AGP9_ARATH
ID AGP9_ARATH Reviewed; 191 AA.
AC Q9C5S0; O82327;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Classical arabinogalactan protein 9;
DE Flags: Precursor;
GN Name=AGP9; OrderedLocusNames=At2g14890; ORFNames=T26I20.5;
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], PROTEIN SEQUENCE OF 21-33, HYDROXYLATION AT
RP PRO-23; PRO-26; PRO-27; PRO-31 AND PRO-33, PYROGLUTAMATE FORMATION AT
RP GLN-21, AND TISSUE SPECIFICITY.
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 [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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C5S0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and at a lower
CC level in leaves and siliques. {ECO:0000269|PubMed:11006345}.
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 ---------------------------------------------------------------------------
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; AF195890; AAG24277.1; -; mRNA.
DR EMBL; AC005396; AAC61286.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06347.1; -; Genomic_DNA.
DR EMBL; AF324669; AAG40020.2; -; mRNA.
DR EMBL; AF326868; AAG41450.1; -; mRNA.
DR EMBL; AF339690; AAK00372.1; -; mRNA.
DR EMBL; AY078968; AAL84965.1; -; mRNA.
DR EMBL; AY125554; AAM78064.1; -; mRNA.
DR PIR; F84522; F84522.
DR RefSeq; NP_179095.1; NM_127053.5. [Q9C5S0-1]
DR AlphaFoldDB; Q9C5S0; -.
DR BioGRID; 1337; 1.
DR STRING; 3702.AT2G14890.1; -.
DR PaxDb; Q9C5S0; -.
DR EnsemblPlants; AT2G14890.1; AT2G14890.1; AT2G14890. [Q9C5S0-1]
DR GeneID; 815978; -.
DR Gramene; AT2G14890.1; AT2G14890.1; AT2G14890. [Q9C5S0-1]
DR KEGG; ath:AT2G14890; -.
DR Araport; AT2G14890; -.
DR TAIR; locus:2060475; AT2G14890.
DR eggNOG; ENOG502RZNG; Eukaryota.
DR HOGENOM; CLU_1527270_0_0_1; -.
DR InParanoid; Q9C5S0; -.
DR PRO; PR:Q9C5S0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5S0; baseline and differential.
DR Genevisible; Q9C5S0; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR044981; AGP9/17/18.
DR PANTHER; PTHR37209; PTHR37209; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Glycoprotein; GPI-anchor; Hydroxylation; Lipoprotein; Membrane;
KW Proteoglycan; Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:11006345"
FT CHAIN 21..172
FT /note="Classical arabinogalactan protein 9"
FT /id="PRO_0000268999"
FT PROPEP 173..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000269000"
FT REGION 20..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 23
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 27
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 31
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 33
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT LIPID 172
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="V -> G (in Ref. 4; AAG40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="G -> C (in Ref. 4; AAG40020)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="T -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 18416 MW; 585BDFD2CA873768 CRC64;
MARSFAIAVI CIVLIAGVTG QAPTSPPTAT PAPPTPTTPP PAATPPPVSA PPPVTTSPPP
VTTAPPPANP PPPVSSPPPA SPPPATPPPV ASPPPPVASP PPATPPPVAT PPPAPLASPP
AQVPAPAPTT KPDSPSPSPS SSPPLPSSDA PGPSTDSISP APSPTDVNDQ NGASKMVSSL
VFGSVLVWFM I
