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COX3_PIG
ID   COX3_PIG                Reviewed;         261 AA.
AC   Q35916; O79879;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome c oxidase subunit 3;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide III;
GN   Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3;
OS   Sus scrofa (Pig).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9732457; DOI=10.1007/pl00006388;
RA   Ursing B.M., Arnason U.;
RT   "The complete mitochondrial DNA sequence of the pig (Sus scrofa).";
RL   J. Mol. Evol. 47:302-306(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Landrace;
RX   PubMed=10433971; DOI=10.1016/s0378-1119(99)00247-4;
RA   Lin C.S., Sun Y.L., Liu C.Y., Yang P.C., Chang L.C., Cheng I.C.,
RA   Mao S.J.T., Huang M.C.;
RT   "Complete nucleotide sequence of pig (Sus scrofa) mitochondrial genome and
RT   dating evolutionary divergence within artiodactyla.";
RL   Gene 236:107-114(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX   PubMed=3017295; DOI=10.1007/bf00499094;
RA   Watanabe T., Hayashi Y., Kimura J., Yasuda Y., Saitou N., Tomita T.,
RA   Ogasawara N.;
RT   "Pig mitochondrial DNA: polymorphism, restriction map orientation, and
RT   sequence data.";
RL   Biochem. Genet. 24:385-396(1986).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P00420};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00420};
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC       COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC       are encoded in the nuclear genome. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC       {ECO:0000250|UniProtKB:P00415}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00415}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00415}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05235.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ002189; CAA05235.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF034253; AAD34191.1; -; Genomic_DNA.
DR   EMBL; M26139; AAA32032.1; -; Genomic_DNA.
DR   PIR; T10978; T10978.
DR   RefSeq; NP_008640.1; NC_000845.1.
DR   AlphaFoldDB; Q35916; -.
DR   SMR; Q35916; -.
DR   STRING; 9823.ENSSSCP00000019141; -.
DR   PaxDb; Q35916; -.
DR   PeptideAtlas; Q35916; -.
DR   Ensembl; ENSSSCT00000019677; ENSSSCP00000019141; ENSSSCG00000018082.
DR   Ensembl; ENSSSCT00070061679; ENSSSCP00070052584; ENSSSCG00070030642.
DR   GeneID; 808507; -.
DR   KEGG; ssc:808507; -.
DR   CTD; 4514; -.
DR   VGNC; VGNC:99792; MT-CO3.
DR   eggNOG; KOG4664; Eukaryota.
DR   GeneTree; ENSGT00390000013064; -.
DR   HOGENOM; CLU_044071_0_0_1; -.
DR   InParanoid; Q35916; -.
DR   OMA; SIYWWGS; -.
DR   OrthoDB; 1304563at2759; -.
DR   TreeFam; TF343435; -.
DR   Reactome; R-SSC-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-SSC-611105; Respiratory electron transport.
DR   Reactome; R-SSC-9707564; Cytoprotection by HMOX1.
DR   Proteomes; UP000008227; Mitochondrion.
DR   Proteomes; UP000314985; Mitochondrion.
DR   Bgee; ENSSSCG00000018082; Expressed in psoas major muscle and 43 other tissues.
DR   ExpressionAtlas; Q35916; baseline.
DR   Genevisible; Q35916; SS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR   CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR   Gene3D; 1.20.120.80; -; 1.
DR   InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR   InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR   InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR   InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   PANTHER; PTHR11403; PTHR11403; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; SSF81452; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..261
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183831"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        16..34
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        35..40
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        41..66
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        67..72
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        73..105
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        106..128
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        129..152
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        153..155
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        156..183
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        184..190
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        191..223
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        224..232
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TRANSMEM        233..256
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   TOPO_DOM        257..261
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00415"
FT   CONFLICT        22..24
FT                   /note="LSA -> YSG (in Ref. 3; AAA32032)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  29728 MW;  07E93FCA7FC1784B CRC64;
     MTHQTHAYHM VNPSPWPLTG ALSALLMTSG LTMWFHFNSM LLLSLGLLTN TLTMYQWWRD
     IIRESTFQGH HTSVVQKGLR YGMILFIISE VLFFTGFFWA FYHSSLAPTP ELGGCWPPTG
     IHPLNPLEVP LLNTSILLAS GVSITWAHHS LMEGDRKHMI QALSITIALG VYFTLLQASE
     YYEAPFTISD GVYGSTFFVA TGFHGLHVII GSTFLAVCLL RQLKFHFTSN HHFGFEAAAW
     YWHFVDVVWL FLYVSIYWWG S
 
 
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