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INVC_ARATH
ID   INVC_ARATH              Reviewed;         664 AA.
AC   B9DFA8; Q0WWN9; Q7Y209; Q9C8Z1;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Alkaline/neutral invertase C, mitochondrial {ECO:0000305};
DE            Short=A/N-INVC {ECO:0000303|PubMed:21441406};
DE            EC=3.2.1.26 {ECO:0000269|PubMed:23135328};
DE   Flags: Precursor;
GN   Name=INVC {ECO:0000303|PubMed:21441406};
GN   OrderedLocusNames=At3g06500 {ECO:0000312|Araport:AT3G06500};
GN   ORFNames=F5E6.17 {ECO:0000312|EMBL:AAG51337.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=23135328; DOI=10.1007/s00425-012-1794-8;
RA   Martin M.L., Lechner L., Zabaleta E.J., Salerno G.L.;
RT   "A mitochondrial alkaline/neutral invertase isoform (A/N-InvC) functions in
RT   developmental energy-demanding processes in Arabidopsis.";
RL   Planta 237:813-822(2013).
CC   -!- FUNCTION: Mitochondrial invertase that cleaves sucrose into glucose and
CC       fructose and is involved in the regulation of aerial tissue development
CC       and floral transition. May be modulating hormone balance in relation to
CC       the radicle emergence. {ECO:0000269|PubMed:23135328}.
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:0000269|PubMed:23135328};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:23135328};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23135328}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, roots and flowers.
CC       {ECO:0000269|PubMed:23135328}.
CC   -!- DISRUPTION PHENOTYPE: Delayed germination time, reduced plant growth,
CC       delayed flowering and reduced oxygen consumption in the dark.
CC       {ECO:0000269|PubMed:23135328}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51337.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC020580; AAG51337.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE74403.1; -; Genomic_DNA.
DR   EMBL; BT008650; AAP40464.1; -; mRNA.
DR   EMBL; AK316698; BAH19425.1; -; mRNA.
DR   EMBL; AK226304; BAE98459.1; -; mRNA.
DR   RefSeq; NP_187302.2; NM_111526.4.
DR   AlphaFoldDB; B9DFA8; -.
DR   SMR; B9DFA8; -.
DR   STRING; 3702.AT3G06500.1; -.
DR   CAZy; GH100; Glycoside Hydrolase Family 100.
DR   iPTMnet; B9DFA8; -.
DR   PaxDb; B9DFA8; -.
DR   PRIDE; B9DFA8; -.
DR   ProteomicsDB; 247217; -.
DR   EnsemblPlants; AT3G06500.1; AT3G06500.1; AT3G06500.
DR   GeneID; 819828; -.
DR   Gramene; AT3G06500.1; AT3G06500.1; AT3G06500.
DR   KEGG; ath:AT3G06500; -.
DR   Araport; AT3G06500; -.
DR   TAIR; locus:2084329; AT3G06500.
DR   eggNOG; ENOG502QT23; Eukaryota.
DR   HOGENOM; CLU_020846_0_0_1; -.
DR   InParanoid; B9DFA8; -.
DR   OMA; YPTMLVP; -.
DR   OrthoDB; 373994at2759; -.
DR   PRO; PR:B9DFA8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; B9DFA8; baseline and differential.
DR   Genevisible; B9DFA8; AT.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR   GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:TAIR.
DR   GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR   GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR   GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
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; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..664
FT                   /note="Alkaline/neutral invertase C, mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000431499"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   MOD_RES         657
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT   CONFLICT        9
FT                   /note="V -> I (in Ref. 5; BAE98459)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="V -> F (in Ref. 3; AAP40464)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   664 AA;  74722 MW;  14E8108C181727D0 CRC64;
     MNSRSCICVS AMKPCCRFLI SFRSSSLFGF SPPNSGKFIN SSKLHCTKID SRSIRSGIHC
     RRIVLDRNAF CDSDSISWGG GGSRVLRARG SSRGRGRGVL VIPHVASDFR NYSTSSLDSH
     VNDKSFESMF VKPLVFKEVE KTEGIPKRER GNVGGGKDAN FGNVGVRKET ERCLSQTEVE
     KEAWKLLRGA VVNYCGFPVG TVAANDPGDT QTLNYDQVFI RDFVPSAYAF MLDGEGEIVR
     NFLLHTLQLQ SWEKTVDCHS PGPGLMPASF KVKSAPLEGN DGSFEEFLDP DFGGSAIGRV
     SPVDSGLWWI ILLRAYGKLT GDYTLQERID VQTGIKLILK LCLADGFDMF PTLLVTDGSC
     MVDRRMGIHG HPLEIQALFY SALRCAREML IVNDGTKSLV TAVNNRLSAL SFHIREYYWV
     DIKKINEIYR YNTEEYSADA TNKFNIYPEQ IPTWLVDWIP DKGGYFIGNL QPAHMDFRFF
     TLGNLWAVIS SLGNQEQNEG VMTLIEEKWD DLVANMPLKI CFPALEKDEW RIITGSDPKN
     TPWSYHNGGS WPTLLWQFTL ACIKMGKLEL AKKAVAVAEK RLKEDEWPEY YDTKSGRFVG
     KQSRLYQTWT IAGFLAAKKL IEQPEKASLL FWEEDYQLLE TCVCGLSKSS GRKNKCSRFT
     PPRS
 
 
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