ID   EP1G_DAUCA              Reviewed;         389 AA.
AC   Q39688;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Epidermis-specific secreted glycoprotein EP1;
DE   AltName: Full=52/54 kDa medium protein;
DE   Flags: Precursor;
GN   Name=EP1;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039 {ECO:0000312|EMBL:AAA33136.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-29, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8275102; DOI=10.1046/j.1365-313x.1993.04050855.x;
RA   van Engelen F.A., Hartog M.V., Thomas T.L., Taylor B., Sturm A.,
RA   van Kammen A., de Vries S.C.;
RT   "The carrot secreted glycoprotein gene EP1 is expressed in the epidermis
RT   and has sequence homology to Brassica S-locus glycoproteins.";
RL   Plant J. 4:855-862(1993).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 27-33 AND 272-278, GLYCOSYLATION AT ASN-29 AND ASN-274,
RP   AND STRUCTURE OF CARBOHYDRATE ON ASN-29 AND ASN-274.
RX   PubMed=2065672; DOI=10.1111/j.1432-1033.1991.tb16106.x;
RA   Sturm A.;
RT   "Heterogeneity of the complex N-linked oligosaccharides at specific
RT   glycosylation sites of two secreted carrot glycoproteins.";
RL   Eur. J. Biochem. 199:169-179(1991).
RN   [3]
RP   GLYCOSYLATION.
RX   PubMed=16668246; DOI=10.1104/pp.96.3.705;
RA   van Engelen F.A., Sterk P., Booij H., Cordewener J.H.G., Rook W.,
RA   van Kammen A., de Vries S.C.;
RT   "Heterogeneity and cell type-specific localization of a cell wall
RT   glycoprotein from carrot suspension cells.";
RL   Plant Physiol. 96:705-712(1991).
CC   -!- FUNCTION: May be involved in the limitation of water flow through the
CC       outer epidermal cell wall, either by direct modification of wall
CC       structure or as a signal instructing the protoplast to restrict water
CC       transport across the cell wall. {ECO:0000303|PubMed:8275102}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8275102}.
CC   -!- TISSUE SPECIFICITY: In 14-day old seedlings, expressed in the epidermis
CC       and apical dome of the shoot and in the hypocotyl, cotyledon and
CC       epidermis of the root. In developing seeds, expressed in both the inner
CC       and outer epidermis of the integument. {ECO:0000269|PubMed:8275102}.
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DR   EMBL; L16983; AAA33136.1; -; mRNA.
DR   PIR; S36638; S36638.
DR   AlphaFoldDB; Q39688; -.
DR   SMR; Q39688; -.
DR   iPTMnet; Q39688; -.
DR   PRIDE; Q39688; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0006833; P:water transport; NAS:UniProtKB.
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   Direct protein sequencing; Glycoprotein; Lectin; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:8275102"
FT   CHAIN           25..389
FT                   /note="Epidermis-specific secreted glycoprotein EP1"
FT                   /id="PRO_0000021187"
FT   DOMAIN          88..193
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2065672"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2065672"
FT   CONFLICT        25
FT                   /note="L -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="E -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="L -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  43552 MW;  5EAE49865FD8EC73 CRC64;
     MARFFPLTLT ILLFFIQRID FCHTLVPANE TFKFVNEGEL GQYISEYFGD YRPLDPFTSP
     FQLCFYNQTP TAFTLALRMG LRRTESLMRW VWEANRGNPV DENATLTFGP DGNLVLARSN
     GQVAWQTSTA NKGVVGLKIL PNGNMVLYDS KGKFLWQSFD TPTDTLLVGQ SLKMGAVTKL
     VSRASPGENV NGPYSLVMEP KGLHLYYKPT TSPKPIRYYS FSLFTKLNKN ESLQNVTFEF
     ENENDQGFAF LLSLKYGTSN SLGGASILNR IKYNTTLSFL RLEIDGNVKI YTYNDKVDYG
     AWEVTYTLFL KAPPPLFQVS LAATESESSE CQLPKKCGNF GLCEESQCVG CPTSSGPVLA
     WSKTCEPPKL SSCGPKDFHY NKLGGWITT