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COQ2_CAEEL
ID   COQ2_CAEEL              Reviewed;         356 AA.
AC   Q8I7J4; Q5DX46;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189};
DE            Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE            EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189};
DE   AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE            Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
DE            Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE   Flags: Precursor;
GN   Name=coq-2; ORFNames=F57B9.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC       an all-trans polyprenyl group. Mediates the second step in the final
CC       reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the
CC       condensation of the polyisoprenoid side chain with PHB, generating the
CC       first membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC         hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC         Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC         ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC         ChEBI:CHEBI:78396; EC=2.5.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03189};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03189};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03189}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q8I7J4-1; Sequence=Displayed;
CC       Name=e;
CC         IsoId=Q8I7J4-2; Sequence=VSP_017679, VSP_017680;
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03189}.
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DR   EMBL; FO081266; CCD70307.1; -; Genomic_DNA.
DR   EMBL; FO081266; CCD70311.1; -; Genomic_DNA.
DR   RefSeq; NP_498513.2; NM_066112.5.
DR   RefSeq; NP_871684.1; NM_181955.4. [Q8I7J4-2]
DR   AlphaFoldDB; Q8I7J4; -.
DR   SMR; Q8I7J4; -.
DR   EPD; Q8I7J4; -.
DR   PaxDb; Q8I7J4; -.
DR   PeptideAtlas; Q8I7J4; -.
DR   EnsemblMetazoa; F57B9.4a.1; F57B9.4a.1; WBGene00000762.
DR   EnsemblMetazoa; F57B9.4e.1; F57B9.4e.1; WBGene00000762. [Q8I7J4-2]
DR   GeneID; 175969; -.
DR   KEGG; cel:CELE_F57B9.4; -.
DR   UCSC; F57B9.4e; c. elegans. [Q8I7J4-1]
DR   CTD; 175969; -.
DR   WormBase; F57B9.4a; CE50155; WBGene00000762; coq-2.
DR   WormBase; F57B9.4e; CE32446; WBGene00000762; coq-2. [Q8I7J4-2]
DR   eggNOG; KOG1381; Eukaryota.
DR   GeneTree; ENSGT00940000153771; -.
DR   HOGENOM; CLU_034879_3_3_1; -.
DR   InParanoid; Q8I7J4; -.
DR   OrthoDB; 1343847at2759; -.
DR   Reactome; R-CEL-1268020; Mitochondrial protein import.
DR   Reactome; R-CEL-2142789; Ubiquinol biosynthesis.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:Q8I7J4; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000762; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:WormBase.
DR   CDD; cd13959; PT_UbiA_COQ2; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   HAMAP; MF_01635; UbiA; 1.
DR   InterPro; IPR006370; HB_polyprenyltransferase-like.
DR   InterPro; IPR039653; Prenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Isoprene biosynthesis; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transferase;
KW   Transit peptide; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   CHAIN           45..356
FT                   /note="4-hydroxybenzoate polyprenyltransferase,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT                   /id="PRO_0000228626"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT   VAR_SEQ         202..243
FT                   /note="LTFNWGALLGWCALKGDLSSSAPFWMYAAALQWTLIYDTIYA -> ATLNWS
FT                   VLIAWAELGHFNDFGIFLPLYTATILHTVIYDTIYS (in isoform e)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_017679"
FT   VAR_SEQ         346..356
FT                   /note="EVFQILIRPYH -> EDEKTKESRKNIGDENFDDVLVTTN (in isoform
FT                   e)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_017680"
SQ   SEQUENCE   356 AA;  38923 MW;  63ED6DB213D5065C CRC64;
     MITRSIGIAR RSNSINCIVG SNTSTSYSLD ESTKRWISTS TKQPMSLIPT ASSLVASSPP
     NLKPYLQLMR VDKPIGTWLL YWPCTWSIAM ATPAGQLPSI YMLSLFGAGA FLMRSAGCVI
     NDLWDKDFDK KVERTKLRPL ACGSLTEKQA IGLLAGLLSS SLAILLQLNW YSVAVGASSM
     ALVVGYPLAK RFTYWPQFVL GLTFNWGALL GWCALKGDLS SSAPFWMYAA ALQWTLIYDT
     IYAHQDKADD IMIGVKSTAL RLGADTKKWL SAFGVGTVAS LTACGIASDQ TWPYYVALAA
     TTAQLGWQVG TVDIDNGSDC WDKFKSNSWM GIILFSGIVA STLLKEVFQI LIRPYH
 
 
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