETGRQG QPRGPGLRTR
LLVTALFGAG LGGAWLAMRA EKERQQQRRR TEALRQASVG QGDFSLLDHR GQARCKADFR
GQWVLLYFGF THCPDICPDE LEKLVQVVRQ LEAQPGLPPV QPVFITVDPA RDDVAAMARY
VQDFHPRLLG LTGSAEQVAQ VSRSYRVYYS AGPKDADQDY IVDHSIAIYL LNPDGLFTDY
YGRARSAEQI ADSVRRHMAA FRSVLH
//
