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ELOV5_MACFA
ID   ELOV5_MACFA             Reviewed;         299 AA.
AC   Q4R516;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
DE            EC=2.3.1.199 {ECO:0000250|UniProtKB:Q9NYP7, ECO:0000255|HAMAP-Rule:MF_03205};
DE   AltName: Full=3-keto acyl-CoA synthase ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE   AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE            Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE   AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE   AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
GN   Name=ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205}; ORFNames=QflA-11914;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC       reactions that constitute the long-chain fatty acids elongation cycle.
CC       This endoplasmic reticulum-bound enzymatic process allows the addition
CC       of 2 carbons to the chain of long- and very long-chain fatty acids
CC       (VLCFAs) per cycle. Condensing enzyme that acts specifically toward
CC       polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6)
CC       acyl-CoA. May participate in the production of monounsaturated and of
CC       polyunsaturated VLCFAs of different chain lengths that are involved in
CC       multiple biological processes as precursors of membrane lipids and
CC       lipid mediators (By similarity). In conditions where the essential
CC       linoleic and alpha linoleic fatty acids are lacking it is also involved
CC       in the synthesis of Mead acid from oleic acid (By similarity).
CC       {ECO:0000250|UniProtKB:Q8BHI7, ECO:0000255|HAMAP-Rule:MF_03205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC         chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC         EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC         (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:71481; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC         (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC         ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC         octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC         oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-
CC         eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:75121, ChEBI:CHEBI:76559;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC         3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA =
CC         (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489,
CC         ChEBI:CHEBI:71491; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC         (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:73852; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA
CC         = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862,
CC         ChEBI:CHEBI:73863; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC         Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03205}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite
CC       {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein
CC       localizes to the soma and proximal portion of the dendritic tree.
CC       {ECO:0000255|HAMAP-Rule:MF_03205}.
CC   -!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03205}.
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DR   EMBL; AB169728; BAE01809.1; -; mRNA.
DR   RefSeq; NP_001306343.1; NM_001319414.1.
DR   AlphaFoldDB; Q4R516; -.
DR   SMR; Q4R516; -.
DR   STRING; 9541.XP_005552785.1; -.
DR   GeneID; 102140887; -.
DR   CTD; 60481; -.
DR   eggNOG; KOG3071; Eukaryota.
DR   UniPathway; UPA00658; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0097447; C:dendritic tree; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0009922; F:fatty acid elongase activity; ISS:UniProtKB.
DR   GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; ISS:UniProtKB.
DR   GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; ISS:UniProtKB.
DR   GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:InterPro.
DR   GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR   HAMAP; MF_03205; VLCF_elongase_5; 1.
DR   InterPro; IPR002076; ELO_fam.
DR   InterPro; IPR033677; ELOVL5.
DR   PANTHER; PTHR11157; PTHR11157; 1.
DR   PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
DR   Pfam; PF01151; ELO; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell projection; Endoplasmic reticulum;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..299
FT                   /note="Elongation of very long chain fatty acids protein 5"
FT                   /id="PRO_0000282839"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT   REGION          275..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP7"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP7"
SQ   SEQUENCE   299 AA;  35231 MW;  A939940343409C84 CRC64;
     MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP KYMRNKQPFS
     CRGILVVYNL GLTLLSLYMF CELVTGVWEG KYNFFCQGTR TAGESDMKII RVLRWYYFSK
     LIEFMDTFFF ILRKNNHQIT VLHVYHHASM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
     YSYYGLSSVP SMRPYLWWKK YITQGQLLQF VLTIIQTSCG VIWPCTFPLG WLYFQIGYMI
     SLIALFTNFY IQTYNKKGAS RRKDHLKDHQ NGSVAAVNGH TNSFSPLENN VKPRKLRKD
 
 
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