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C85A1_ARATH
ID   C85A1_ARATH             Reviewed;         465 AA.
AC   Q9FMA5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Cytochrome P450 85A1 {ECO:0000303|PubMed:12427998};
DE            Short=AtCYP85A1 {ECO:0000303|PubMed:12427998};
DE            EC=1.14.-.- {ECO:0000269|PubMed:11402205};
DE   AltName: Full=3-dehydroteasterone synthase {ECO:0000303|PubMed:11402205};
DE            EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE   AltName: Full=Brassinosteroid-6-oxidase 1 {ECO:0000303|PubMed:12529536};
DE            Short=BR6ox 1 {ECO:0000303|PubMed:12529536};
DE   AltName: Full=C6-oxidase 1 {ECO:0000303|PubMed:12529536};
DE   AltName: Full=Castasterone synthase {ECO:0000303|PubMed:11402205};
DE            EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE   AltName: Full=Teasterone synthase {ECO:0000303|PubMed:11402205};
DE            EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE   AltName: Full=Typhasterol synthase {ECO:0000303|PubMed:11402205};
DE            EC=1.14.14.- {ECO:0000269|PubMed:11402205};
GN   Name=CYP85A1 {ECO:0000303|PubMed:12427998};
GN   Synonyms=BR6OX1 {ECO:0000303|PubMed:12529536};
GN   OrderedLocusNames=At5g38970 {ECO:0000312|Araport:AT5G38970};
GN   ORFNames=K15E6.150 {ECO:0000312|EMBL:BAB08653.1};
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=11402205; DOI=10.1104/pp.126.2.770;
RA   Shimada Y., Fujioka S., Miyauchi N., Kushiro M., Takatsuto S., Nomura T.,
RA   Yokota T., Kamiya Y., Bishop G.J., Yoshida S.;
RT   "Brassinosteroid-6-oxidases from Arabidopsis and tomato catalyze multiple
RT   C-6 oxidations in brassinosteroid biosynthesis.";
RL   Plant Physiol. 126:770-779(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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   INDUCTION.
RX   PubMed=12427998; DOI=10.1104/pp.011254;
RA   Goda H., Shimada Y., Asami T., Fujioka S., Yoshida S.;
RT   "Microarray analysis of brassinosteroid-regulated genes in Arabidopsis.";
RL   Plant Physiol. 130:1319-1334(2002).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12529536; DOI=10.1104/pp.013029;
RA   Shimada Y., Goda H., Nakamura A., Takatsuto S., Fujioka S., Yoshida S.;
RT   "Organ-specific expression of brassinosteroid-biosynthetic genes and
RT   distribution of endogenous brassinosteroids in Arabidopsis.";
RL   Plant Physiol. 131:287-297(2003).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=21364326; DOI=10.4161/psb.6.3.13206;
RA   Perez-Espana V.H., Sanchez-Leon N., Vielle-Calzada J.-P.;
RT   "CYP85A1 is required for the initiation of female gametogenesis in
RT   Arabidopsis thaliana.";
RL   Plant Signal. Behav. 6:321-326(2011).
RN   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX   PubMed=32333772; DOI=10.1093/pcp/pcaa053;
RA   Hamasaki H., Ayano M., Nakamura A., Fujioka S., Asami T., Takatsuto S.,
RA   Yoshida S., Oka Y., Matsui M., Shimada Y.;
RT   "Light activates brassinosteroid biosynthesis to promote hook opening and
RT   petiole development in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 61:1239-1251(2020).
CC   -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC       biosynthesis (PubMed:11402205, PubMed:12529536). Converts 6-
CC       deoxocastasterone (6-deoxoCS) to castasterone (CS). May also convert 6-
CC       deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-
CC       deoxoteasterone (6-deoxo3DT, 6-deoxo-3-DHT) to 3-dehydroteasterone
CC       (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY)
CC       (PubMed:11402205, PubMed:12529536). Required for the initiation of
CC       female gametogenesis (megagametogenesis) (PubMed:21364326).
