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COX42_RAT
ID   COX42_RAT               Reviewed;         172 AA.
AC   Q91Y94;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Cytochrome c oxidase subunit 4 isoform 2, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase subunit IV isoform 2;
DE            Short=COX IV-2;
DE   Flags: Precursor;
GN   Name=Cox4i2; Synonyms=Cox4b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11311561; DOI=10.1016/s0378-1119(01)00385-7;
RA   Huettemann M., Kadenbach B., Grossman L.I.;
RT   "Mammalian subunit IV isoforms of cytochrome c oxidase.";
RL   Gene 267:111-123(2001).
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:P00424}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00424}.
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:P00423}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00423}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00423}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC       {ECO:0000305}.
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DR   EMBL; AF255347; AAK49191.1; -; mRNA.
DR   RefSeq; NP_445924.1; NM_053472.1.
DR   RefSeq; XP_006235342.1; XM_006235280.3.
DR   RefSeq; XP_017447569.1; XM_017592080.1.
DR   AlphaFoldDB; Q91Y94; -.
DR   SMR; Q91Y94; -.
DR   STRING; 10116.ENSRNOP00000010418; -.
DR   iPTMnet; Q91Y94; -.
DR   PhosphoSitePlus; Q91Y94; -.
DR   jPOST; Q91Y94; -.
DR   PaxDb; Q91Y94; -.
DR   GeneID; 84683; -.
DR   KEGG; rno:84683; -.
DR   UCSC; RGD:69422; rat.
DR   CTD; 84701; -.
DR   RGD; 69422; Cox4i2.
DR   VEuPathDB; HostDB:ENSRNOG00000007827; -.
DR   eggNOG; KOG4075; Eukaryota.
DR   HOGENOM; CLU_117340_1_1_1; -.
DR   InParanoid; Q91Y94; -.
DR   OMA; MLSRATW; -.
DR   OrthoDB; 1591226at2759; -.
DR   PhylomeDB; Q91Y94; -.
DR   TreeFam; TF105061; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:Q91Y94; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000007827; Expressed in heart and 19 other tissues.
DR   Genevisible; Q91Y94; RN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; ISO:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:RGD.
DR   CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR   Gene3D; 1.10.442.10; -; 1.
DR   InterPro; IPR013288; Cyt_c_oxidase_su4.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR   InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR   PANTHER; PTHR10707; PTHR10707; 1.
DR   Pfam; PF02936; COX4; 1.
DR   PRINTS; PR01873; CYTCOXIDASE4.
DR   SUPFAM; SSF81406; SSF81406; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..172
FT                   /note="Cytochrome c oxidase subunit 4 isoform 2,
FT                   mitochondrial"
FT                   /id="PRO_0000006091"
FT   TOPO_DOM        19..101
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   TRANSMEM        102..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   TOPO_DOM        128..172
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00423"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   172 AA;  20170 MW;  FBBF5527F83E7EF0 CRC64;
     MFSRATRSLV MKTGGLRTQG THSPGSAASS SQRRMTPYVD CYAQRSYPMP DEPYCTELSE
     EQRALKEKEK GSWAQLSQAE KVALYRLQFH ETFAEMNHRS NEWKTVMGCV FFFIGFTALV
     IWWQRVYVFP KKVVTLTEER KAQQLQRLLD MKSNPIQGLS AHWDYEKKEW KK
 
 
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