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C96AF_ARATH
ID   C96AF_ARATH             Reviewed;         497 AA.
AC   Q9FVS9;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Alkane hydroxylase MAH1 {ECO:0000303|PubMed:17905869};
DE            EC=1.14.-.- {ECO:0000305|PubMed:17905869};
DE   AltName: Full=Cytochrome P450 96A15 {ECO:0000305};
DE   AltName: Full=Protein MID-CHAIN ALKANE HYDROXYLASE 1 {ECO:0000303|PubMed:17905869};
GN   Name=CYP96A15 {ECO:0000305}; Synonyms=MAH1 {ECO:0000303|PubMed:17905869};
GN   OrderedLocusNames=At1g57750 {ECO:0000312|Araport:AT1G57750};
GN   ORFNames=T8L23.21 {ECO:0000312|EMBL:AAG50737.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17905869; DOI=10.1104/pp.107.107300;
RA   Greer S., Wen M., Bird D., Wu X., Samuels L., Kunst L., Jetter R.;
RT   "The cytochrome P450 enzyme CYP96A15 is the midchain alkane hydroxylase
RT   responsible for formation of secondary alcohols and ketones in stem
RT   cuticular wax of Arabidopsis.";
RL   Plant Physiol. 145:653-667(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19346242; DOI=10.1093/jxb/erp061;
RA   Wen M., Jetter R.;
RT   "Composition of secondary alcohols, ketones, alkanediols, and ketols in
RT   Arabidopsis thaliana cuticular waxes.";
RL   J. Exp. Bot. 60:1811-1821(2009).
CC   -!- FUNCTION: Involved in the formation of secondary alcohols and ketones
CC       in stem cuticular wax. Catalyzes the hydroxylation of a methylene unit
CC       in the middle of alkane molecules to form secondary alcohols and
CC       possibly also a second hydroxylation leading to the corresponding
CC       ketones. {ECO:0000269|PubMed:17905869}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:17905869}; Single-pass membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FVS9-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in the expanding regions of the
CC       inflorescence stems, specifically to the epidermal pavement cells,
CC       petioles and siliques. {ECO:0000269|PubMed:17905869}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but stem wax of mutant plants are devoid of secondary
CC       alcohols and ketones and have increased alkane amounts.
CC       {ECO:0000269|PubMed:17905869, ECO:0000269|PubMed:19346242}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; AC079733; AAG50737.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33458.1; -; Genomic_DNA.
DR   EMBL; AF419610; AAL31942.1; -; mRNA.
DR   EMBL; AY090941; AAM13991.1; -; mRNA.
DR   EMBL; BT005810; AAO64745.1; -; mRNA.
DR   PIR; G96611; G96611.
DR   RefSeq; NP_176086.1; NM_104570.3. [Q9FVS9-1]
DR   AlphaFoldDB; Q9FVS9; -.
DR   SMR; Q9FVS9; -.
DR   STRING; 3702.AT1G57750.1; -.
DR   iPTMnet; Q9FVS9; -.
DR   PaxDb; Q9FVS9; -.
DR   PRIDE; Q9FVS9; -.
DR   ProteomicsDB; 240459; -. [Q9FVS9-1]
DR   EnsemblPlants; AT1G57750.1; AT1G57750.1; AT1G57750. [Q9FVS9-1]
DR   GeneID; 842150; -.
DR   Gramene; AT1G57750.1; AT1G57750.1; AT1G57750. [Q9FVS9-1]
DR   KEGG; ath:AT1G57750; -.
DR   Araport; AT1G57750; -.
DR   TAIR; locus:2206470; AT1G57750.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_27_2_1; -.
DR   InParanoid; Q9FVS9; -.
DR   OMA; VIRRMTF; -.
DR   OrthoDB; 1247045at2759; -.
DR   PhylomeDB; Q9FVS9; -.
DR   BioCyc; ARA:AT1G57750-MON; -.
DR   BioCyc; MetaCyc:AT1G57750-MON; -.
DR   PRO; PR:Q9FVS9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FVS9; baseline and differential.
DR   Genevisible; Q9FVS9; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0080133; F:midchain alkane hydroxylase activity; IMP:TAIR.
DR   GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Alkane hydroxylase MAH1"
FT                   /id="PRO_0000431452"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         444
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q96242"
SQ   SEQUENCE   497 AA;  57696 MW;  C0A37BA59164AB78 CRC64;
     MAMLGFYVTF IFFLVCLFTY FFLQKKPQGQ PILKNWPFLR MLPGMLHQIP RIYDWTVEVL
     EATNLTFYFK GPWLSGTDML FTADPRNIHH ILSSNFGNYP KGPEFKKIFD VLGEGILTVD
     FELWEEMRKS NHALFHNQDF IELSVSSNKS KLKEGLVPFL DNAAQKNIII ELQDVFQRFM
     FDTSSILMTG YDPMSLSIEM LEVEFGEAAD IGEEAIYYRH FKPVILWRLQ NWIGIGLERK
     MRTALATVNR MFAKIISSRR KEEISRAKTE PYSKDALTYY MNVDTSKYKL LKPNKDKFIR
     DVIFSLVLAG RDTTSSVLTW FFWLLSKHPQ VMAKLRHEIN TKFDNEDLEK LVYLHAALSE
     SMRLYPPLPF NHKSPAKPDV LPSGHKVDAN SKIVICIYAL GRMRSVWGED ALDFKPERWI
     SDNGGLRHEP SYKFMAFNSG PRTCLGKNLA LLQMKMVALE IIRNYDFKVI EGHKVEPIPS
     ILLRMKHGLK VTVTKKI
 
 
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