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EDR2L_ARATH
ID   EDR2L_ARATH             Reviewed;         719 AA.
AC   Q8VZF6; Q9FH45;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Protein ENHANCED DISEASE RESISTANCE 2-like;
GN   Name=EDR2L; OrderedLocusNames=At5g45560; ORFNames=MFC19.23;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
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).
CC   -!- FUNCTION: Binds to phosphatidylinositol-4-phosphate (PtdIns(4)P). May
CC       regulate the salicylic acid- (SA-) mediated resistance to pathogens (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endosome
CC       membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The pleckstrin homology domain (3-110) binds to
CC       phosphatidylinositol-4-phosphate (PtdIns(4)P). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11194.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB022213; BAB11194.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB018113; BAB11194.1; JOINED; Genomic_DNA.
DR   EMBL; CP002688; AED95268.1; -; Genomic_DNA.
DR   EMBL; AY064989; AAL57642.1; -; mRNA.
DR   RefSeq; NP_199369.2; NM_123924.3.
DR   AlphaFoldDB; Q8VZF6; -.
DR   SMR; Q8VZF6; -.
DR   STRING; 3702.AT5G45560.1; -.
DR   iPTMnet; Q8VZF6; -.
DR   PaxDb; Q8VZF6; -.
DR   PRIDE; Q8VZF6; -.
DR   ProteomicsDB; 224739; -.
DR   EnsemblPlants; AT5G45560.1; AT5G45560.1; AT5G45560.
DR   GeneID; 834592; -.
DR   Gramene; AT5G45560.1; AT5G45560.1; AT5G45560.
DR   KEGG; ath:AT5G45560; -.
DR   Araport; AT5G45560; -.
DR   TAIR; locus:2163548; AT5G45560.
DR   eggNOG; ENOG502QS0N; Eukaryota.
DR   HOGENOM; CLU_018946_0_0_1; -.
DR   InParanoid; Q8VZF6; -.
DR   OMA; INICKHE; -.
DR   OrthoDB; 268655at2759; -.
DR   PhylomeDB; Q8VZF6; -.
DR   PRO; PR:Q8VZF6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8VZF6; baseline and differential.
DR   Genevisible; Q8VZF6; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR045096; EDR2-like.
DR   InterPro; IPR009769; EDR2_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR12136; PTHR12136; 1.
DR   Pfam; PF07059; EDR2_C; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00234; START; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50848; START; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endoplasmic reticulum; Endosome; Membrane; Plant defense;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..719
FT                   /note="Protein ENHANCED DISEASE RESISTANCE 2-like"
FT                   /id="PRO_0000428906"
FT   TRANSMEM        665..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3..110
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          180..392
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   REGION          134..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  81725 MW;  240A36A041D69E34 CRC64;
     MSKVVYEGWM VRYGRRKIGR SYIHMRYFVL EPRLLAYYKK KPQDNQLPIK TMVIDGNCRV
     EDRGLKTHHG HMVYVLSIYN KKEKHHRITM AAFNIQEALM WKEKIECVID QHQDSLVPSG
     QQYVSFEYKP GMDAGRTASS SDHESPFSAL EDENDSQRDL LRRTTIGNGP PESILDWTKE
     FDAELSNQSS SNQAFSRKHW RLLQCQNGLR IFEELLEVDY LPRSCSRAMK AVGVVEATCE
     EIFELVMSMD GTRYEWDCSF HNGRLVEEVD GHTAILYHRL LLDWFPMVVW PRDLCYVRYW
     RRNDDGSYVV LFRSREHENC GPQPGFVRAH LESGGFNIAP LKPRNGRPRT QVQHLIQIDL
     KGWGSGYLPA FQQHCLLQML NSVSGLREWF SQTDDRGQPI RIPVMVNMAS SSLALGKGGK
     HHHKSSLSID QTNGASRNSV LMDEDSDDDD EFQIPDSEPE PETSKQDQET DAKKTEEPAL
     NIDLSCFSGN LRHDDNENAR NCWRISDGNN FKVRGKSFCD DKRKIPAGKH LMDLVAVDWF
     KDTKRMDHVV RRKGCAAQVA AEKGLFSTVV NVQVPGSTHY SMVFYFVTKE LVPGSLFQRF
     VDGDDEFRNS RLKLIPLVPK GSWIVRQSVG STPCLLGKAV DCNYIRGPTY LEIDVDIGSS
     TVANGVLGLV IGVITSLVVE MAFLVQANTP EELPERLIGA VRVSHVELSS AIVPNLDSD
 
 
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