EXL5_ARATH
ID EXL5_ARATH Reviewed; 358 AA.
AC Q94CH5; A8MR69; B3H6N8; Q1PFC8; Q9LQS4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=GDSL esterase/lipase EXL5;
DE EC=3.1.1.-;
DE AltName: Full=Family II extracellular lipase 5;
DE Short=Family II lipase EXL5;
DE Flags: Precursor;
GN Name=EXL5; OrderedLocusNames=At1g75920; ORFNames=T4O12.14;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-353 (ISOFORM 1), AND TISSUE SPECIFICITY.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-343 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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 [6]
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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q94CH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94CH5-2; Sequence=VSP_036684;
CC Name=3;
CC IsoId=Q94CH5-3; Sequence=VSP_036685;
CC Name=4;
CC IsoId=Q94CH5-4; Sequence=VSP_036683, VSP_036684;
CC -!- TISSUE SPECIFICITY: Flower buds. {ECO:0000269|PubMed:11431566}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26758.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007396; AAF26758.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35775.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35776.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35777.1; -; Genomic_DNA.
DR EMBL; AY028613; AAK30020.1; -; mRNA.
DR EMBL; DQ446435; ABE65778.1; -; mRNA.
DR RefSeq; NP_001077830.1; NM_001084361.2. [Q94CH5-2]
DR RefSeq; NP_001077831.1; NM_001084362.1. [Q94CH5-3]
DR RefSeq; NP_001117605.1; NM_001124133.2. [Q94CH5-4]
DR RefSeq; NP_565122.1; NM_106242.2.
DR AlphaFoldDB; Q94CH5; -.
DR BioGRID; 29144; 1.
DR iPTMnet; Q94CH5; -.
DR PaxDb; Q94CH5; -.
DR PeptideAtlas; Q94CH5; -.
DR PRIDE; Q94CH5; -.
DR EnsemblPlants; AT1G75920.1; AT1G75920.1; AT1G75920.
DR EnsemblPlants; AT1G75920.2; AT1G75920.2; AT1G75920. [Q94CH5-2]
DR EnsemblPlants; AT1G75920.3; AT1G75920.3; AT1G75920. [Q94CH5-3]
DR EnsemblPlants; AT1G75920.4; AT1G75920.4; AT1G75920. [Q94CH5-4]
DR GeneID; 843925; -.
DR Gramene; AT1G75920.1; AT1G75920.1; AT1G75920.
DR Gramene; AT1G75920.2; AT1G75920.2; AT1G75920. [Q94CH5-2]
DR Gramene; AT1G75920.3; AT1G75920.3; AT1G75920. [Q94CH5-3]
DR Gramene; AT1G75920.4; AT1G75920.4; AT1G75920. [Q94CH5-4]
DR KEGG; ath:AT1G75920; -.
DR Araport; AT1G75920; -.
DR InParanoid; Q94CH5; -.
DR OMA; HERTIPL; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q94CH5; -.
DR PRO; PR:Q94CH5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94CH5; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..358
FT /note="GDSL esterase/lipase EXL5"
FT /id="PRO_0000367332"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..51
FT /note="MFRKKMLVLALFSIYFLSIEAVRNESFPALLAFGDSMVDTGNNNYLLTLMK
FT -> MACALRGPIETISAHQTMTSPLP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_036683"
FT VAR_SEQ 81..95
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_036684"
FT VAR_SEQ 82..127
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036685"
SQ SEQUENCE 358 AA; 39946 MW; BB410768A8EBF1FF CRC64;
MFRKKMLVLA LFSIYFLSIE AVRNESFPAL LAFGDSMVDT GNNNYLLTLM KGNYWPYGWN
FDSKIPTGRF GNGRVFSDVV GIILKSSLQC FFVISAEGLG IKRIVPAYRK LYIAPSDLKT
GVSFASGGAG VDPVTSKLLR VLSPADQVKD FKGYKRKLKG VVGRSKAKKI VANSVILVSE
GNNDIGITYA IHDAGMRLMT PKVYTSKLVG WNKKFIKDLY DHGARKFAVM GVIPLGCLPM
SRLIFGGFFV WCNFLANTIS EDYNKKLKSG IKSWRGASDF RGARFVYVDM YNSLMDVINN
HRKYGFTHEK NGCCCMLTAI VPCSNPDKYV FYDFAHPSEK AYKTIAKKLV EDIKTGLA
