C05AK_ARATH
ID C05AK_ARATH Reviewed; 515 AA.
AC Q9LJY5;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome P450 705A22 {ECO:0000303|PubMed:23284057};
DE EC=1.14.-.- {ECO:0000305};
DE AltName: Full=Protein GRAVITY PERSISTENCE SIGNAL 1 {ECO:0000303|PubMed:23284057};
GN Name=CYP705A22 {ECO:0000303|PubMed:23284057};
GN Synonyms=GPS1 {ECO:0000303|PubMed:23284057};
GN OrderedLocusNames=At3g20130 {ECO:0000312|Araport:AT3G20130};
GN ORFNames=MAL21.16 {ECO:0000312|EMBL:BAB01873.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23284057; DOI=10.3732/ajb.1200436;
RA Withers J.C., Shipp M.J., Rupasinghe S.G., Sukumar P., Schuler M.A.,
RA Muday G.K., Wyatt S.E.;
RT "Gravity Persistent Signal 1 (GPS1) reveals novel cytochrome P450s involved
RT in gravitropism.";
RL Am. J. Bot. 100:183-193(2013).
CC -!- FUNCTION: Plays a role in the gravitropic response of the inflorescence
CC stems and roots. May affect the synthesis of flavonols that have a role
CC in regulating auxin transport. {ECO:0000269|PubMed:23284057}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit loss of tropic response to
CC gravity when reoriented relative to the gravity vector in the cold.
CC {ECO:0000269|PubMed:23284057}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP000383; BAB01873.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76337.1; -; Genomic_DNA.
DR EMBL; BT006472; AAP21280.1; -; mRNA.
DR EMBL; AK228328; BAF00269.1; -; mRNA.
DR RefSeq; NP_188648.1; NM_112904.3.
DR AlphaFoldDB; Q9LJY5; -.
DR SMR; Q9LJY5; -.
DR STRING; 3702.AT3G20130.1; -.
DR PaxDb; Q9LJY5; -.
DR ProteomicsDB; 240442; -.
DR EnsemblPlants; AT3G20130.1; AT3G20130.1; AT3G20130.
DR GeneID; 821556; -.
DR Gramene; AT3G20130.1; AT3G20130.1; AT3G20130.
DR KEGG; ath:AT3G20130; -.
DR Araport; AT3G20130; -.
DR TAIR; locus:2087615; AT3G20130.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9LJY5; -.
DR OMA; FNGRAFN; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9LJY5; -.
DR BioCyc; ARA:AT3G20130-MON; -.
DR PRO; PR:Q9LJY5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJY5; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009958; P:positive gravitropism; 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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="Cytochrome P450 705A22"
FT /id="PRO_0000440767"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 454
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:P04798"
SQ SEQUENCE 515 AA; 58709 MW; C381C48AF50EDC23 CRC64;
MEAVISFDFQ NCFIFILIFL LTFLCFFFFF KKPKDSRVNF DLPPSPPSLP IIGHVHLLLS
TLTHKSLQKL SSRYGPLLYL RIFNVPIILV SSASVAYEIF RTQDVNISSR GVTAVDESLV
FGSSSFVTAP YGDYWKFMKK LTVMKLLGPQ AQEQSRDIRA DDIKRFCRNL LDKARKKESV
EIGKEAMNLM NNILCKMSMG RSFSEENGET EKLRGLVTES IGLMKKMFLA VLLRRQLQKL
GISLFKKDIM GVSNKFDVLL EKVLVEHREK PEKDQGTVML DVLLAAYGDE NAEYKITKNH
IKAFFVDLFI GATDTSVQTI QWTMAEIMNN THILERMREE IDSVVGKSRL IQETDLPNLP
YLHAVIKEAL RLHPPGPLLP REFQQGCKIG GFYIPEKTTL LINAYVVMRD PNVWEDPEEF
KPERFLASSR SGQEDERREQ ALKFLPFGSG RRGCPGSNLA YMIVGSAIGM MVQCFDWRIE
GEKVNMKEAV KGTILTMAHP LKLTPVTRQP PLTWI
