ID   AGP1_ARATH              Reviewed;         131 AA.
AC   Q8LCN5; Q94A23; Q9ZT19;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Classical arabinogalactan protein 1;
DE   Flags: Precursor;
GN   Name=AGP1; OrderedLocusNames=At5g64310; ORFNames=MSJ1.15;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RA   Schultz C.J., Gilson P.R., Oxley D., Youl J.J., Bacic A.;
RT   "GPI-anchors on arabinogalactan-proteins: implications for signalling in
RT   plants.";
RL   Trends Plant Sci. 3:426-431(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [3]
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   [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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=11006345; DOI=10.2307/3871187;
RA   Schultz C.J., Johnson K.L., Currie G., Bacic A.;
RT   "The classical arabinogalactan protein gene family of Arabidopsis.";
RL   Plant Cell 12:1751-1767(2000).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12177459; DOI=10.1104/pp.003459;
RA   Schultz C.J., Rumsewicz M.P., Johnson K.L., Jones B.J., Gaspar Y.M.,
RA   Bacic A.;
RT   "Using genomic resources to guide research directions. The arabinogalactan
RT   protein gene family as a test case.";
RL   Plant Physiol. 129:1448-1463(2002).
CC   -!- FUNCTION: Proteoglycan that seems to be implicated in diverse
CC       developmental roles such as differentiation, cell-cell recognition,
CC       embryogenesis and programmed cell death.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and at a lower
CC       level in roots and leaves. {ECO:0000269|PubMed:11006345}.
CC   -!- PTM: O-glycosylated on the hydroxyproline residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the classical AGP family. {ECO:0000305}.
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DR   EMBL; AF082298; AAC77823.1; -; mRNA.
DR   EMBL; AB008268; BAB09862.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97868.1; -; Genomic_DNA.
DR   EMBL; AY050438; AAK91454.1; -; mRNA.
DR   EMBL; AY093798; AAM10414.1; -; mRNA.
DR   EMBL; AY086494; AAM63495.1; -; mRNA.
DR   RefSeq; NP_201236.1; NM_125827.3.
DR   AlphaFoldDB; Q8LCN5; -.
DR   STRING; 3702.AT5G64310.1; -.
DR   iPTMnet; Q8LCN5; -.
DR   PaxDb; Q8LCN5; -.
DR   PRIDE; Q8LCN5; -.
DR   EnsemblPlants; AT5G64310.1; AT5G64310.1; AT5G64310.
DR   GeneID; 836552; -.
DR   Gramene; AT5G64310.1; AT5G64310.1; AT5G64310.
DR   KEGG; ath:AT5G64310; -.
DR   Araport; AT5G64310; -.
DR   TAIR; locus:2173388; AT5G64310.
DR   eggNOG; ENOG502S8AB; Eukaryota.
DR   HOGENOM; CLU_1941037_0_0_1; -.
DR   InParanoid; Q8LCN5; -.
DR   OMA; GHTMAQS; -.
DR   OrthoDB; 1647509at2759; -.
DR   PRO; PR:Q8LCN5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LCN5; baseline and differential.
DR   Genevisible; Q8LCN5; AT.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR044959; AGP.
DR   PANTHER; PTHR36321; PTHR36321; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Proteoglycan; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..108
FT                   /note="Classical arabinogalactan protein 1"
FT                   /id="PRO_0000268985"
FT   PROPEP          109..131
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000268986"
FT   REGION          22..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           108
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        13
FT                   /note="A -> P (in Ref. 5; AAM63495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="P -> T (in Ref. 4; AAM10414/AAK91454)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   131 AA;  12637 MW;  E377DED79DE19392 CRC64;
     MAFSKSLVFV LLAALLISSA VAQSPAPAPS NVGGRRISPA PSPKKMTAPA PAPEVSPSPS
     PAAALTPESS ASPPSPPLAD SPTADSPALS PSAISDSPTE APGPAQGGAV SNKFASFGSV
     AVMLTAAVLV I