AGP10_ARATH
ID AGP10_ARATH Reviewed; 127 AA.
AC Q9M0S4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Classical arabinogalactan protein 10;
DE Flags: Precursor;
GN Name=AGP10; OrderedLocusNames=At4g09030; ORFNames=F23J3.60;
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 22-37, PYROGLUTAMATE
RP FORMATION AT GLN-22, HYDROXYLATION AT PRO-24; PRO-26; PRO-28; PRO-32 AND
RP PRO-36, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION, AND GPI-ANCHOR AT ASN-107.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and at a lower
CC level in roots and siliques. {ECO:0000269|PubMed:11006345}.
CC -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC residues are glycosylated with arabinogalactan.
CC {ECO:0000269|PubMed:11006345}.
CC -!- SIMILARITY: Belongs to the classical AGP family. {ECO:0000305}.
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DR EMBL; AF195891; AAG24278.1; -; mRNA.
DR EMBL; AC005359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161513; CAB78027.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82714.1; -; Genomic_DNA.
DR EMBL; AK229123; BAF00998.1; -; mRNA.
DR PIR; C85091; C85091.
DR RefSeq; NP_192642.1; NM_116972.5.
DR AlphaFoldDB; Q9M0S4; -.
DR BioGRID; 11781; 4.
DR STRING; 3702.AT4G09030.1; -.
DR PaxDb; Q9M0S4; -.
DR ProteomicsDB; 245021; -.
DR EnsemblPlants; AT4G09030.1; AT4G09030.1; AT4G09030.
DR GeneID; 826482; -.
DR Gramene; AT4G09030.1; AT4G09030.1; AT4G09030.
DR KEGG; ath:AT4G09030; -.
DR Araport; AT4G09030; -.
DR TAIR; locus:2122353; AT4G09030.
DR eggNOG; ENOG502RRI8; Eukaryota.
DR HOGENOM; CLU_1909540_0_0_1; -.
DR InParanoid; Q9M0S4; -.
DR OMA; IAMMICA; -.
DR OrthoDB; 1651413at2759; -.
DR PRO; PR:Q9M0S4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0S4; baseline and differential.
DR Genevisible; Q9M0S4; 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 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 10"
FT /id="PRO_0000269001"
FT PROPEP 108..127
FT /note="Removed in mature form"
FT /id="PRO_0000269002"
FT REGION 22..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..90
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 32
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT MOD_RES 36
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345"
FT LIPID 107
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000269|PubMed:11006345"
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 32
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
SQ SEQUENCE 127 AA; 12071 MW; 97BF87D0519D734E CRC64;
MASKSVVVLL FLALIASSAI AQAPGPAPTR SPLPSPAQPP RTAAPTPSIT PTPTPTPSAT
PTAAPVSPPA GSPLPSSASP PAPPTSLTPD GAPVAGPTGS TPVDNNNAAT LAAGSLAGFV
FVASLLL
