FAH12_RICCO
ID FAH12_RICCO Reviewed; 387 AA.
AC Q41131; B9SQ58; D2CPE1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Oleate hydroxylase FAH12 {ECO:0000303|PubMed:27056057, ECO:0000303|PubMed:7624314};
DE Short=RcFAH12 {ECO:0000303|PubMed:27056057};
DE EC=1.14.-.- {ECO:0000269|PubMed:27056057};
DE AltName: Full=Oleate Delta(12)-hydroxylase {ECO:0000303|PubMed:27056057};
DE AltName: Full=Phosphatidylcholine 12-monooxygenase {ECO:0000303|PubMed:8784737};
DE EC=1.14.18.4 {ECO:0000269|PubMed:8784737};
GN Name=FAH12 {ECO:0000303|PubMed:7624314};
GN ORFNames=RCOM_0146820 {ECO:0000312|EMBL:EEF34257.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. Baker 296; TISSUE=Endosperm;
RX PubMed=7624314; DOI=10.1073/pnas.92.15.6743;
RA van de Loo F.J., Broun P., Turner S., Somerville C.;
RT "An oleate 12-hydroxylase from Ricinus communis L. is a fatty acyl
RT desaturase homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6743-6747(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANTS OLE-1
RP SER-49; ALA-242 AND GLN-319, MUTAGENESIS OF PHE-49; VAL-242 AND HIS-319,
RP DEVELOPMENTAL STAGE, AND PATHWAY.
RC TISSUE=Endosperm;
RX PubMed=27056057; DOI=10.1007/s00425-016-2508-4;
RA Venegas-Caleron M., Sanchez R., Salas J.J., Garces R., Martinez-Force E.;
RT "Molecular and biochemical characterization of the OLE-1 high-oleic castor
RT seed (Ricinus communis L.) mutant.";
RL Planta 244:245-258(2016).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Rogusus;
RX PubMed=1417766; DOI=10.1042/bj2870141;
RA Smith M.A., Jonsson L., Stymne S., Stobart K.;
RT "Evidence for cytochrome b5 as an electron donor in ricinoleic acid
RT biosynthesis in microsomal preparations from developing castor bean
RT (Ricinus communis L.).";
RL Biochem. J. 287:141-144(1992).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=8784737; DOI=10.1007/bf02523827;
RA Lin J.T., McKeon T.A., Goodrich-Tanrikulu M., Stafford A.E.;
RT "Characterization of oleoyl-12-hydroxylase in castor microsomes using the
RT putative substrate, 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine.";
RL Lipids 31:571-577(1996).
RN [6]
RP FUNCTION.
RX PubMed=9085577; DOI=10.1104/pp.113.3.933;
RA Broun P., Somerville C.;
RT "Accumulation of ricinoleic, lesquerolic, and densipolic acids in seeds of
RT transgenic Arabidopsis plants that express a fatty acyl hydroxylase cDNA
RT from castor bean.";
RL Plant Physiol. 113:933-942(1997).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=22371508; DOI=10.1104/pp.111.192153;
RA Hu Z., Ren Z., Lu C.;
RT "The phosphatidylcholine diacylglycerol cholinephosphotransferase is
RT required for efficient hydroxy fatty acid accumulation in transgenic
RT Arabidopsis.";
RL Plant Physiol. 158:1944-1954(2012).
CC -!- FUNCTION: Oleate hydroxylase involved in the biosynthesis of
CC ricinoleate (PubMed:7624314, PubMed:27056057). It uses cytochrome b5 as
CC an electron donor (PubMed:1417766). May act on both oleic acid
CC (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (PubMed:8784737).
CC {ECO:0000269|PubMed:1417766, ECO:0000269|PubMed:27056057,
CC ECO:0000269|PubMed:7624314, ECO:0000269|PubMed:8784737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-acyl-2-[(R)-12-
CC hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 Fe(III)-[cytochrome
CC b5] + H2O; Xref=Rhea:RHEA:46360, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58293,
CC ChEBI:CHEBI:86048; EC=1.14.18.4;
CC Evidence={ECO:0000269|PubMed:8784737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + AH2 + O2 = (12R)-hydroxy-(9Z)-
CC octadecenoate + A + H2O; Xref=Rhea:RHEA:55956, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:91295;
CC Evidence={ECO:0000269|PubMed:27056057};
CC -!- ACTIVITY REGULATION: Inhibited by oleoyloxyethyl phosphocholine.
