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BGA17_ARATH
ID   BGA17_ARATH             Reviewed;         697 AA.
AC   Q93Z24; Q2V4C9; Q9SSM8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Beta-galactosidase 17;
DE            Short=Lactase 17;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL17; OrderedLocusNames=At1g72990; ORFNames=F3N23.19;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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.
RX   PubMed=16267099; DOI=10.1093/pcp/pci223;
RA   Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT   "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 47:55-63(2006).
RN   [5]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17466346; DOI=10.1016/j.phytochem.2007.03.021;
RA   Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P.,
RA   Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT   family 35.";
RL   Phytochemistry 68:1510-1520(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q93Z24-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q93Z24-2; Sequence=VSP_026468;
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher expression levels in roots
CC       and siliques. {ECO:0000269|PubMed:16267099,
CC       ECO:0000269|PubMed:17466346}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC008017; AAD55646.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35400.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35401.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58944.1; -; Genomic_DNA.
DR   EMBL; AY058198; AAL25611.1; -; mRNA.
DR   EMBL; AY142008; AAM98272.1; -; mRNA.
DR   PIR; C96755; C96755.
DR   RefSeq; NP_001031273.1; NM_001036196.2. [Q93Z24-2]
DR   RefSeq; NP_001321343.1; NM_001334560.1. [Q93Z24-1]
DR   RefSeq; NP_565051.1; NM_105957.3. [Q93Z24-1]
DR   AlphaFoldDB; Q93Z24; -.
DR   SMR; Q93Z24; -.
DR   STRING; 3702.AT1G72990.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; Q93Z24; -.
DR   PRIDE; Q93Z24; -.
DR   ProteomicsDB; 240657; -. [Q93Z24-1]
DR   EnsemblPlants; AT1G72990.1; AT1G72990.1; AT1G72990. [Q93Z24-1]
DR   EnsemblPlants; AT1G72990.2; AT1G72990.2; AT1G72990. [Q93Z24-2]
DR   EnsemblPlants; AT1G72990.4; AT1G72990.4; AT1G72990. [Q93Z24-1]
DR   GeneID; 843630; -.
DR   Gramene; AT1G72990.1; AT1G72990.1; AT1G72990. [Q93Z24-1]
DR   Gramene; AT1G72990.2; AT1G72990.2; AT1G72990. [Q93Z24-2]
DR   Gramene; AT1G72990.4; AT1G72990.4; AT1G72990. [Q93Z24-1]
DR   KEGG; ath:AT1G72990; -.
DR   Araport; AT1G72990; -.
DR   TAIR; locus:2032667; AT1G72990.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   InParanoid; Q93Z24; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q93Z24; -.
DR   BioCyc; ARA:AT1G72990-MON; -.
DR   PRO; PR:Q93Z24; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q93Z24; baseline and differential.
DR   Genevisible; Q93Z24; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..697
FT                   /note="Beta-galactosidase 17"
FT                   /id="PRO_0000293096"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        301
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..92
FT                   /note="MAMTSWPSTGRQRRHQLASMLLLVLVVVGIYVPVFALLPSLSYTPQSLPSAI
FT                   PQDEKMISRKFYIKDDNFWKDGNRFQIIGGDLHYFRVLPE -> MTISGKMGIVFRSLV
FT                   VICITFVFFQRLWMQ (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_026468"
SQ   SEQUENCE   697 AA;  78640 MW;  7A13124157BCE54A CRC64;
     MAMTSWPSTG RQRRHQLASM LLLVLVVVGI YVPVFALLPS LSYTPQSLPS AIPQDEKMIS
     RKFYIKDDNF WKDGNRFQII GGDLHYFRVL PEYWEDRLLR ANALGLNTIQ VYVPWNLHEP
     KPGKMVFEGI GDLVSFLKLC EKLDFLVMLR AGPYICGEWD LGGFPAWLLA VKPRLQLRTS
     DPVYLKLVER WWDVLLPKVF PLLYSNGGPV IMVQIENEYG SYGNDKAYLR KLVSMARGHL
     GDDIIVYTTD GGTKETLDKG TVPVADVYSA VDFSTGDDPW PIFKLQKKFN APGRSPPLSS
     EFYTGWLTHW GEKITKTDAE FTAASLEKIL SRNGSAVLYM VHGGTNFGFY NGANTGSEES
     DYKPDLTSYD YDAPIKESGD IDNPKFQALQ RVIKKYNASP HPISPSNKQR KAYGSIKMQM
     TTSLFDLVRM TDPADVITSA NPISMESVGQ MFGFLLYESS YIAKKSGNTL RIPKVHDRAQ
     VFVSCLSQDV DVGVLRYIGT TERWNNQPIS LPTIECTTNT SLFILVENMG RVNYGPYIFD
     DKGILSSVYL DGQILHGWKM IPIPFHNLNQ EPNLTFEMQH TKNRSKKFEL TNDVGRKEPA
     LFAGEFSINS EEEIKDTYLS FNGWGKGVAF VNEFNIGRYW PSVGPQCNLY VPAPLLKRGK
     NTLVVFELES PHLELSLEAV DHQDFTCGSN VSKVNQL
 
 
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