CC       {ECO:0000269|PubMed:11402205, ECO:0000269|PubMed:12529536,
CC       ECO:0000269|PubMed:21364326}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 6alpha-hydroxyteasterone + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69959, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20716,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188499;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69960;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC         teasterone; Xref=Rhea:RHEA:69963, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:26863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69964;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 3-dehydro-6alpha-hydroxyteasterone + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69947,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69948;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-6alpha-hydroxyteasterone + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 3-dehydroteasterone + H(+) + 2 H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69951,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69952;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxotyphasterol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 6alpha-hydroxytyphasterol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69939, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20717,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69940;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC         typhasterol; Xref=Rhea:RHEA:69943, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27173, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69944;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxocastasterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 6alpha-hydroxycastasterone + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69875, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20712,
CC         ChEBI:CHEBI:20760, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69876;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6alpha-hydroxycastasterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = castasterone + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:69879, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:20760, ChEBI:CHEBI:23051,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69880;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--
CC         hemoprotein reductase] = 3-dehydroteasterone + 2 H(+) + 3 H2O + 2
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70039,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC         ChEBI:CHEBI:20710, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70040;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxocastasterone + 2 O2 + 2 reduced [NADPH--hemoprotein
CC         reductase] = castasterone + 2 H(+) + 3 H2O + 2 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:70031, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:20712, ChEBI:CHEBI:23051,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70032;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--hemoprotein
CC         reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC         reductase] + teasterone; Xref=Rhea:RHEA:70043, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:20716, ChEBI:CHEBI:26863,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70044;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-deoxotyphasterol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC         reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC         reductase] + typhasterol; Xref=Rhea:RHEA:70035, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:27173,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70036;
CC         Evidence={ECO:0000269|PubMed:11402205};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC       {ECO:0000269|PubMed:11402205}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9FMA5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FMA5-2; Sequence=VSP_014451;
CC       Name=3;
CC         IsoId=Q9FMA5-3; Sequence=VSP_014452, VSP_014453;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in apical shoots, hypocotyls,
CC       siliques and roots (PubMed:12529536, PubMed:32333772). Also present in
CC       the female gametophyte (PubMed:21364326). {ECO:0000269|PubMed:12529536,
CC       ECO:0000269|PubMed:21364326, ECO:0000269|PubMed:32333772}.
CC   -!- DEVELOPMENTAL STAGE: In the female gametophyte, accumulates in ovules
CC       and its neighboring sporophytic cells. {ECO:0000269|PubMed:21364326}.
CC   -!- INDUCTION: Repressed by brassinolide (BL) treatment (PubMed:12427998).
CC       Induced rapidly and transiently in seedlings hooks but fades out of
CC       hypocotyls after exposure to light (PubMed:32333772).
CC       {ECO:0000269|PubMed:12427998, ECO:0000269|PubMed:32333772}.
CC   -!- DISRUPTION PHENOTYPE: No obvious morphological alteration during
CC       vegetative or floral development, but semi-sterile phenotype with
CC       several female gametophytes arrested before the first nuclear mitotic
CC       division of the haploid functional megaspore.
CC       {ECO:0000269|PubMed:21364326}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB035868; BAB60858.1; -; mRNA.
DR   EMBL; AB009048; BAB08653.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94380.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94381.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94382.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70769.1; -; Genomic_DNA.
DR   RefSeq; NP_001332353.1; NM_001344281.1. [Q9FMA5-2]
DR   RefSeq; NP_198713.3; NM_123259.4. [Q9FMA5-2]
DR   RefSeq; NP_851105.1; NM_180774.2. [Q9FMA5-1]
DR   RefSeq; NP_974862.1; NM_203133.2. [Q9FMA5-3]
DR   AlphaFoldDB; Q9FMA5; -.
DR   SMR; Q9FMA5; -.
