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INVB_ARATH
ID   INVB_ARATH              Reviewed;         571 AA.
AC   Q9SW48; B9DHG6;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Probable alkaline/neutral invertase B {ECO:0000305};
DE            Short=A/N-INVB {ECO:0000303|PubMed:21441406};
DE            EC=3.2.1.26 {ECO:0000250|UniProtKB:Q9FXA8};
GN   Name=INVB {ECO:0000303|PubMed:21441406};
GN   OrderedLocusNames=At4g34860 {ECO:0000312|Araport:AT4G34860};
GN   ORFNames=T11I11.100 {ECO:0000312|EMBL:CAB45447.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=21441406; DOI=10.1093/jxb/err069;
RA   Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W.,
RA   Rolland F., Van den Ende W.;
RT   "Exploring the neutral invertase-oxidative stress defence connection in
RT   Arabidopsis thaliana.";
RL   J. Exp. Bot. 62:3849-3862(2011).
CC   -!- FUNCTION: Invertase that cleaves sucrose into glucose and fructose.
CC       {ECO:0000250|UniProtKB:Q9LQF2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC         residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC         Evidence={ECO:0000250|UniProtKB:Q9FXA8};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC       {ECO:0000305}.
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DR   EMBL; AL079347; CAB45447.1; -; Genomic_DNA.
DR   EMBL; AL161586; CAB80203.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86429.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86430.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67946.1; -; Genomic_DNA.
DR   EMBL; AY050417; AAK91433.1; -; mRNA.
DR   EMBL; BT002695; AAO11611.1; -; mRNA.
DR   EMBL; AK317518; BAH20183.1; -; mRNA.
DR   PIR; T10232; T10232.
DR   RefSeq; NP_001031790.1; NM_001036713.3.
DR   RefSeq; NP_001329737.1; NM_001342308.1.
DR   RefSeq; NP_195212.1; NM_119652.3.
DR   AlphaFoldDB; Q9SW48; -.
DR   SMR; Q9SW48; -.
DR   STRING; 3702.AT4G34860.1; -.
DR   CAZy; GH100; Glycoside Hydrolase Family 100.
DR   iPTMnet; Q9SW48; -.
DR   PaxDb; Q9SW48; -.
DR   PRIDE; Q9SW48; -.
DR   ProteomicsDB; 247032; -.
DR   EnsemblPlants; AT4G34860.1; AT4G34860.1; AT4G34860.
DR   EnsemblPlants; AT4G34860.2; AT4G34860.2; AT4G34860.
DR   EnsemblPlants; AT4G34860.3; AT4G34860.3; AT4G34860.
DR   GeneID; 829638; -.
DR   Gramene; AT4G34860.1; AT4G34860.1; AT4G34860.
DR   Gramene; AT4G34860.2; AT4G34860.2; AT4G34860.
DR   Gramene; AT4G34860.3; AT4G34860.3; AT4G34860.
DR   KEGG; ath:AT4G34860; -.
DR   Araport; AT4G34860; -.
DR   TAIR; locus:2116870; AT4G34860.
DR   eggNOG; ENOG502QPS0; Eukaryota.
DR   HOGENOM; CLU_020846_1_1_1; -.
DR   InParanoid; Q9SW48; -.
DR   OMA; CLEEDKQ; -.
DR   OrthoDB; 331795at2759; -.
DR   PhylomeDB; Q9SW48; -.
DR   PRO; PR:Q9SW48; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SW48; baseline and differential.
DR   Genevisible; Q9SW48; AT.
DR   GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR   GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR024746; Glyco_hydro_100.
DR   PANTHER; PTHR31916; PTHR31916; 1.
DR   Pfam; PF12899; Glyco_hydro_100; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..571
FT                   /note="Probable alkaline/neutral invertase B"
FT                   /id="PRO_0000431498"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18433157"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         94
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   CONFLICT        158
FT                   /note="M -> V (in Ref. 4; BAH20183)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   571 AA;  65037 MW;  E10CA0EC5CAB9941 CRC64;
     MSSFNLSVDV NQNGNIKNVD SLSTLDDIDD IDFAKLLEKP RPLNIDRLRS LDERSLTELT
     GSPQLRNADN ASRAPDHADY VISPSFGRRS GFNTPRSQPG FESHPMVGEA WDALRRSMVY
     FRGQPVGTIA AVDNSEEKLN YDQVFVRDFV PSALAFLMNG EPDIVKNFLL KTLRLQSWEK
     KIDRFQLGEG VMPASFKVFH DPVRNHETLI ADFGESAIGR VAPVDSGFWW IILLRAYTKS
     TGDSSLADMP ECQKGIRLIL SLCLSEGFDT FPTLLCADGC CMIDRRMGVY GYPIEIQALF
     FMALRCALLL LKHDGEGKEM VEQIVKRLHA LSYHMRSYFW LDLKQLNDIY RYKTEEYSHT
     AVNKFNVIPD SLPEWVFDFM PPHGGFFIGN VSPARMDFRW FALGNCIAIL SSLATPEQST
     AIMDLIESRW EELVGEMPLK VCYPAIESHE WRIVTGCDPK NTRWSYHNGG SWPVLLWLLT
     AACIKTGRPQ IARRAIEVAE ARLHKDHWPE YYDGKVGRYV GKQSRKNQTW SVAGYLVAKM
     MLEDPSHVGM VCLEEDKQMK PVMRRSNSWT C
 
 
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