PLRX1_ARATH
ID PLRX1_ARATH Reviewed; 956 AA.
AC Q9LJ64; Q8RWX5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Pollen-specific leucine-rich repeat extensin-like protein 1;
DE Short=AtPEX1;
DE Short=Pollen-specific LRR/EXTENSIN1;
DE AltName: Full=Cell wall hydroxyproline-rich glycoprotein;
DE Flags: Precursor;
GN Name=PEX1; OrderedLocusNames=At3g19020; ORFNames=K13E13.23;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-712.
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 [4]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12644681; DOI=10.1104/pp.102.014928;
RA Baumberger N., Doesseger B., Guyot R., Diet A., Parsons R.L., Clark M.A.,
RA Simmons M.P., Bedinger P., Goff S.A., Ringli C., Keller B.;
RT "Whole-genome comparison of leucine-rich repeat extensins in Arabidopsis
RT and rice. A conserved family of cell wall proteins form a vegetative and a
RT reproductive clade.";
RL Plant Physiol. 131:1313-1326(2003).
CC -!- FUNCTION: Modulates cell morphogenesis by regulating cell wall
CC formation and assembly, and/or growth polarization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, stamen, pollen, and
CC pollinated carpels. {ECO:0000269|PubMed:12644681}.
CC -!- PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated on hydroxyprolines. {ECO:0000250}.
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DR EMBL; AP000735; BAB01698.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76184.1; -; Genomic_DNA.
DR EMBL; AY091043; AAM13864.1; -; mRNA.
DR RefSeq; NP_188532.2; NM_112788.3.
DR PDB; 6QWN; X-ray; 3.89 A; A/B/C/D/E=31-400.
DR PDB; 6TME; X-ray; 2.33 A; A/B=31-400.
DR PDBsum; 6QWN; -.
DR PDBsum; 6TME; -.
DR AlphaFoldDB; Q9LJ64; -.
DR SMR; Q9LJ64; -.
DR STRING; 3702.AT3G19020.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR PaxDb; Q9LJ64; -.
DR PRIDE; Q9LJ64; -.
DR ProteomicsDB; 236637; -.
DR EnsemblPlants; AT3G19020.1; AT3G19020.1; AT3G19020.
DR GeneID; 821435; -.
DR Gramene; AT3G19020.1; AT3G19020.1; AT3G19020.
DR KEGG; ath:AT3G19020; -.
DR Araport; AT3G19020; -.
DR TAIR; locus:2085889; AT3G19020.
DR eggNOG; ENOG502QRPA; Eukaryota.
DR HOGENOM; CLU_000288_23_3_1; -.
DR OMA; FGPHKNA; -.
DR OrthoDB; 725535at2759; -.
DR PRO; PR:Q9LJ64; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJ64; baseline and differential.
DR Genevisible; Q9LJ64; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005199; F:structural constituent of cell wall; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Hydroxylation; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..956
FT /note="Pollen-specific leucine-rich repeat extensin-like
FT protein 1"
FT /id="PRO_0000395468"
FT REPEAT 39..59
FT /note="LRR 1"
FT REPEAT 60..84
FT /note="LRR 2"
FT REPEAT 119..143
FT /note="LRR 3"
FT REPEAT 144..166
FT /note="LRR 4"
FT REPEAT 168..191
FT /note="LRR 5"
FT REPEAT 192..215
FT /note="LRR 6"
FT REPEAT 217..238
FT /note="LRR 7"
FT REPEAT 240..261
FT /note="LRR 8"
FT REPEAT 262..285
FT /note="LRR 9"
FT REPEAT 287..309
FT /note="LRR 10"
FT REPEAT 310..332
FT /note="LRR 11"
FT REGION 355..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..956
FT /note="Contains the Ser-Pro(4) repeats"
FT COMPBIAS 355..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 622
FT /note="R -> C (in Ref. 3; AAM13864)"
FT /evidence="ECO:0000305"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:6TME"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6TME"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:6TME"
SQ SEQUENCE 956 AA; 102823 MW; E34E185E63BB47C3 CRC64;
MTRRTMEKPF GCFLLLFCFT ISIFFYSAAA LTDEEASFLT RRQLLALSEN GDLPDDIEYE
VDLDLKFANN RLKRAYIALQ AWKKAFYSDP FNTAANWVGP DVCSYKGVFC APALDDPSVL
VVAGIDLNHA DIAGYLPPEL GLLTDVALFH VNSNRFCGVI PKSLSKLTLM YEFDVSNNRF
VGPFPTVALS WPSLKFLDIR YNDFEGKLPP EIFDKDLDAI FLNNNRFEST IPETIGKSTA
SVVTFAHNKF SGCIPKTIGQ MKNLNEIVFI GNNLSGCLPN EIGSLNNVTV FDASSNGFVG
SLPSTLSGLA NVEQMDFSYN KFTGFVTDNI CKLPKLSNFT FSYNFFNGEA QSCVPGSSQE
KQFDDTSNCL QNRPNQKSAK ECLPVVSRPV DCSKDKCAGG GGGGSNPSPK PTPTPKAPEP
KKEINPPNLE EPSKPKPEES PKPQQPSPKP ETPSHEPSNP KEPKPESPKQ ESPKTEQPKP
KPESPKQESP KQEAPKPEQP KPKPESPKQE SSKQEPPKPE ESPKPEPPKP EESPKPQPPK
QETPKPEESP KPQPPKQETP KPEESPKPQP PKQETPKPEE SPKPQPPKQE QPPKTEAPKM
GSPPLESPVP NDPYDASPIK KRRPQPPSPS TEETKTTSPQ SPPVHSPPPP PPVHSPPPPV
FSPPPPMHSP PPPVYSPPPP VHSPPPPPVH SPPPPVHSPP PPVHSPPPPV HSPPPPVHSP
PPPVHSPPPP VQSPPPPPVF SPPPPAPIYS PPPPPVHSPP PPVHSPPPPP VHSPPPPVHS
PPPPVHSPPP PVHSPPPPVH SPPPPSPIYS PPPPVFSPPP KPVTPLPPAT SPMANAPTPS
SSESGEISTP VQAPTPDSED IEAPSDSNHS PVFKSSPAPS PDSEPEVEAP VPSSEPEVEA
PKQSEATPSS SPPSSNPSPD VTAPPSEDND DGDNFILPPN IGHQYASPPP PMFPGY
