COX5_DICDI
ID COX5_DICDI Reviewed; 120 AA.
AC P29505; Q55CP8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytochrome c oxidase subunit 5;
DE AltName: Full=Cytochrome c oxidase polypeptide V;
GN Name=cxeA; Synonyms=cox5; ORFNames=DDB_G0269118;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 41-60.
RC STRAIN=AX3;
RX PubMed=1661610; DOI=10.1016/0167-4781(91)90220-g;
RA Rizzuto R., Sandona D., Brini M., Capaldi R.A., Bisson R.;
RT "The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is
RT the putative zinc-binding subunit: primary structure of subunit V from the
RT slime mold Dictyostelium discoideum.";
RL Biochim. Biophys. Acta 1129:100-104(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=8382151; DOI=10.1111/j.1432-1033.1993.tb17564.x;
RA Rizzuto R., Sandona D., Brini M., Marschalek R., Dingermann T., Bisson R.;
RT "Structure of the promoter region of the gene encoding cytochrome c oxidase
RT subunit V in Dictyostelium.";
RL Eur. J. Biochem. 211:411-414(1993).
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:P04037}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04037}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII) (By similarity). Slime mold cytochrome c
CC oxidase consists of at least seven different polypeptides species,
CC subunits I, II, III, IV, V, VI, and VIIe/s in order of MW (Probable).
CC {ECO:0000250|UniProtKB:P04037, ECO:0000305|PubMed:1661610}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04037}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04037}; Matrix side
CC {ECO:0000250|UniProtKB:P04037}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC {ECO:0000305}.
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DR EMBL; X55671; CAA39206.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71909.1; -; Genomic_DNA.
DR EMBL; X64771; CAA46018.1; -; Genomic_DNA.
DR PIR; S19718; S19718.
DR RefSeq; XP_646433.1; XM_641341.1.
DR AlphaFoldDB; P29505; -.
DR SMR; P29505; -.
DR STRING; 44689.DDB0191104; -.
DR SWISS-2DPAGE; P29505; -.
DR PaxDb; P29505; -.
DR EnsemblProtists; EAL71909; EAL71909; DDB_G0269118.
DR GeneID; 8617392; -.
DR KEGG; ddi:DDB_G0269118; -.
DR dictyBase; DDB_G0269118; cxeA.
DR eggNOG; ENOG502RHQC; Eukaryota.
DR HOGENOM; CLU_2054088_0_0_1; -.
DR InParanoid; P29505; -.
DR OMA; RDDFGHE; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P29505; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS00848; COX5B_1; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..120
FT /note="Cytochrome c oxidase subunit 5"
FT /id="PRO_0000197033"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04037"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT MOD_RES 2
FT /note="Blocked amino end (Ser)"
SQ SEQUENCE 120 AA; 13498 MW; B5CB93AF53577A79 CRC64;
MSKIVKFLKE LATPSHSMEF FHKPASNSLL DASELNFVRR NIKREDFGHE VLTGAFGTLK
SPVIVESIFH SRIVACEGGD GEEHDILFHT VAEKKPTICL DCGQVFKLKH ISSEGEVMYY
