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C71BZ_ARATH
ID   C71BZ_ARATH             Reviewed;         500 AA.
AC   Q9LXM3; F4J1W9; Q1PEI9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Cytochrome P450 71B38;
DE            EC=1.14.-.-;
GN   Name=CYP71B38; OrderedLocusNames=At3g44250; ORFNames=T10D17_40;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   CONCEPTUAL TRANSLATION.
RA   Bak S., Paquette S.;
RT   "The Arabidopsis P450 site at http://www.p450.kvl.dk/.";
RL   Unpublished observations (APR-2001).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LXM3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LXM3-2; Sequence=VSP_042262;
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE77881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB88993.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL353865; CAB88993.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77881.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DQ446729; ABE65988.1; -; mRNA.
DR   PIR; T49141; T49141.
DR   RefSeq; NP_190011.1; NM_114293.2.
DR   AlphaFoldDB; Q9LXM3; -.
DR   SMR; Q9LXM3; -.
DR   STRING; 3702.AT3G44250.1; -.
DR   PaxDb; Q9LXM3; -.
DR   PRIDE; Q9LXM3; -.
DR   ProteomicsDB; 240454; -. [Q9LXM3-1]
DR   GeneID; 823550; -.
DR   KEGG; ath:AT3G44250; -.
DR   Araport; AT3G44250; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; Q9LXM3; -.
DR   OrthoDB; 871849at2759; -.
DR   PhylomeDB; Q9LXM3; -.
DR   BioCyc; ARA:AT3G44250-MON; -.
DR   PRO; PR:Q9LXM3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXM3; baseline and differential.
DR   Genevisible; Q9LXM3; 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   2: Evidence at transcript level;
KW   Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 71B38"
FT                   /id="PRO_0000052112"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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   VAR_SEQ         157..185
FT                   /note="KSVDETQNSSVDLRKVLFSFTASIICRLA -> NLLMS (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:17147637"
FT                   /id="VSP_042262"
SQ   SEQUENCE   500 AA;  56996 MW;  946D080EEFFA6D13 CRC64;
     MSIFLCFLLL LPLSLILFKK LLPSKGKLPP GPIGLPIIGN LHQLGKLLYK SFHKISQEYG
     PVVLLRLGVV PVIVVSSKEG AEEVLKTHDL ETCTRPKTAA TGLFTYNFKD IGFAPFGDDW
     REMRKITTLE LFSVKKLKSF RYIREEESEL LVKKISKSVD ETQNSSVDLR KVLFSFTASI
     ICRLAFGQNF HQCDFVDMEK VEELVLESEA NLGTFAFADF FPGGWLIDRI SGQHSRVNKA
     FYKLTNFYKH VIDDHLKTGQ PQDHSDIVSV MLDMINKPTK ADSFKVTYDH LKGVMSDIFL
     AGVNGGANTM IWTLTELSRH PRVMKKLQEE IRAMLGPNKE RITEEDLEKV EYLKLVMVET
     FRLHPPAPLL LPRLTMSDIK IQGYNIPKNT MIQINTYAIG RDPKYWKQPG EFIPERFLDS
     PIDYKGQHFE LLPFGAGRRI CPGMATGITM VELGLLNLLY FFDWSLPNGM TIEDIDMEED
     EGFAIAKKVP LVLIQTSHRW
 
 
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