EP1L2_ARATH
ID EP1L2_ARATH Reviewed; 455 AA.
AC Q9ZVA2; Q56Z24; Q8H788; Q8VZ33;
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 2 {ECO:0000305};
DE AltName: Full=Curculin-like (Mannose-binding) lectin family protein {ECO:0000303|PubMed:23738689};
DE Flags: Precursor;
GN OrderedLocusNames=At1g78830 {ECO:0000312|Araport:AT1G78830};
GN ORFNames=F9K20.12 {ECO:0000312|EMBL:AAC83028.1};
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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 399-455.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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).
RN [7]
RP S-NITROSYLATION AT CYS-374.
RX PubMed=22115780; DOI=10.1016/j.bbrc.2011.11.036;
RA Fares A., Rossignol M., Peltier J.B.;
RT "Proteomics investigation of endogenous S-nitrosylation in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 416:331-336(2011).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23738689; DOI=10.1111/tpj.12257;
RA Shen J., Suen P.K., Wang X., Lin Y., Lo S.W., Rojo E., Jiang L.;
RT "An in vivo expression system for the identification of cargo proteins of
RT vacuolar sorting receptors in Arabidopsis culture cells.";
RL Plant J. 75:1003-1017(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23738689}. Secreted,
CC cell wall {ECO:0000269|PubMed:18796151}.
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DR EMBL; AC005679; AAC83028.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36160.1; -; Genomic_DNA.
DR EMBL; AF083787; AAN60345.1; -; mRNA.
DR EMBL; AF428439; AAL16208.1; -; mRNA.
DR EMBL; AY150414; AAN12959.1; -; mRNA.
DR EMBL; AY065301; AAL38777.1; -; mRNA.
DR EMBL; AK221145; BAD95140.1; -; mRNA.
DR PIR; F96817; F96817.
DR RefSeq; NP_565191.1; NM_106531.3.
DR AlphaFoldDB; Q9ZVA2; -.
DR SMR; Q9ZVA2; -.
DR PaxDb; Q9ZVA2; -.
DR PRIDE; Q9ZVA2; -.
DR ProteomicsDB; 230053; -.
DR EnsemblPlants; AT1G78830.1; AT1G78830.1; AT1G78830.
DR GeneID; 844220; -.
DR Gramene; AT1G78830.1; AT1G78830.1; AT1G78830.
DR KEGG; ath:AT1G78830; -.
DR Araport; AT1G78830; -.
DR TAIR; locus:2037548; AT1G78830.
DR eggNOG; ENOG502QU13; Eukaryota.
DR HOGENOM; CLU_043351_0_0_1; -.
DR InParanoid; Q9ZVA2; -.
DR OMA; DESTMRW; -.
DR OrthoDB; 556631at2759; -.
DR PhylomeDB; Q9ZVA2; -.
DR PRO; PR:Q9ZVA2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVA2; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; 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; 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.
PE 1: Evidence at protein 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 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5009974826"
FT DOMAIN 44..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:0000269|PubMed:22115780"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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 258..261
FT /note="Missing (in Ref. 3; AAN60345)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="T -> I (in Ref. 4; AAL38777)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> I (in Ref. 3; AAN60345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 50343 MW; 89870536616439F9 CRC64;
MSRFAILVTL ALAIATVSVV IAQVPPEKQF RVVNEGEFGE YITEYDASYR FIESSNQSFF
TSPFQLLFYN TTPSAYILAL RVGLRRDEST MRWIWDANRN NPVGENATLS LGRNGNLVLA
EADGRVKWQT NTANKGVTGF QILPNGNIVL HDKNGKFVWQ SFDHPTDTLL TGQSLKVNGV
NKLVSRTSDS NGSDGPYSMV LDKKGLTMYV NKTGTPLVYG GWPDHDFRGT VTFAVTREFD
NLTEPSAYEL LLEPAPQPAT NPGNNRRLLQ VRPIGSGGGT LNLNKINYNG TISYLRLGSD
GSLKAYSYFP AATYLKWEES FSFFSTYFVR QCGLPSFCGD YGYCDRGMCN ACPTPKGLLG
WSDKCAPPKT TQFCSGVKGK TVNYYKIVGV EHFTGPYVND GQGPTSVNDC KAKCDRDCKC
LGYFYKEKDK KCLLAPLLGT LIKDANTSSV AYIKY
