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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
 
 
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