DR   BioGRID; 19140; 15.
DR   IntAct; Q9FMA5; 14.
DR   STRING; 3702.AT5G38970.1; -.
DR   PaxDb; Q9FMA5; -.
DR   PRIDE; Q9FMA5; -.
DR   EnsemblPlants; AT5G38970.1; AT5G38970.1; AT5G38970. [Q9FMA5-1]
DR   EnsemblPlants; AT5G38970.2; AT5G38970.2; AT5G38970. [Q9FMA5-2]
DR   EnsemblPlants; AT5G38970.3; AT5G38970.3; AT5G38970. [Q9FMA5-3]
DR   EnsemblPlants; AT5G38970.4; AT5G38970.4; AT5G38970. [Q9FMA5-2]
DR   GeneID; 833889; -.
DR   Gramene; AT5G38970.1; AT5G38970.1; AT5G38970. [Q9FMA5-1]
DR   Gramene; AT5G38970.2; AT5G38970.2; AT5G38970. [Q9FMA5-2]
DR   Gramene; AT5G38970.3; AT5G38970.3; AT5G38970. [Q9FMA5-3]
DR   Gramene; AT5G38970.4; AT5G38970.4; AT5G38970. [Q9FMA5-2]
DR   KEGG; ath:AT5G38970; -.
DR   Araport; AT5G38970; -.
DR   TAIR; locus:2152292; AT5G38970.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   InParanoid; Q9FMA5; -.
DR   OMA; WTATRDR; -.
DR   OrthoDB; 574756at2759; -.
DR   PhylomeDB; Q9FMA5; -.
DR   BioCyc; ARA:AT5G38970-MON; -.
DR   BioCyc; MetaCyc:AT5G38970-MON; -.
DR   UniPathway; UPA00381; -.
DR   PRO; PR:Q9FMA5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMA5; baseline and differential.
DR   Genevisible; Q9FMA5; 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; IDA:TAIR.
DR   GO; GO:0016491; F:oxidoreductase 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:0016132; P:brassinosteroid biosynthetic process; IDA:TAIR.
DR   GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
DR   GO; GO:0009561; P:megagametogenesis; IMP:UniProtKB.
DR   GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Brassinosteroid biosynthesis; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..465
FT                   /note="Cytochrome P450 85A1"
FT                   /id="PRO_0000052169"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         415
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"
FT   VAR_SEQ         1..81
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014451"
FT   VAR_SEQ         396..419
FT                   /note="KKSLESQNSCFVFGGGTRLCPGKE -> VSPWSHKTHALCLEVGQGFVLVRN
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014452"
FT   VAR_SEQ         420..465
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014453"
SQ   SEQUENCE   465 AA;  53767 MW;  0C00459C9C866D1F CRC64;
     MGAMMVMMGL LLIIVSLCSA LLRWNQMRYT KNGLPPGTMG WPIFGETTEF LKQGPNFMRN
     QRLRYGSFFK SHLLGCPTLI SMDSEVNRYI LKNESKGLVP GYPQSMLDIL GTCNMAAVHG
     SSHRLMRGSL LSLISSTMMR DHILPKVDHF MRSYLDQWNE LEVIDIQDKT KHMAFLSSLT
     QIAGNLRKPF VEEFKTAFFK LVVGTLSVPI DLPGTNYRCG IQARNNIDRL LRELMQERRD
     SGETFTDMLG YLMKKEGNRY PLTDEEIRDQ VVTILYSGYE TVSTTSMMAL KYLHDHPKAL
     QELRAEHLAF RERKRQDEPL GLEDVKSMKF TRAVIYETSR LATIVNGVLR KTTRDLEING
     YLIPKGWRIY VYTREINYDA NLYEDPLIFN PWRWMKKSLE SQNSCFVFGG GTRLCPGKEL
     GIVEISSFLH YFVTRYRWEE IGGDELMVFP RVFAPKGFHL RISPY
 
 
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