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EP1L1_ARATH
ID   EP1L1_ARATH             Reviewed;         455 AA.
AC   Q9ZVA1; Q8L854;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 143.
DE   RecName: Full=EP1-like glycoprotein 1 {ECO:0000303|PubMed:16891401};
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g78820 {ECO:0000312|Araport:AT1G78820};
GN   ORFNames=F9K20.13 {ECO:0000312|EMBL:AAC83044.1};
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=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;
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   DISRUPTION PHENOTYPE.
RX   PubMed=16891401; DOI=10.1105/tpc.106.042200;
RA   Khanna R., Shen Y., Toledo-Ortiz G., Kikis E.A., Johannesson H.,
RA   Hwang Y.-S., Quail P.H.;
RT   "Functional profiling reveals that only a small number of phytochrome-
RT   regulated early-response genes in Arabidopsis are necessary for optimal
RT   deetiolation.";
RL   Plant Cell 18:2157-2171(2006).
RN   [5]
RP   INDUCTION BY RED LIGHT.
RX   PubMed=17076805; DOI=10.1111/j.1365-313x.2006.02914.x;
RA   Tepperman J.M., Hwang Y.S., Quail P.H.;
RT   "phyA dominates in transduction of red-light signals to rapidly responding
RT   genes at the initiation of Arabidopsis seedling de-etiolation.";
RL   Plant J. 48:728-742(2006).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18796151; DOI=10.1186/1471-2229-8-94;
RA   Irshad M., Canut H., Borderies G., Pont-Lezica R., Jamet E.;
RT   "A new picture of cell wall protein dynamics in elongating cells of
RT   Arabidopsis thaliana: confirmed actors and newcomers.";
RL   BMC Plant Biol. 8:94-94(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:18796151}.
CC   -!- INDUCTION: Up-regulated by continuous red light.
CC       {ECO:0000269|PubMed:17076805}.
CC   -!- DISRUPTION PHENOTYPE: Defect in both hypocotyl and cotyledon
CC       photoresponsiveness during deetiolation. {ECO:0000269|PubMed:16891401}.
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DR   EMBL; AC005679; AAC83044.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36159.1; -; Genomic_DNA.
DR   EMBL; AY035116; AAK59621.1; -; mRNA.
DR   EMBL; AY056346; AAL07195.1; -; mRNA.
DR   EMBL; AY062708; AAL32786.1; -; mRNA.
DR   EMBL; AY093367; AAM13366.1; -; mRNA.
DR   EMBL; AY120736; AAM53294.1; -; mRNA.
DR   PIR; E96817; E96817.
DR   RefSeq; NP_178003.1; NM_106530.3.
DR   AlphaFoldDB; Q9ZVA1; -.
DR   SMR; Q9ZVA1; -.
DR   STRING; 3702.AT1G78820.1; -.
DR   PaxDb; Q9ZVA1; -.
DR   PRIDE; Q9ZVA1; -.
DR   ProteomicsDB; 220618; -.
DR   EnsemblPlants; AT1G78820.1; AT1G78820.1; AT1G78820.
DR   GeneID; 844219; -.
DR   Gramene; AT1G78820.1; AT1G78820.1; AT1G78820.
DR   KEGG; ath:AT1G78820; -.
DR   Araport; AT1G78820; -.
DR   TAIR; locus:2037563; AT1G78820.
DR   eggNOG; ENOG502QU13; Eukaryota.
DR   HOGENOM; CLU_043351_0_0_1; -.
DR   InParanoid; Q9ZVA1; -.
DR   OMA; GMCVGCP; -.
DR   OrthoDB; 556631at2759; -.
DR   PhylomeDB; Q9ZVA1; -.
DR   PRO; PR:Q9ZVA1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZVA1; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR035446; SLSG/EP1.
DR   Pfam; PF01453; B_lectin; 1.
DR   PIRSF; PIRSF002686; SLG; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Disulfide bond; Glycoprotein; Lectin; Reference proteome;
KW   S-nitrosylation; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..455
FT                   /note="EP1-like glycoprotein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5009974821"
FT   DOMAIN          43..163
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          374..455
FT                   /note="PAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   MOD_RES         374
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZVA2"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        410..432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   DISULFID        414..420
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   CONFLICT        44
FT                   /note="E -> K (in Ref. 3; AAM53294)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  50594 MW;  2ECB4DFE4599F7D4 CRC64;
     MLRFDYLLIT ALAISTVSVV MAQVPPEKQF RVLNEPGYAP YITEYDASYR FLNSPNQNFF
     TIPFQLMFYN TTPSAYVLAL RVGTRRDMSF TRWIWDANRN NPVGDNSTLS FGRNGNLVLA
     ELNGQVKWQT NTANKGVTGF QILPNGNMVL HDKHGKFVWQ SFDHPTDTLL VGQSLKVNGV
     NKLVSRTSDM NGSDGPYSMV LDNKGLTMYV NKTGTPLVYG GWTDHDFRGT VTFAVTREFD
     NLTEPSAYEL LLEPAPQPAT NPGNNRRLLQ VRPIGSGGGT LNLNKINYNG TISYLRLGSD
     GSLKAFSYFP AATYLEWEET FAFFSNYFVR QCGLPTFCGD YGYCDRGMCV GCPTPKGLLA
     WSDKCAPPKT TQFCSGGKGK AVNYYKIVGV EHFTGPYVND GQGPTSVNDC KAKCDRDCKC
     LGYFYKEKDK KCLLAPLLGT LIKDANTSSV AYIKY
 
 
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