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EP1L4_ARATH
ID   EP1L4_ARATH             Reviewed;         443 AA.
AC   Q9ZVA5;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=EP1-like glycoprotein 4 {ECO:0000305};
DE   AltName: Full=Curculin-like (Mannose-binding) lectin family protein {ECO:0000303|PubMed:23738689};
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g78860 {ECO:0000312|Araport:AT1G78860};
GN   ORFNames=F9K20.9 {ECO:0000312|EMBL:AAC83024.1};
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   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   [4]
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; AAC83024.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36163.1; -; Genomic_DNA.
DR   PIR; A96818; A96818.
DR   RefSeq; NP_178007.1; NM_106534.2.
DR   AlphaFoldDB; Q9ZVA5; -.
DR   SMR; Q9ZVA5; -.
DR   IntAct; Q9ZVA5; 1.
DR   STRING; 3702.AT1G78860.1; -.
DR   PaxDb; Q9ZVA5; -.
DR   PRIDE; Q9ZVA5; -.
DR   ProteomicsDB; 222325; -.
DR   EnsemblPlants; AT1G78860.1; AT1G78860.1; AT1G78860.
DR   GeneID; 844223; -.
DR   Gramene; AT1G78860.1; AT1G78860.1; AT1G78860.
DR   KEGG; ath:AT1G78860; -.
DR   Araport; AT1G78860; -.
DR   TAIR; locus:2037568; AT1G78860.
DR   eggNOG; ENOG502QWJD; Eukaryota.
DR   HOGENOM; CLU_043351_0_0_1; -.
DR   InParanoid; Q9ZVA5; -.
DR   OMA; ECQWPEK; -.
DR   OrthoDB; 556631at2759; -.
DR   PhylomeDB; Q9ZVA5; -.
DR   PRO; PR:Q9ZVA5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZVA5; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; 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   3: Inferred from homology;
KW   Cell wall; Disulfide bond; Glycoprotein; Lectin; Reference proteome;
KW   Secreted; Signal; WD repeat.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..443
FT                   /note="EP1-like glycoprotein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5009974830"
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        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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   CARBOHYD        434
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"
SQ   SEQUENCE   443 AA;  49194 MW;  437C2AE10D9E0ACF CRC64;
     MEFSTTLALF FTLSIFLVGA QAKVPVDDQF RVVNEGGYTD YSPIEYNPDV RGFVPFSDNF
     RLCFYNTTQN AYTLALRIGN RAQESTLRWV WEANRGSPVK ENATLTFGED GNLVLAEADG
     RVVWQTNTAN KGVVGIKILE NGNMVIYDSN GKFVWQSFDS PTDTLLVGQS LKLNGQNKLV
     SRLSPSVNAN GPYSLVMEAK KLVLYYTTNK TPKPIGYYEY EFFTKIAQLQ SMTFQAVEDA
     DTTWGLHMEG VDSGSQFNVS TFLSRPKHNA TLSFLRLESD GNIRVWSYST LATSTAWDVT
     YTAFTNDNTD GNDECRIPEH CLGFGLCKKG QCNACPSDIG LLGWDETCKI PSLASCDPKT
     FHYFKIEGAD SFMTKYNGGS TTTESACGDK CTRDCKCLGF FYNRKSSRCW LGYELKTLTK
     TGDTSLVAYV KAPNASKKSA LAI
 
 
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