EP1L3_ARATH
ID EP1L3_ARATH Reviewed; 441 AA.
AC Q9ZVA4; Q8H153;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=EP1-like glycoprotein 3 {ECO:0000303|PubMed:15276441};
DE AltName: Full=Curculin-like (Mannose-binding) lectin family protein {ECO:0000303|PubMed:23738689};
DE AltName: Full=Putative receptor-like protein kinase-like protein {ECO:0000303|PubMed:12833529};
DE Flags: Precursor;
GN OrderedLocusNames=At1g78850 {ECO:0000312|Araport:AT1G78850};
GN ORFNames=F9K20.10 {ECO:0000312|EMBL:AAC83025.1};
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 INDUCTION BY FUNGAL ELICITOR, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12833529; DOI=10.1002/pmic.200300413;
RA Ndimba B.K., Chivasa S., Hamilton J.M., Simon W.J., Slabas A.R.;
RT "Proteomic analysis of changes in the extracellular matrix of Arabidopsis
RT cell suspension cultures induced by fungal elicitors.";
RL Proteomics 3:1047-1059(2003).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY PROGRAMMED
RP CELL DEATH.
RX PubMed=15276441; DOI=10.1016/j.phytochem.2004.04.020;
RA Swidzinski J.A., Leaver C.J., Sweetlove L.J.;
RT "A proteomic analysis of plant programmed cell death.";
RL Phytochemistry 65:1829-1838(2004).
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 CAUTION.
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 -!- FUNCTION: May be involved in a cell-to cell programmed cell death (PCD)
CC signaling mechanism. {ECO:0000303|PubMed:15276441}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12833529,
CC ECO:0000269|PubMed:18796151}.
CC -!- INDUCTION: Up-regulated by fungal elicitor (PubMed:12833529). Up-
CC regulated in both heat- and senescence-induced programmed cell death
CC (PCD) (PubMed:15276441). {ECO:0000269|PubMed:12833529,
CC ECO:0000269|PubMed:15276441}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:12833529}.
CC -!- CAUTION: Identified as a cargo protein of vacuolar sorting receptors
CC (PubMed:23738689). This was based on interactions with truncated
CC vacuolar sorting receptors and their co-secretion in the culture medium
CC (PubMed:23738689). This function is however not supported by recent
CC evidences. {ECO:0000305|PubMed:23738689}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005679; AAC83025.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36162.1; -; Genomic_DNA.
DR EMBL; AY054501; AAK96692.1; -; mRNA.
DR EMBL; BT000758; AAN31898.1; -; mRNA.
DR PIR; H96817; H96817.
DR RefSeq; NP_178006.1; NM_106533.3.
DR AlphaFoldDB; Q9ZVA4; -.
DR SMR; Q9ZVA4; -.
DR IntAct; Q9ZVA4; 1.
DR STRING; 3702.AT1G78850.1; -.
DR iPTMnet; Q9ZVA4; -.
DR MetOSite; Q9ZVA4; -.
DR SwissPalm; Q9ZVA4; -.
DR PaxDb; Q9ZVA4; -.
DR PRIDE; Q9ZVA4; -.
DR ProteomicsDB; 222324; -.
DR EnsemblPlants; AT1G78850.1; AT1G78850.1; AT1G78850.
DR GeneID; 844222; -.
DR Gramene; AT1G78850.1; AT1G78850.1; AT1G78850.
DR KEGG; ath:AT1G78850; -.
DR Araport; AT1G78850; -.
DR TAIR; locus:2037508; AT1G78850.
DR eggNOG; ENOG502QWJD; Eukaryota.
DR HOGENOM; CLU_043351_0_0_1; -.
DR InParanoid; Q9ZVA4; -.
DR OMA; HEFWVNV; -.
DR OrthoDB; 556631at2759; -.
DR PhylomeDB; Q9ZVA4; -.
DR PRO; PR:Q9ZVA4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVA4; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005539; F:glycosaminoglycan binding; IPI:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:1904383; P:response to sodium phosphate; IEP:TAIR.
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 1: Evidence at protein level;
KW Cell wall; Disulfide bond; Glycoprotein; Lectin; Phosphoprotein;
KW Reference proteome; Secreted; Signal; WD repeat.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..441
FT /note="EP1-like glycoprotein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5009974827"
FT DOMAIN 29..159
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT REPEAT 254..296
FT /note="WD"
FT /evidence="ECO:0000255"
FT DOMAIN 356..433
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 387..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 391..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT CONFLICT 432
FT /note="A -> T (in Ref. 3; AAN31898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49051 MW; EAD06180A1C38150 CRC64;
MKFSITLALC FTLSIFLIGS QAKVPVDDQF RVVNEGGYTD YSPIEYNPDV RGFVPFSDNF
RLCFYNTTPN AYTLALRIGN RVQESTLRWV WEANRGSPVK ENATLTFGED GNLVLAEADG
RLVWQTNTAN KGAVGIKILE NGNMVIYDSS GKFVWQSFDS PTDTLLVGQS LKLNGRTKLV
SRLSPSVNTN GPYSLVMEAK KLVLYYTTNK TPKPIAYFEY EFFTKITQFQ SMTFQAVEDS
DTTWGLVMEG VDSGSKFNVS TFLSRPKHNA TLSFIRLESD GNIRVWSYST LATSTAWDVT
YTAFTNADTD GNDECRIPEH CLGFGLCKKG QCNACPSDKG LLGWDETCKS PSLASCDPKT
FHYFKIEGAD SFMTKYNGGS STTESACGDK CTRDCKCLGF FYNRKSSRCW LGYELKTLTR
TGDSSLVAYV KAPNANKKST L
