ID   CVIF2_ARATH             Reviewed;         180 AA.
AC   O49603;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Cell wall / vacuolar inhibitor of fructosidase 2;
DE            Short=AtC/VIF2;
DE   Flags: Precursor;
GN   Name=C/VIF2; Synonyms=CIF2, VIF2; OrderedLocusNames=At5g64620;
GN   ORFNames=MUB3.14;
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].
RA   Greiner S., Krausgrill S., Rausch T.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, TISSUE SPECIFICITY, DISULFIDE BOND, GENE FAMILY, AND
RP   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 both cell wall (cell wall
CC       invertase CWI) and vacuoles (vacuolar invertase VI).
CC       {ECO:0000269|PubMed:14871666, ECO:0000269|PubMed:15327983}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed at low levels in seedlings, stems,
CC       leaves and flowers (in all organs), and, to a lower extent, in roots
CC       and siliques. {ECO:0000269|PubMed:15327983}.
CC   -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR   EMBL; Y12807; CAA73335.1; -; mRNA.
DR   EMBL; AB010076; BAB11429.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97927.1; -; Genomic_DNA.
DR   EMBL; BT003882; AAO41931.1; -; mRNA.
DR   EMBL; BT004919; AAO50452.1; -; mRNA.
DR   EMBL; AY086575; AAM63637.1; -; mRNA.
DR   RefSeq; NP_201267.1; NM_125858.4.
DR   AlphaFoldDB; O49603; -.
DR   SMR; O49603; -.
DR   BioGRID; 21825; 1.
DR   STRING; 3702.AT5G64620.1; -.
DR   PaxDb; O49603; -.
DR   PRIDE; O49603; -.
DR   ProteomicsDB; 220324; -.
DR   EnsemblPlants; AT5G64620.1; AT5G64620.1; AT5G64620.
DR   GeneID; 836583; -.
DR   Gramene; AT5G64620.1; AT5G64620.1; AT5G64620.
DR   KEGG; ath:AT5G64620; -.
DR   Araport; AT5G64620; -.
DR   TAIR; locus:2174774; AT5G64620.
DR   eggNOG; ENOG502RXIR; Eukaryota.
DR   HOGENOM; CLU_033761_5_1_1; -.
DR   InParanoid; O49603; -.
DR   OMA; TSYYDLC; -.
DR   OrthoDB; 1439149at2759; -.
DR   PhylomeDB; O49603; -.
DR   PRO; PR:O49603; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O49603; baseline and differential.
DR   Genevisible; O49603; 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   Gene3D; 1.20.140.40; -; 1.
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   Disulfide bond; Glycoprotein; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..180
FT                   /note="Cell wall / vacuolar inhibitor of fructosidase 2"
FT                   /id="PRO_5000147151"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..141
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  19634 MW;  023B8688AF8D0274 CRC64;
     MASSLIFLLL VTLTFSASTL ISAKSNTTTI IESTCKTTNY YKFCVSALKS DPRSPTADTK
     GLASIMVGVG MTNATSTANY IAGNLSATVK DTVLKKVLQD CSEKYALAAD SLRLTIQDLD
     DEAYDYASMH VLAAQDYPNV CRNIFRRVKG LAYPVEIRRR EASLRRICGV VSGILDRLVE