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CVIF1_ARATH
ID   CVIF1_ARATH             Reviewed;         205 AA.
AC   F4HWQ8; Q9C7Y8;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Cell wall / vacuolar inhibitor of fructosidase 1;
DE            Short=AtC/VIF1;
DE   Flags: Precursor;
GN   Name=C/VIF1; Synonyms=CIF1, VIF1; OrderedLocusNames=At1g47960;
GN   ORFNames=T2J15.13;
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 [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 2).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=14871666; DOI=10.1016/j.bbapap.2003.09.017;
RA   Rausch T., Greiner S.;
RT   "Plant protein inhibitors of invertases.";
RL   Biochim. Biophys. Acta 1696:253-261(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DISULFIDE BOND, GENE
RP   FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=15327983; DOI=10.1016/j.febslet.2004.07.062;
RA   Link M., Rausch T., Greiner S.;
RT   "In Arabidopsis thaliana, the invertase inhibitors AtC/VIF1 and 2 exhibit
RT   distinct target enzyme specificities and expression profiles.";
RL   FEBS Lett. 573:105-109(2004).
CC   -!- FUNCTION: Inhibits fructosidases from vacuoles (vacuolar invertase VI).
CC       {ECO:0000269|PubMed:14871666, ECO:0000269|PubMed:15327983}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4HWQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4HWQ8-2; Sequence=VSP_043174;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots, senescent leaves and
CC       flowers (in sepals), and, to a lower extent, in stems, specifically in
CC       the vascular tissues (e.g. in the phloem).
CC       {ECO:0000269|PubMed:15327983}.
CC   -!- DISRUPTION PHENOTYPE: Increased vacuolar invertase activity leading to
CC       accumulation of hexose. {ECO:0000269|PubMed:15327983}.
CC   -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR   EMBL; AC051631; AAG51534.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32232.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58162.1; -; Genomic_DNA.
DR   EMBL; AF412119; AAL06571.1; -; mRNA.
DR   EMBL; AY056119; AAL07005.1; -; mRNA.
DR   EMBL; AY090265; AAL90926.1; -; mRNA.
DR   EMBL; BX816333; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY084290; AAM60881.1; -; mRNA.
DR   PIR; H96519; H96519.
DR   RefSeq; NP_001320618.1; NM_001333288.1. [F4HWQ8-2]
DR   RefSeq; NP_564516.2; NM_103692.3. [F4HWQ8-1]
DR   AlphaFoldDB; F4HWQ8; -.
DR   SMR; F4HWQ8; -.
DR   STRING; 3702.AT1G47960.1; -.
DR   PaxDb; F4HWQ8; -.
DR   PRIDE; F4HWQ8; -.
DR   ProteomicsDB; 220323; -. [F4HWQ8-1]
DR   EnsemblPlants; AT1G47960.1; AT1G47960.1; AT1G47960. [F4HWQ8-1]
DR   EnsemblPlants; AT1G47960.2; AT1G47960.2; AT1G47960. [F4HWQ8-2]
DR   GeneID; 841214; -.
DR   Gramene; AT1G47960.1; AT1G47960.1; AT1G47960. [F4HWQ8-1]
DR   Gramene; AT1G47960.2; AT1G47960.2; AT1G47960. [F4HWQ8-2]
DR   KEGG; ath:AT1G47960; -.
DR   Araport; AT1G47960; -.
DR   TAIR; locus:2202605; AT1G47960.
DR   eggNOG; ENOG502S67R; Eukaryota.
DR   HOGENOM; CLU_033761_5_0_1; -.
DR   InParanoid; F4HWQ8; -.
DR   OMA; WIHPLKE; -.
DR   OrthoDB; 1302509at2759; -.
DR   PRO; PR:F4HWQ8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HWQ8; baseline and differential.
DR   Genevisible; F4HWQ8; AT.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR   CDD; cd15796; CIF_like; 1.
DR   Gene3D; 1.20.140.40; -; 1.
DR   InterPro; IPR034087; C/VIF1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
DR   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   Pfam; PF04043; PMEI; 1.
DR   SMART; SM00856; PMEI; 1.
DR   SUPFAM; SSF101148; SSF101148; 1.
DR   TIGRFAMs; TIGR01614; PME_inhib; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Reference proteome;
KW   Signal; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..205
FT                   /note="Cell wall / vacuolar inhibitor of fructosidase 1"
FT                   /id="PRO_0000417021"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..134
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         162..205
FT                   /note="FYSNSIVKEEACGSSWPSLALNIDSKACVVSLQNIQFNRGRTCW -> VRML
FT                   L (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT                   /id="VSP_043174"
SQ   SEQUENCE   205 AA;  22326 MW;  4BE23211526B24DC CRC64;
     MKMMKVMMLI VMMMMVMVMV SEGSIIEPTC KETPDFNLCV SLLNSDPRGS SADTSGLALI
     LIDKIKGLAT KTLNEINGLY KKRPELKRAL DECSRRYKTI LNADVPEAIE AISKGVPKFG
     EDGVIDAGVE ASVCQGGFNG SSPLTSLTKS MQKISNVTRA IFYSNSIVKE EACGSSWPSL
     ALNIDSKACV VSLQNIQFNR GRTCW
 
 
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