C72C1_ARATH
ID C72C1_ARATH Reviewed; 519 AA.
AC Q9SHG5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome P450 72C1;
DE EC=1.14.-.-;
DE AltName: Full=Protein CHIBI 2;
DE AltName: Full=Protein DWARFISH WITH LOW FERTILITY;
DE AltName: Full=Protein SHRINK 1;
DE AltName: Full=Protein SUPPRESSOR OF PHYB-4 PROTEIN 7;
GN Name=CYP72C1; Synonyms=CHI2, DLF, SHK1, SOB7; OrderedLocusNames=At1g17060;
GN ORFNames=F20D23.24;
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15689343; DOI=10.1093/jxb/eri073;
RA Nakamura M., Satoh T., Tanaka S., Mochizuki N., Yokota T., Nagatani A.;
RT "Activation of the cytochrome P450 gene, CYP72C1, reduces the levels of
RT active brassinosteroids in vivo.";
RL J. Exp. Bot. 56:833-840(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15773850; DOI=10.1111/j.1365-313x.2005.02357.x;
RA Takahashi N., Nakazawa M., Shibata K., Yokota T., Ishikawa A., Suzuki K.,
RA Kawashima M., Ichikawa T., Shimada H., Matsui M.;
RT "shk1-D, a dwarf Arabidopsis mutant caused by activation of the CYP72C1
RT gene, has altered brassinosteroid levels.";
RL Plant J. 42:13-22(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15773851; DOI=10.1111/j.1365-313x.2005.02358.x;
RA Turk E.M., Fujioka S., Seto H., Shimada Y., Takatsuto S., Yoshida S.,
RA Wang H., Torres Q.I., Ward J.M., Murthy G., Zhang J., Walker J.C.,
RA Neff M.M.;
RT "BAS1 and SOB7 act redundantly to modulate Arabidopsis photomorphogenesis
RT via unique brassinosteroid inactivation mechanisms.";
RL Plant J. 42:23-34(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20396969; DOI=10.1007/s10059-010-0055-6;
RA Jung J.H., Lee M., Park C.M.;
RT "A transcriptional feedback loop modulating signaling crosstalks between
RT auxin and brassinosteroid in Arabidopsis.";
RL Mol. Cells 29:449-456(2010).
RN [8]
RP FUNCTION.
RX PubMed=20669042; DOI=10.1007/s11103-010-9663-y;
RA Thornton L.E., Rupasinghe S.G., Peng H., Schuler M.A., Neff M.M.;
RT "Arabidopsis CYP72C1 is an atypical cytochrome P450 that inactivates
RT brassinosteroids.";
RL Plant Mol. Biol. 74:167-181(2010).
CC -!- FUNCTION: Atypical cytochrome P450 involved in brassinosteroids (BRs)
CC inactivation and regulation of BRs homeostasis. Does not possess carbon
CC 26 hydroxylase activity and may inactivate BRs by hydroxylation of
CC carbons other than C-26. Acts in association with CYP734A1 to
CC inactivate BRs and modulate photomorphogenesis.
CC {ECO:0000269|PubMed:15689343, ECO:0000269|PubMed:15773850,
CC ECO:0000269|PubMed:15773851, ECO:0000269|PubMed:20396969,
CC ECO:0000269|PubMed:20669042}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, roots, cotyledons, stamens
CC and silique junctions. {ECO:0000269|PubMed:15773850,
CC ECO:0000269|PubMed:15773851}.
CC -!- INDUCTION: By brassinolide (BL), auxin and dark treatment.
CC {ECO:0000269|PubMed:15689343, ECO:0000269|PubMed:15773850}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but increased length of dark-grown hypocotyls, reduced
CC responsiveness of hypocotyls to light and increased responsiveness to
CC brassinolide (BL). {ECO:0000269|PubMed:15773850,
CC ECO:0000269|PubMed:15773851, ECO:0000269|PubMed:20396969}.
CC -!- MISCELLANEOUS: The gain-of-function mutant shk1-D (T-DNA tagging) shows
CC a severe dwarf phenotype and an important reduction of the levels of
CC the BRs castasterone (CS), 6-deoxocastasterone (6-deoxoCS) and 6-
CC deoxotyphasterol (6-deoxoTY). The gain-of-function mutant chi2 show
CC reduced length of hypocotyls grown in red, far-red and blue lights or
CC darkeness. The gain of function mutant dlf1-D shows severe dwarf
CC phenotype with low fertility.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD50024.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50024.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK229082; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D86306; D86306.
DR AlphaFoldDB; Q9SHG5; -.
DR SMR; Q9SHG5; -.
DR STRING; 3702.AT1G17060.1; -.
DR PeptideAtlas; Q9SHG5; -.
DR PRIDE; Q9SHG5; -.
DR ProteomicsDB; 240497; -.
DR EnsemblPlants; AT1G17060.1; AT1G17060.1; AT1G17060.
DR Gramene; AT1G17060.1; AT1G17060.1; AT1G17060.
DR Araport; AT1G17060; -.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; Q9SHG5; -.
DR BioCyc; ARA:AT1G17060-MON; -.
DR PRO; PR:Q9SHG5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHG5; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 Growth regulation; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..519
FT /note="Cytochrome P450 72C1"
FT /id="PRO_0000411194"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 467
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 CONFLICT 350
FT /note="D -> G (in Ref. 3; AK229082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 59594 MW; 26CF94F21C96F2E9 CRC64;
MLEIITVRKV FLIGFLILIL NWVWRAVNWV WLRPKRLEKY LKKQGFSGNS YRILMGDMRE
SNQMDQVAHS LPLPLDADFL PRMMPFLHHT VLKHGKKCFT WYGPYPNVIV MDPETLREIM
SKHELFPKPK IGSHNHVFLS GLLNHEGPKW SKHRSILNPA FRIDNLKSIL PAFNSSCKEM
LEEWERLASA KGTMELDSWT HCHDLTRNML ARASFGDSYK DGIKIFEIQQ EQIDLGLLAI
RAVYIPGSKF LPTKFNRRLR ETERDMRAMF KAMIETKEEE IKRGRGTDKN SDLLFSMLAS
NTKTIKEQGP DSGLSLDDLI DDCKAFYLAG QNVTSSLFVW TLVALSQHQD WQNKARDEIS
QAFGNNEPDF EGLSHLKVVT MILHEVLRLY SPAYFTCRIT KQEVKLERFS LPEGVVVTIP
MLLVHHDSDL WGDDVKEFKP ERFANGVAGA TKGRLSFLPF SSGPRTCIGQ NFSMLQAKLF
LAMVLQRFSV ELSPSYTHAP FPAATTFPQH GAHLIIRKL
