ASD2_ARATH
ID ASD2_ARATH Reviewed; 674 AA.
AC Q8VZR2; Q9XH04;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-L-arabinofuranosidase 2;
DE Short=AtASD2;
DE EC=3.2.1.55;
DE AltName: Full=Beta-D-xylosidase;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=ASD2; Synonyms=ARAF2; OrderedLocusNames=At5g26120; ORFNames=T1N24.13;
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], TISSUE SPECIFICITY, AND INDUCTION BY HORMONES.
RC STRAIN=cv. Columbia;
RX PubMed=14512381; DOI=10.1093/jxb/erg269;
RA Fulton L.M., Cobbett C.S.;
RT "Two alpha-L-arabinofuranosidase genes in Arabidopsis thaliana are
RT differentially expressed during vegetative growth and flower development.";
RL J. Exp. Bot. 54:2467-2477(2003).
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18344421; DOI=10.1104/pp.107.110023;
RA Chavez Montes R.A., Ranocha P., Martinez Y., Minic Z., Jouanin L.,
RA Marquis M., Saulnier L., Fulton L.M., Cobbett C.S., Bitton F., Renou J.-P.,
RA Jauneau A., Goffner D.;
RT "Cell wall modifications in Arabidopsis plants with altered alpha-L-
RT arabinofuranosidase activity.";
RL Plant Physiol. 147:63-77(2008).
CC -!- FUNCTION: May be involved in the coordinated dissolution of the cell
CC wall matrix during abscission and in the secondary cell wall formation
CC in xylem vessels. {ECO:0000269|PubMed:18344421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High expression in flowers, siliques and stems.
CC Observed in the vasculature of older root tissue, at the tip of anthers
CC and in the petal blade of fully developed flowers, in floral abscission
CC zones and in silique replum tissue. Expressed in the cambium and
CC phloem, but not in the xylem or in the vascular system of floral
CC tissues. {ECO:0000269|PubMed:14512381, ECO:0000269|PubMed:18344421}.
CC -!- INDUCTION: Not induced by hormones or during leaf senescence.
CC {ECO:0000269|PubMed:14512381}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, even in asd1 and asd2
CC double mutant. {ECO:0000269|PubMed:18344421}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY243510; AAO92262.1; -; mRNA.
DR EMBL; AF149413; AAD40132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93527.1; -; Genomic_DNA.
DR EMBL; AY063925; AAL36281.1; -; mRNA.
DR EMBL; BT006062; AAP04047.1; -; mRNA.
DR RefSeq; NP_197984.2; NM_122513.4.
DR AlphaFoldDB; Q8VZR2; -.
DR SMR; Q8VZR2; -.
DR STRING; 3702.AT5G26120.1; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR PaxDb; Q8VZR2; -.
DR PRIDE; Q8VZR2; -.
DR ProteomicsDB; 246848; -.
DR EnsemblPlants; AT5G26120.1; AT5G26120.1; AT5G26120.
DR GeneID; 832681; -.
DR Gramene; AT5G26120.1; AT5G26120.1; AT5G26120.
DR KEGG; ath:AT5G26120; -.
DR Araport; AT5G26120; -.
DR TAIR; locus:2180652; AT5G26120.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_3_0_1; -.
DR InParanoid; Q8VZR2; -.
DR OMA; PMVDEHY; -.
DR OrthoDB; 366915at2759; -.
DR PhylomeDB; Q8VZR2; -.
DR BioCyc; ARA:AT5G26120-MON; -.
DR PRO; PR:Q8VZR2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZR2; baseline and differential.
DR Genevisible; Q8VZR2; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IBA:GO_Central.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Extracellular matrix; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..674
FT /note="Alpha-L-arabinofuranosidase 2"
FT /id="PRO_0000384372"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 75439 MW; C9FD37B9F397890B CRC64;
MDMETSWRFL RSVCLLSFIL GSFSVYQTLC LVDAQEDAIV TLQVDASNVT RRPIPETLFG
IFFEEINHAG AGGLWAELVS NRGFEAGGQI IPSNIWPWSI IGDESSIYVV TDRSSCFERN
KIALRMEVLC DSNSCPLGGV GVYNPGYWGM NIEEGKKYKV VLYVRSTGDI DVSVSFTSSN
GSVTLASENI IALASDLLNW TKKEMLLEAN GTDNGARLQF TTTKKGSIWF DQVSAMPMDT
YKGHGFRNDL FQMMVDLKPR FIRFPGGCFV EGDWLGNAFR WKETVRAWEE RPGHYGDVWK
YWTDDGLGHF EFFQLAEDLG ASPIWVFNNG ISHNDQVETK NVMPFVQEAI DGIEFARGDS
NSTWGSVRAA MGHPEPFELK YVAVGNEDCF KSYYRGNYLE FYNAIKKAYP DIKIISNCDA
SAKPLDHPAD YFDYHIYTLA RDLFSKSHDF DNTPRNGPKA FVSEYAVNKA DAKNGNLLAA
LGEAAFLLGL EKNSDIVEMV SYAPLFVNTN DRRWIPDAIV FNSSHLYGTP SYWVQHFFTE
SSGATLLNST LKGKTSSVEA SAISFQTNGK DYIQIKAVNF GEQSVNLKVA VTGLMAKFYG
SKKKVLTSAS VMDENSFSNP NMIVPQESLL EMTEQEDLMF VLPPHSFSSF DLLTESENVI
KMPISDSYKK TSTM
