C70B1_ARATH
ID C70B1_ARATH Reviewed; 524 AA.
AC Q9C788; A0MEF2; Q8GWJ5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytochrome P450 704B1;
DE AltName: Full=Long-chain fatty acid omega-hydroxylase;
DE EC=1.14.14.80 {ECO:0000269|PubMed:19700560};
GN Name=CYP704B1; OrderedLocusNames=At1g69500; ORFNames=F10D13.15;
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] OF 11-524.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-524.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19700560; DOI=10.1104/pp.109.144469;
RA Dobritsa A.A., Shrestha J., Morant M., Pinot F., Matsuno M., Swanson R.,
RA Moller B.L., Preuss D.;
RT "CYP704B1 is a long-chain fatty acid omega-hydroxylase essential for
RT sporopollenin synthesis in pollen of Arabidopsis.";
RL Plant Physiol. 151:574-589(2009).
CC -!- FUNCTION: Involved in pollen wall development. Catalyzes the conversion
CC of long-chain fatty acids to the corresponding omega-hydroxylated fatty
CC acids. Omega-hydroxylated fatty acids, together with in-chain
CC hydroxylated fatty acids, are key monomeric aliphatic building blocks
CC for sporopollenin synthesis during exine formation.
CC {ECO:0000269|PubMed:19700560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:19700560};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in anthers from early stage
CC 9 to early stage 12 of flower development, with a peak during stages 9
CC to 11. {ECO:0000269|PubMed:19700560}.
CC -!- DISRUPTION PHENOTYPE: Lack of exine in pollen grain walls.
CC {ECO:0000269|PubMed:19700560}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28457.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC43393.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC073178; AAG60111.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34933.1; -; Genomic_DNA.
DR EMBL; AK118803; BAC43393.1; ALT_INIT; mRNA.
DR EMBL; DQ446413; ABE65757.1; -; mRNA.
DR EMBL; DQ652922; ABK28457.1; ALT_SEQ; mRNA.
DR RefSeq; NP_177109.3; NM_105617.3.
DR AlphaFoldDB; Q9C788; -.
DR SMR; Q9C788; -.
DR STRING; 3702.AT1G69500.1; -.
DR PaxDb; Q9C788; -.
DR PRIDE; Q9C788; -.
DR EnsemblPlants; AT1G69500.1; AT1G69500.1; AT1G69500.
DR GeneID; 843283; -.
DR Gramene; AT1G69500.1; AT1G69500.1; AT1G69500.
DR KEGG; ath:AT1G69500; -.
DR Araport; AT1G69500; -.
DR TAIR; locus:2007181; AT1G69500.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9C788; -.
DR OMA; KVWHQRR; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9C788; -.
DR BioCyc; MetaCyc:AT1G69500-MON; -.
DR BRENDA; 1.14.14.80; 399.
DR PRO; PR:Q9C788; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C788; baseline and differential.
DR Genevisible; Q9C788; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0080110; P:sporopollenin biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="Cytochrome P450 704B1"
FT /id="PRO_0000425851"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 471
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"
SQ SEQUENCE 524 AA; 60101 MW; 24D5413C85200213 CRC64;
MSLCLVIACM VTSWIFLHRW GQRNKSGPKT WPLVGAAIEQ LTNFDRMHDW LVEYLYNSRT
VVVPMPFTTY TYIADPINVE YVLKTNFSNY PKGETYHSYM EVLLGDGIFN SDGELWRKQR
KTASFEFASK NLRDFSTVVF KEYSLKLFTI LSQASFKEQQ VDMQELLMRM TLDSICKVGF
GVEIGTLAPE LPENHFAKAF DTANIIVTLR FIDPLWKMKK FLNIGSEALL GKSIKVVNDF
TYSVIRRRKA ELLEAQISPT NNNNNNNNKV KHDILSRFIE ISDDPDSKET EKSLRDIVLN
FVIAGRDTTA TTLTWAIYMI MMNENVAEKL YSELQELEKE SAEATNTSLH QYDTEDFNSF
NEKVTEFAGL LNYDSLGKLH YLHAVITETL RLYPAVPQDP KGVLEDDMLP NGTKVKAGGM
VTYVPYSMGR MEYNWGSDAA LFKPERWLKD GVFQNASPFK FTAFQAGPRI CLGKDSAYLQ
MKMAMAILCR FYKFHLVPNH PVKYRMMTIL SMAHGLKVTV SRRS
