EXL6_ARATH
ID EXL6_ARATH Reviewed; 343 AA.
AC Q93X94; Q9LQS3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GDSL esterase/lipase EXL6;
DE EC=3.1.1.-;
DE AltName: Full=Family II extracellular lipase 6;
DE Short=Family II lipase EXL6;
DE Flags: Precursor;
GN Name=EXL6; OrderedLocusNames=At1g75930; ORFNames=T4O12.260;
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 75-87; 255-269 AND 326-340,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Pollen;
RX PubMed=11431566; DOI=10.1126/science.1060972;
RA Mayfield J.A., Fiebig A., Johnstone S.E., Preuss D.;
RT "Gene families from the Arabidopsis thaliana pollen coat proteome.";
RL Science 292:2482-2485(2001).
RN [2]
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 [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 REVIEW.
RX PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
RA Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
RT "GDSL family of serine esterases/lipases.";
RL Prog. Lipid Res. 43:534-552(2004).
RN [5]
RP GENE FAMILY.
RX PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
RA Ling H.;
RT "Sequence analysis of GDSL lipase gene family in Arabidopsis thaliana.";
RL Pak. J. Biol. Sci. 11:763-767(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RA Sassa M., Saito H., Nakamura K., Ishiguro S.;
RT "Function of Arabidopsis EXL4 and EXL6 to form pollen coats.";
RL (In) Proceedings of the 19th international conference on Arabidopsis
RL research, abstract#9044, Montreal (2008).
CC -!- FUNCTION: Required for the formation of pollen coats and male
CC fertility. {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, pollen coat {ECO:0000269|PubMed:11431566, ECO:0000269|Ref.6}.
CC Note=Localized in small granules in the tapetal cells.
CC -!- TISSUE SPECIFICITY: Flower buds and pollen.
CC {ECO:0000269|PubMed:11431566}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in tapetal cells at the flower
CC developmental stage 10 to middle 12, where the components of pollen
CC coat are synthesized actively. {ECO:0000269|Ref.6}.
CC -!- DISRUPTION PHENOTYPE: Reduced pollen fertility. Pollen grain exhibit a
CC partial formation of coat and impaired water absorption and germination
CC capacities. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26759.2; Type=Erroneous gene model prediction; Note=The predicted gene At1g75930 has been split into 2 genes: At1g75930 and At1g75940.; Evidence={ECO:0000305};
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DR EMBL; AY028614; AAK30021.1; -; mRNA.
DR EMBL; AC007396; AAF26759.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35778.1; -; Genomic_DNA.
DR PIR; B96788; B96788.
DR RefSeq; NP_177721.1; NM_106243.4.
DR AlphaFoldDB; Q93X94; -.
DR SMR; Q93X94; -.
DR STRING; 3702.AT1G75930.1; -.
DR PaxDb; Q93X94; -.
DR PRIDE; Q93X94; -.
DR ProteomicsDB; 222267; -.
DR EnsemblPlants; AT1G75930.1; AT1G75930.1; AT1G75930.
DR GeneID; 843926; -.
DR Gramene; AT1G75930.1; AT1G75930.1; AT1G75930.
DR KEGG; ath:AT1G75930; -.
DR Araport; AT1G75930; -.
DR TAIR; locus:2204425; AT1G75930.
DR eggNOG; ENOG502R619; Eukaryota.
DR HOGENOM; CLU_015101_0_1_1; -.
DR InParanoid; Q93X94; -.
DR OMA; WNYDYKI; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q93X94; -.
DR BioCyc; ARA:AT1G75930-MON; -.
DR PRO; PR:Q93X94; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93X94; baseline and differential.
DR Genevisible; Q93X94; AT.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0070505; C:pollen coat; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; ISS:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Extracellular matrix; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..343
FT /note="GDSL esterase/lipase EXL6"
FT /id="PRO_0000367333"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 259
FT /note="Y -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38596 MW; 1EA9C347B109EEE6 CRC64;
MFRGKIFVLS LFSIYVLSSA AEKNTSFSAL FAFGDSVLDT GNNNFLLTLL KGNYWPYGLS
FDYKFPTGRF GNGRVFTDIV AEGLQIKRLV PAYSKIRRIS SEDLKTGVCF ASGGSGIDDL
TSRTLRVLSA GDQVKDFKDY LKKLRRVVKR KKKVKEIVSN AVFLISEGNN DLGYFVAPAL
LRLQSTTTYT SKMVVWTRKF LKDLYDLGAR KFAVMGVMPV GCLPIHRASF GGVFGWCNFL
LNRITEDFNM KLQKGLTSYA VEYDFKDAKF VYVDIYGTLM DLVKNPMAYG FTEAKKACCC
MPNAIIPCFH PDKYVFYDFA HPSQKAYEVI SKPIVYQIAK GLA
