(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 80.
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=10.1105/tpc.12.9.1751;
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}.
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   STRING; 3702.AT4G26320.1; -.
DR   PaxDb; 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   HOGENOM; HOG000029117; -.
DR   InParanoid; Q9STQ3; -.
DR   OMA; MEAMKMR; -.
DR   PRO; PR:Q9STQ3; -.
DR   Proteomes; UP000006548; Chromosome 4.
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; AGP1/3/12/13/14/21.
DR   PANTHER; PTHR34114; PTHR34114; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9STQ3.
DR   SWISS-2DPAGE; Q9STQ3.
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
//

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