AGP6_ARATH
ID AGP6_ARATH Reviewed; 150 AA.
AC Q9LY91; Q9XFR4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Classical arabinogalactan protein 6;
DE Flags: Precursor;
GN Name=AGP6; OrderedLocusNames=At5g14380; ORFNames=F18O22_170;
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].
RC STRAIN=cv. Columbia;
RX PubMed=10451111;
RX DOI=10.1002/(sici)1522-2683(19990701)20:10<2027::aid-elps2027>3.0.co;2-a;
RA Sherrier D.J., Prime T.A., Dupree P.;
RT "Glycosylphosphatidylinositol-anchored cell-surface proteins from
RT Arabidopsis.";
RL Electrophoresis 20:2027-2035(1999).
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 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 [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 FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25336567; DOI=10.1093/mp/ssu114;
RA Jia Q.S., Zhu J., Xu X.F., Lou Y., Zhang Z.L., Zhang Z.P., Yang Z.N.;
RT "Arabidopsis AT-hook protein TEK positively regulates the expression of
RT arabinogalactan proteins in controlling nexine layer formation in the
RT pollen wall.";
RL Mol. Plant 0:0-0(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 (By similarity). Plays an
CC important role during the formation of the nexine layer of the pollen
CC wall (PubMed:25336567). {ECO:0000250, ECO:0000269|PubMed:25336567}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the anthers.
CC {ECO:0000269|PubMed:25336567}.
CC -!- DEVELOPMENTAL STAGE: Initially detected in the tapetum and
CC microsporocytes during meiosis. Highest expression during the tetrad
CC stage. After microspores were released from tetrad, slightly detected
CC in the tapetum and microspores. {ECO:0000269|PubMed:25336567}.
CC -!- INDUCTION: Up-regulated by AHL16/TEK. {ECO:0000269|PubMed:25336567}.
CC -!- PTM: O-glycosylated on the hydroxyproline residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the classical AGP family. {ECO:0000305}.
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DR EMBL; AJ012459; CAB42531.1; -; mRNA.
DR EMBL; AL163817; CAB87777.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92024.1; -; Genomic_DNA.
DR EMBL; BT006161; AAP04145.1; -; mRNA.
DR EMBL; BT008563; AAP40390.1; -; mRNA.
DR EMBL; AK229630; BAF01475.1; -; mRNA.
DR PIR; T48611; T48611.
DR PIR; T52587; T52587.
DR RefSeq; NP_196942.1; NM_121442.3.
DR AlphaFoldDB; Q9LY91; -.
DR BioGRID; 16566; 2.
DR STRING; 3702.AT5G14380.1; -.
DR PaxDb; Q9LY91; -.
DR EnsemblPlants; AT5G14380.1; AT5G14380.1; AT5G14380.
DR GeneID; 831289; -.
DR Gramene; AT5G14380.1; AT5G14380.1; AT5G14380.
DR KEGG; ath:AT5G14380; -.
DR Araport; AT5G14380; -.
DR TAIR; locus:2145713; AT5G14380.
DR eggNOG; ENOG502SDBC; Eukaryota.
DR HOGENOM; CLU_1878253_0_0_1; -.
DR InParanoid; Q9LY91; -.
DR OMA; PAADHEG; -.
DR PRO; PR:Q9LY91; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY91; baseline and differential.
DR Genevisible; Q9LY91; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010208; P:pollen wall assembly; IDA:UniProtKB.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Proteoglycan; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..126
FT /note="Classical arabinogalactan protein 6"
FT /id="PRO_0000268995"
FT PROPEP 127..150
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000268996"
FT REGION 19..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 126
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="T -> A (in Ref. 1; CAB42531)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="P -> T (in Ref. 1; CAB42531)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="T -> A (in Ref. 1; CAB42531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 14569 MW; 80ABF4AE89A28F8A CRC64;
MARQFVVLVL LTLTIATAFA ADAPSASPKK SPSPTAAPTK APTATTKAPS APTKAPAAAP
KSSSASSPKA SSPAAEGPVP EDDYSASSPS DSAEAPTVSS PPAPTPDSTS AADGPSDGPT
AESPKSGAVT TAKFSVVGTV ATVGFFFFSF
