AGP13_ARATH
ID AGP13_ARATH Reviewed; 59 AA.
AC Q9STQ3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Arabinogalactan protein 13 {ECO:0000303|PubMed:11006345};
DE Short=AtAGP13 {ECO:0000303|PubMed:11006345};
DE AltName: Full=Arabinogalactan peptide 13 {ECO:0000303|PubMed:11006345};
DE Short=AG-peptide 13 {ECO:0000303|PubMed:11006345};
DE Flags: Precursor;
GN Name=AGP13 {ECO:0000303|PubMed:11006345}; OrderedLocusNames=At4g26320;
GN ORFNames=T25K17.130;
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], HYDROXYLATION AT PRO-31; PRO-33 AND PRO-35, AND
RP PROTEIN SEQUENCE OF 28-37.
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 Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 28-37, HYDROXYLATION AT PRO-31; PRO-33 AND PRO-35,
RP GLYCOSYLATION AT PRO-31; PRO-33 AND PRO-35, AND GPI-ANCHOR AT SER-37.
RX PubMed=15322080; DOI=10.1074/jbc.m407594200;
RA Schultz C.J., Ferguson K.L., Lahnstein J., Bacic A.;
RT "Post-translational modifications of arabinogalactan-peptides of
RT Arabidopsis thaliana. Endoplasmic reticulum and
RT glycosylphosphatidylinositol-anchor signal cleavage sites and hydroxylation
RT of proline.";
RL J. Biol. Chem. 279:45503-45511(2004).
RN [6]
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000269|PubMed:15322080}.
CC -!- PTM: Contains 4-hydroxyproline; hydroxylated on Pro-31, Pro-33 and Pro-
CC 35. {ECO:0000269|PubMed:11006345, ECO:0000269|PubMed:15322080}.
CC -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC residues are glycosylated with arabinogalactan.
CC {ECO:0000305|PubMed:15322080}.
CC -!- SIMILARITY: Belongs to the AG-peptide 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; AF195894; AAG24281.1; -; mRNA.
DR EMBL; AL049171; CAB38961.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79487.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85185.1; -; Genomic_DNA.
DR EMBL; BT024797; ABD60680.1; -; mRNA.
DR PIR; T06016; T06016.
DR RefSeq; NP_194362.1; NM_118765.3.
DR AlphaFoldDB; Q9STQ3; -.
DR STRING; 3702.AT4G26320.1; -.
DR PaxDb; Q9STQ3; -.
DR PRIDE; Q9STQ3; -.
DR EnsemblPlants; AT4G26320.1; AT4G26320.1; AT4G26320.
DR GeneID; 828738; -.
DR Gramene; AT4G26320.1; AT4G26320.1; AT4G26320.
DR KEGG; ath:AT4G26320; -.
DR Araport; AT4G26320; -.
DR TAIR; locus:2136814; AT4G26320.
DR eggNOG; ENOG502R7SE; Eukaryota.
DR HOGENOM; CLU_183441_3_0_1; -.
DR InParanoid; Q9STQ3; -.
DR OMA; MKQFFAM; -.
DR PRO; PR:Q9STQ3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STQ3; baseline and differential.
DR Genevisible; Q9STQ3; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR039281; AGP3/12/13/14/21.
DR PANTHER; PTHR34114; PTHR34114; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydroxylation; Lipoprotein; Membrane; Proteoglycan; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT PEPTIDE 28..37
FT /note="Arabinogalactan protein 13"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT /id="PRO_0000269013"
FT PROPEP 38..59
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:11006345,
FT ECO:0000305|PubMed:15322080"
FT /id="PRO_0000269014"
FT MOD_RES 31
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT MOD_RES 33
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT MOD_RES 35
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT LIPID 37
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:15322080"
FT CARBOHYD 31
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
FT CARBOHYD 33
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
FT CARBOHYD 35
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
SQ SEQUENCE 59 AA; 6052 MW; 4C6C2356AE464B3A CRC64;
MEAMKMRLFV AVLVAAMAFS AVQQAAAVEA PAPSPTSDAS LAIPAFFASV ATLAFGFLF