CC {ECO:0000269|PubMed:8784737}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.3. {ECO:0000269|PubMed:8784737};
CC Temperature dependence:
CC Optimum temperature is 22.5 degrees Celsius.
CC {ECO:0000269|PubMed:8784737};
CC -!- PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:27056057}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:1417766};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds. Barely detected in leaves.
CC {ECO:0000269|PubMed:7624314}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during seeds
CC development. {ECO:0000269|PubMed:27056057}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Promotes the accumulation of hydroxy fatty acids when
CC expressed in A.thaliana. {ECO:0000269|PubMed:22371508}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; U22378; AAC49010.1; -; mRNA.
DR EMBL; EU523112; ACD39348.1; -; mRNA.
DR EMBL; EQ974077; EEF34257.1; -; Genomic_DNA.
DR PIR; T09839; T09839.
DR RefSeq; NP_001310650.1; NM_001323721.1.
DR RefSeq; XP_002528127.1; XM_002528081.2.
DR AlphaFoldDB; Q41131; -.
DR STRING; 3988.XP_002528127.1; -.
DR PRIDE; Q41131; -.
DR GeneID; 8267537; -.
DR KEGG; ag:AAC49010; -.
DR KEGG; rcu:8267537; -.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR OrthoDB; 577374at2759; -.
DR BRENDA; 1.14.18.4; 1204.
DR UniPathway; UPA01038; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0102518; F:(11Z)-eicosenoate 14-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR GO; GO:0050183; F:phosphatidylcholine 12-monooxygenase activity; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="Oleate hydroxylase FAH12"
FT /id="PRO_0000434633"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..113
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 145..149
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 319..323
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT VARIANT 49
FT /note="F -> S (in OLE-1; enhanced accumulation of oleic
FT acid but low ricinoleic acid levels in seeds, high-oleic
FT castor mutant 1; when associated with A-242 and Q-319)"
FT /evidence="ECO:0000269|PubMed:27056057"
FT VARIANT 242
FT /note="V -> A (in OLE-1; enhanced accumulation of oleic
FT acid but low ricinoleic acid levels in seeds, high-oleic
FT castor mutant 1; when associated with S-49 and Q-319)"
FT /evidence="ECO:0000269|PubMed:27056057"
FT VARIANT 319
FT /note="H -> Q (in OLE-1; enhanced accumulation of oleic
FT acid but low ricinoleic acid levels in seeds, high-oleic
FT castor mutant 1; when associated with S-49 and A-242)"
FT /evidence="ECO:0000269|PubMed:27056057"
FT MUTAGEN 49
FT /note="F->S: Strongly reduced ricinoleic acid accumulation;
FT when associated with A-242."
FT /evidence="ECO:0000269|PubMed:27056057"
FT MUTAGEN 242
FT /note="V->A: Lower ricinoleic acid accumulation. Strongly
FT reduced ricinoleic acid accumulation; when associated with
FT S-49 or Q-319."
FT /evidence="ECO:0000269|PubMed:27056057"
FT MUTAGEN 319
FT /note="H->Q: Strongly reduced ricinoleic acid accumulation;
FT when associated with A-242."
FT /evidence="ECO:0000269|PubMed:27056057"
FT CONFLICT 176
FT /note="L -> S (in Ref. 1; AAC49010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44435 MW; 85C582CC65FE37D9 CRC64;
MGGGGRMSTV ITSNNSEKKG GSSHLKRAPH TKPPFTLGDL KRAIPPHCFE RSFVRSFSYV
AYDVCLSFLF YSIATNFFPY ISSPLSYVAW LVYWLFQGCI LTGLWVIGHE CGHHAFSEYQ
LADDIVGLIV HSALLVPYFS WKYSHRRHHS NIGSLERDEV FVPKSKSKIS WYSKYLNNPP
GRVLTLAATL LLGWPLYLAF NVSGRPYDRF ACHYDPYGPI FSERERLQIY IADLGIFATT
FVLYQATMAK GLAWVMRIYG VPLLIVNCFL VMITYLQHTH PAIPRYGSSE WDWLRGAMVT
VDRDYGVLNK VFHNIADTHV AHHLFATVPH YHAMEATKAI KPIMGEYYRY DGTPFYKALW
REAKECLFVE PDEGAPTQGV FWYRNKY
