ID   SCO1_BOVIN              Reviewed;         305 AA.
AC   A1A4J8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein SCO1 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=SCO1; Synonyms=SCOD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Copper metallochaperone essential for the maturation of
CC       cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the
CC       synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-
CC       CO2/COX2 during its subsequent maturation. Involved in transporting
CC       copper to the Cu(A) site on MT-CO2/COX2. Plays an important role in the
CC       regulation of copper homeostasis by controlling the abundance and cell
CC       membrane localization of copper transporter CTR1.
CC       {ECO:0000250|UniProtKB:O75880, ECO:0000250|UniProtKB:Q5SUC9}.
CC   -!- SUBUNIT: Homodimer. Interacts with COA6. Found in a complex with
CC       TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO2. Interacts with
CC       TMEM177 in a COX20-dependent manner. Interacts with COX20 in a MT-
CC       CO2/COX2- and COX18-dependent manner. Interacts with COX16.
CC       {ECO:0000250|UniProtKB:O75880}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O75880}.
CC       Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75880}; Single-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR   EMBL; BC126613; AAI26614.1; -; mRNA.
DR   RefSeq; NP_001073712.1; NM_001080243.1.
DR   AlphaFoldDB; A1A4J8; -.
DR   SMR; A1A4J8; -.
DR   STRING; 9913.ENSBTAP00000029032; -.
DR   PaxDb; A1A4J8; -.
DR   PRIDE; A1A4J8; -.
DR   Ensembl; ENSBTAT00000029032; ENSBTAP00000029032; ENSBTAG00000021780.
DR   GeneID; 508586; -.
DR   KEGG; bta:508586; -.
DR   CTD; 6341; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021780; -.
DR   VGNC; VGNC:34359; SCO1.
DR   eggNOG; KOG2792; Eukaryota.
DR   GeneTree; ENSGT00390000004323; -.
DR   HOGENOM; CLU_050131_0_3_1; -.
DR   InParanoid; A1A4J8; -.
DR   OMA; IVAHMRP; -.
DR   OrthoDB; 1462537at2759; -.
DR   TreeFam; TF313752; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000021780; Expressed in rumen papilla and 103 other tissues.
DR   ExpressionAtlas; A1A4J8; baseline and differential.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR   CDD; cd02968; SCO; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; PTHR12151; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Copper; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..67
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..305
FT                   /note="Protein SCO1 homolog, mitochondrial"
FT                   /id="PRO_0000280793"
FT   TOPO_DOM        68..101
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:O75880"
FT   TRANSMEM        102..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..305
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:O75880"
FT   REGION          68..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..135
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   DISULFID        173..177
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   305 AA;  33658 MW;  CE41D94A7BBC824A CRC64;
     MAGLLLAPGR IMRLPGSQLW RLFPRGFGVW GPGKETASVL LGRLCARPEE AWRASGLAAC
     CLGSRPLSTA MPPPPGSSGP EWKGSGDPMR PSKPGPVSWK SLAVTFAIGG ALLAGMKYFK
     KEKTEKLEKE RHRSIGKPLL GGPFSLTTHT GEPKTDKDYL GQWVLIYFGF THCPDICPEE
     LEKMIQVVDE IDSIPTLPNL TPLFITIDPE RDTKEAIANY VKEFSPKLIG LTGTKEEIDQ
     VARAFRVYYS PGPKDEDEDY IVDHTIIMYL IGPDGEFLDY FGQNKKNAEI AGSIAAHMRT
     HRKKS