AGP2_ARATH
ID AGP2_ARATH Reviewed; 131 AA.
AC Q9SJY7; Q9ZT18;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Classical arabinogalactan protein 2;
DE Flags: Precursor;
GN Name=AGP2; OrderedLocusNames=At2g22470; ORFNames=F14M13.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 PROTEIN SEQUENCE OF 22-37, HYDROXYLATION AT PRO-24; PRO-26; PRO-28; PRO-34
RP AND PRO-35, AND PYROGLUTAMATE FORMATION AT GLN-22.
RC STRAIN=cv. Columbia;
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 [6]
RP GENE FAMILY, NOMENCLATURE, AND INDUCTION.
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 -!- INDUCTION: By Al treatment. {ECO:0000269|PubMed:12177459}.
CC -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC residues are glycosylated with arabinogalactan.
CC -!- SIMILARITY: Belongs to the classical AGP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC77824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF082299; AAC77824.1; ALT_INIT; mRNA.
DR EMBL; AC006592; AAD22366.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07309.1; -; Genomic_DNA.
DR EMBL; AY062726; AAL32804.1; -; mRNA.
DR EMBL; AY093356; AAM13355.1; -; mRNA.
DR PIR; A84613; A84613.
DR RefSeq; NP_565537.1; NM_127812.3.
DR AlphaFoldDB; Q9SJY7; -.
DR STRING; 3702.AT2G22470.1; -.
DR PaxDb; Q9SJY7; -.
DR EnsemblPlants; AT2G22470.1; AT2G22470.1; AT2G22470.
DR GeneID; 816779; -.
DR Gramene; AT2G22470.1; AT2G22470.1; AT2G22470.
DR KEGG; ath:AT2G22470; -.
DR Araport; AT2G22470; -.
DR TAIR; locus:2041223; AT2G22470.
DR eggNOG; ENOG502SF2J; Eukaryota.
DR HOGENOM; CLU_149596_0_0_1; -.
DR InParanoid; Q9SJY7; -.
DR OMA; GTPMGET; -.
DR PRO; PR:Q9SJY7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; Q9SJY7; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR044959; AGP.
DR PANTHER; PTHR36321; PTHR36321; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydroxylation; Lipoprotein; Membrane; Proteoglycan;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:11006345"
FT CHAIN 22..107
FT /note="Classical arabinogalactan protein 2"
FT /id="PRO_0000268987"
FT PROPEP 108..131
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000268988"
FT REGION 24..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 24
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 26
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 28
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 34
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 35
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT LIPID 107
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
SQ SEQUENCE 131 AA; 12582 MW; 556C229D0F710011 CRC64;
MNSKAMQALI FLGFLATSCL AQAPAPAPTT VTPPPTALPP VTAETPSPIA SPPVPVNEPT
PAPTTSPTTS PVASPPQTDA PAPGPSAGLT PTSSPAPGPD GAADAPSAAW ANKAFLVGTA
VAGALYAVVL A