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LRX2_ARATH
ID   LRX2_ARATH              Reviewed;         786 AA.
AC   O48809; F4HYS8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Leucine-rich repeat extensin-like protein 2;
DE            Short=AtLRX2;
DE            Short=LRR/EXTENSIN2;
DE   AltName: Full=Cell wall hydroxyproline-rich glycoprotein;
DE   Flags: Precursor;
GN   Name=LRX2; OrderedLocusNames=At1g62440; ORFNames=F24O1.18, T3P18.1;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ETHYLENE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=12834403; DOI=10.1046/j.1365-313x.2003.01784.x;
RA   Baumberger N., Steiner M., Ryser U., Keller B., Ringli C.;
RT   "Synergistic interaction of the two paralogous Arabidopsis genes LRX1 and
RT   LRX2 in cell wall formation during root hair development.";
RL   Plant J. 35:71-81(2003).
RN   [4]
RP   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. Together with LRX2,
CC       component of the extracellular mechanism regulating root hair
CC       morphogenesis and elongation. {ECO:0000269|PubMed:12834403}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000305|PubMed:12834403}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots, also present in stems at
CC       low levels. In roots, confined to differentiation zones, the collet,
CC       and meristematic cells of tips. {ECO:0000269|PubMed:12834403}.
CC   -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:12834403}.
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}.
CC   -!- DISRUPTION PHENOTYPE: No visible effect. Enhances LRX1 disruption
CC       phenotype when associated with LRX1 disruption; frequent rupture of
CC       root hairs soon after their initiation. {ECO:0000269|PubMed:12834403}.
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DR   EMBL; AC003113; AAF70841.1; -; Genomic_DNA.
DR   EMBL; AC005698; AAD43602.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33968.2; -; Genomic_DNA.
DR   PIR; T01456; T01456.
DR   RefSeq; NP_176434.2; NM_104924.2.
DR   PDB; 6QXP; X-ray; 3.20 A; A/B/C/D/E/F/G/H=29-385.
DR   PDBsum; 6QXP; -.
DR   AlphaFoldDB; O48809; -.
DR   SMR; O48809; -.
DR   STRING; 3702.AT1G62440.1; -.
DR   PaxDb; O48809; -.
DR   PRIDE; O48809; -.
DR   ProteomicsDB; 238738; -.
DR   EnsemblPlants; AT1G62440.1; AT1G62440.1; AT1G62440.
DR   GeneID; 842542; -.
DR   Gramene; AT1G62440.1; AT1G62440.1; AT1G62440.
DR   KEGG; ath:AT1G62440; -.
DR   Araport; AT1G62440; -.
DR   eggNOG; ENOG502QQD2; Eukaryota.
DR   HOGENOM; CLU_000288_23_4_1; -.
DR   InParanoid; O48809; -.
DR   OMA; NYHHSAN; -.
DR   OrthoDB; 826997at2759; -.
DR   PRO; PR:O48809; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O48809; baseline and differential.
DR   Genevisible; O48809; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Cell wall biogenesis/degradation;
KW   Developmental protein; Glycoprotein; Hydroxylation; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..786
FT                   /note="Leucine-rich repeat extensin-like protein 2"
FT                   /id="PRO_0000395462"
FT   REPEAT          100..124
FT                   /note="LRR 1"
FT   REPEAT          125..147
FT                   /note="LRR 2"
FT   REPEAT          149..172
FT                   /note="LRR 3"
FT   REPEAT          173..196
FT                   /note="LRR 4"
FT   REPEAT          198..219
FT                   /note="LRR 5"
FT   REPEAT          221..243
FT                   /note="LRR 6"
FT   REPEAT          244..267
FT                   /note="LRR 7"
FT   REPEAT          268..291
FT                   /note="LRR 8"
FT   REPEAT          292..315
FT                   /note="LRR 9"
FT   REGION          352..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..786
FT                   /note="Contains the Ser-Pro(4) repeats"
FT   REGION          390..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..736
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   HELIX           51..66
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          100..107
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           119..123
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          158..164
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          182..188
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           191..195
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           237..243
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           262..266
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          277..282
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           286..290
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   HELIX           310..314
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   TURN            361..363
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   TURN            367..369
FT                   /evidence="ECO:0007829|PDB:6QXP"
FT   STRAND          374..379
FT                   /evidence="ECO:0007829|PDB:6QXP"
SQ   SEQUENCE   786 AA;  85485 MW;  3F88E6843946E8CF CRC64;
     MLLFPSTSLR LFFFLFLLFS SCFLQIRGDD DDDDISDDNI KVDPSLKFEN PSLRQAYIAL
     QSWKQAIFSD PFNFTANWNG SDVCSYNGIF CAPSPSSPKT RVVAGIDLNH ADMAGYLPRE
     LGLLTDLALF HLNSNRFCGE VPLTFKHMKL LFELDLSNNR FVGKFPNVVL SLPSLKFLDL
     RYNEFEGSIP SKLFDKELDA IFLNHNRFMF GIPENMGNSP VSALVLADND LGGCIPGSIG
     LMGKTLNEII LSNDNLTGCL PPQIGNLKNV TVFDISFNRL SGPLPSSIGN MKSLEQLNVA
     NNRFTGVIPS SICQLSNLEN FTYSSNFFTG DAPRCVALLG DNVVVNGSMN CIDGKEDQRS
     SKECSSPASR SVDCSKFGCN NFFSPPPPSF KMSPTVRVLP PPPPSSKMSP TFRATPPPPS
     SKMSPSFRAT PPPPSSKMSP SFRATPPPPS SKMSPSVKAY PPPPPPPEYE PSPPPPSSEM
     SPSVRAYPPP PPLSPPPPSP PPPYIYSSPP PPSPSPPPPY IYSSPPPVVN CPPTTQSPPP
     PKYEQTPSPR EYYPSPSPPY YQYTSSPPPP TYYATQSPPP PPPPTYYAVQ SPPPPPPVYY
     PPVTASPPPP PVYYTPVIQS PPPPPVYYSP VTQSPPPPPP VYYPPVTQSP PPSPVYYPPV
     TQSPPPPPVY YLPVTQSPPP PSPVYYPPVA KSPPPPSPVY YPPVTQSPPP PSTPVEYHPP
     ASPNQSPPPE YQSPPPKGCN DSPSNDHHYQ TPTPPSLPPP YYEDTPLPPI RGVSYASPPP
     PSIPYY
 
 
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