ID A0A2P6RMR1_ROSCH Unreviewed; 300 AA.
AC A0A2P6RMR1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Putative very-long-chain 3-oxoacyl-CoA synthase, Butyrate--CoA ligase {ECO:0000313|EMBL:PRQ47717.1};
DE EC=2.3.1.199 {ECO:0000313|EMBL:PRQ47717.1};
DE EC=6.2.1.2 {ECO:0000313|EMBL:PRQ47717.1};
GN ORFNames=RchiOBHm_Chr2g0102761 {ECO:0000313|EMBL:PRQ47717.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ47717.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ47717.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRQ47717.1}.
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DR EMBL; PDCK01000040; PRQ47717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6RMR1; -.
DR STRING; 74649.A0A2P6RMR1; -.
DR EnsemblPlants; PRQ47717; PRQ47717; RchiOBHm_Chr2g0102761.
DR Gramene; PRQ47717; PRQ47717; RchiOBHm_Chr2g0102761.
DR OMA; SFIWLEF; -.
DR OrthoDB; 858036at2759; -.
DR Proteomes; UP000238479; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157:SF11; ELONGATION OF FATTY ACIDS PROTEIN 3-LIKE; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:PRQ47717.1};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000313|EMBL:PRQ47717.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PRQ47717.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 300 AA; 34389 MW; 90DFE0560E6E871A CRC64;
MGRSVIQTLT FWLSEHPSIV GFRWSHANSW GSTWSFLFTA IALYLTISVL LHLLLALLRR
KGRPVPLGPI PALHSLFMTL LSFTIFAGIT LSSAAEIKET KWFWRRSKTP FQWLLCFPLG
TRPSGRVFFW SYIYYLSRFF HMIRTFFTIL RRGRVVPFQL FNHSILTFIS FMWLEFSQSF
QVLAILSTTL VYSVVYAYRF WVAIGLPRAG FAFVVNCQML LLGCNVACHV GVLLMHFMKG
GCNGIGAWGF NSVLNAVILL LFLNFYVKIH WGYGRRVALA AVEEAKAEAA EEEVVRVKDK
//
