C71B7_ARATH
ID C71B7_ARATH Reviewed; 504 AA.
AC Q96514;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cytochrome P450 71B7;
DE EC=1.14.-.-;
GN Name=CYP71B7; OrderedLocusNames=At1g13110; ORFNames=F3F19.13;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9143359; DOI=10.1006/abbi.1997.9943;
RA Maughan J.A., Nugent J.H.A., Hallahan D.L.;
RT "Expression of CYP71B7, a cytochrome P450 expressed sequence Tag from
RT Arabidopsis thaliana.";
RL Arch. Biochem. Biophys. 341:104-111(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19292762; DOI=10.1111/j.1365-313x.2009.03862.x;
RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.;
RT "Tandem affinity purification and mass spectrometric analysis of
RT ubiquitylated proteins in Arabidopsis.";
RL Plant J. 59:344-358(2009).
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 -!- TISSUE SPECIFICITY: Highly expressed in rosette leaves. Also expressed
CC in roots, leaves, flowers, and siliques.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X97864; CAA66458.1; -; mRNA.
DR EMBL; AC007357; AAD31064.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28971.1; -; Genomic_DNA.
DR EMBL; AF462855; AAL58941.1; -; mRNA.
DR EMBL; BT005809; AAO64744.1; -; mRNA.
DR PIR; T52254; T52254.
DR RefSeq; NP_172770.1; NM_101181.3.
DR AlphaFoldDB; Q96514; -.
DR SMR; Q96514; -.
DR BioGRID; 23108; 1.
DR STRING; 3702.AT1G13110.1; -.
DR iPTMnet; Q96514; -.
DR PaxDb; Q96514; -.
DR PRIDE; Q96514; -.
DR ProteomicsDB; 240388; -.
DR EnsemblPlants; AT1G13110.1; AT1G13110.1; AT1G13110.
DR GeneID; 837868; -.
DR Gramene; AT1G13110.1; AT1G13110.1; AT1G13110.
DR KEGG; ath:AT1G13110; -.
DR Araport; AT1G13110; -.
DR TAIR; locus:2031820; AT1G13110.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR InParanoid; Q96514; -.
DR OMA; IVNEWAI; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q96514; -.
DR BioCyc; ARA:AT1G13110-MON; -.
DR PRO; PR:Q96514; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96514; baseline and differential.
DR Genevisible; Q96514; AT.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 1: Evidence at protein level;
KW Heme; Iron; Isopeptide bond; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..504
FT /note="Cytochrome P450 71B7"
FT /id="PRO_0000052085"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 446
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"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
SQ SEQUENCE 504 AA; 57209 MW; B3102961CF954FBA CRC64;
MSILLCFLCL LPVFLVSLSI LSKRLKPSKW KLPPGPKTLP IIGNLHNLTG LPHTCFRNLS
QKFGPVMLLH FGFVPVVVIS SKEGAEEALK TQDLECCSRP ETVATRMISY NFKDIGFAPY
GEEWKALRKL VVMELLNTKK FQSFRYIREE ENDLLIKKLT ESALKKSPVN LKKTLFTLVA
SIVCRLAFGV NIHKCEFVDE DNVADLVNKF EMLVAGVAFT DFFPGVGWLV DRISGQNKTL
NNVFSELDTF FQNVLDDHIK PGRQVSENPD VVDVMLDLMK KQEKDGESFK LTTDHLKGII
SDIFLAGVNT SAVTLNWAMA ELIRNPRVMK KVQDEIRTTL GDKKQRITEQ DLSQVHYFKL
VVKEIFRLHP AAPLLLPRET MSHVKIQGYD IPVKTQMMIN IYSIARDPKL WTNPDEFNPD
RFLDSSIDYR GLNFELLPFG SGRRICPGMT LGITTVELGL LNLLYFFDWV VPVGKNVKDI
NLEETGSIII SKKTTLELVP LVHH