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Database: UniProt
Entry: G3R0Z5_GORGO
LinkDB: G3R0Z5_GORGO
Original site: G3R0Z5_GORGO 
ID   G3R0Z5_GORGO            Unreviewed;       301 AA.
AC   G3R0Z5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Synthesis of cytochrome C oxidase 1 {ECO:0000313|Ensembl:ENSGGOP00000008842.2};
GN   Name=SCO1 {ECO:0000313|Ensembl:ENSGGOP00000008842.2};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000008842.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000008842.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000008842.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000008842.2}
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; CABD030103669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030103670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018869009.1; XM_019013464.1.
DR   AlphaFoldDB; G3R0Z5; -.
DR   STRING; 9593.ENSGGOP00000008842; -.
DR   Ensembl; ENSGGOT00000009082.3; ENSGGOP00000008842.2; ENSGGOG00000009044.3.
DR   GeneID; 101138570; -.
DR   KEGG; ggo:101138570; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   GeneTree; ENSGT00390000004323; -.
DR   HOGENOM; CLU_050131_0_3_1; -.
DR   InParanoid; G3R0Z5; -.
DR   OMA; IVAHMRP; -.
DR   OrthoDB; 169656at2759; -.
DR   TreeFam; TF313752; -.
DR   Proteomes; UP000001519; Chromosome 17.
DR   Bgee; ENSGGOG00000009044; Expressed in adult mammalian kidney and 5 other cell types or tissues.
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:0006878; P:intracellular copper ion homeostasis; IEA:UniProtKB-UniRule.
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; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF4; PROTEIN SCO1 HOMOLOG, MITOCHONDRIAL; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT   REGION          63..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         169
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         173
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   BINDING         260
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037736-1"
FT   DISULFID        169..173
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   301 AA;  33736 MW;  F9767F51A66972C9 CRC64;
     MAMLVLVPGR VTRPLGGQVW RFLPRGLEFW GPAEGPARVL LRQFCARQAE AWRASGRPGY
     CLGTRPLSTA RPPPPWSQKG PGDSTRPSKP GPVSWKSLAI TFAIGGALLA GMKHVKKEKA
     EKLEKERQRH IGKPLLGGPF SLTTHTGERK TDKDYLGQWL LIYFGFTHCP DVCPEELEKM
     IQVVDEIDSI TTLPDLTPLF ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA
     YRVYYSPGPK DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI AAHMRPYRKK
     S
//
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