AGP15_ARATH
ID AGP15_ARATH Reviewed; 61 AA.
AC Q9LYF6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Arabinogalactan protein 15 {ECO:0000303|PubMed:11006345};
DE Short=AtAGP15 {ECO:0000303|PubMed:11006345};
DE AltName: Full=Arabinogalactan peptide 15 {ECO:0000303|PubMed:11006345};
DE Short=AG-peptide 15 {ECO:0000303|PubMed:11006345};
DE Flags: Precursor;
GN Name=AGP15 {ECO:0000303|PubMed:11006345}; OrderedLocusNames=At5g11740;
GN ORFNames=T22P22_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], PROTEIN SEQUENCE OF 23-35, HYDROXYLATION AT
RP PRO-27; PRO-29 AND PRO-31, AND PYROGLUTAMATE FORMATION AT GLN-23.
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 23-35, HYDROXYLATION AT PRO-27; PRO-29 AND PRO-31,
RP PYROGLUTAMATE FORMATION AT GLN-23, GLYCOSYLATION AT PRO-27; PRO-29 AND
RP PRO-31, AND GPI-ANCHOR AT SER-35.
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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=25053647; DOI=10.1093/jxb/eru300;
RA Pereira A.M., Masiero S., Nobre M.S., Costa M.L., Solis M.T.,
RA Testillano P.S., Sprunck S., Coimbra S.;
RT "Differential expression patterns of arabinogalactan proteins in
RT Arabidopsis thaliana reproductive tissues.";
RL J. Exp. Bot. 65:5459-5471(2014).
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 -!- TISSUE SPECIFICITY: Expressed in reproductive tissues. Expressed in
CC chalaza, funiculus, stigma, septum, style, integument and transmitting
CC tract. {ECO:0000269|PubMed:25053647}.
CC -!- PTM: Contains 4-hydroxyproline; hydroxylated on Pro-27, Pro-29 and Pro-
CC 31. {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}.
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DR EMBL; AF195896; AAG24283.1; -; mRNA.
DR EMBL; AL163814; CAB87692.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91716.1; -; Genomic_DNA.
DR EMBL; AF375418; AAK53002.1; -; mRNA.
DR EMBL; AY129482; AAM91068.1; -; mRNA.
DR PIR; T48533; T48533.
DR RefSeq; NP_196735.1; NM_121212.3.
DR AlphaFoldDB; Q9LYF6; -.
DR BioGRID; 16324; 3.
DR IntAct; Q9LYF6; 3.
DR STRING; 3702.AT5G11740.1; -.
DR PaxDb; Q9LYF6; -.
DR EnsemblPlants; AT5G11740.1; AT5G11740.1; AT5G11740.
DR GeneID; 831046; -.
DR Gramene; AT5G11740.1; AT5G11740.1; AT5G11740.
DR KEGG; ath:AT5G11740; -.
DR Araport; AT5G11740; -.
DR TAIR; locus:2181960; AT5G11740.
DR eggNOG; ENOG502SBPF; Eukaryota.
DR HOGENOM; CLU_194211_1_0_1; -.
DR OMA; SSMNVLM; -.
DR PRO; PR:Q9LYF6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYF6; baseline and differential.
DR Genevisible; Q9LYF6; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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..22
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT PEPTIDE 23..35
FT /note="Arabinogalactan protein 15"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT /id="PRO_0000269017"
FT PROPEP 36..61
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:11006345,
FT ECO:0000305|PubMed:15322080"
FT /id="PRO_0000269018"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT MOD_RES 27
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT MOD_RES 29
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT MOD_RES 31
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11006345,
FT ECO:0000269|PubMed:15322080"
FT LIPID 35
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:15322080"
FT CARBOHYD 27
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
FT CARBOHYD 29
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
FT CARBOHYD 31
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000305|PubMed:15322080"
SQ SEQUENCE 61 AA; 5849 MW; B79CA28853CB21C2 CRC64;
MAISKASIVV LMMVIISVVA SAQSEAPAPS PTSGSSAISA SFVSAGVAAV AALVFGSALR
I
