ID   PMEI_ACTDE              Reviewed;         185 AA.
AC   P83326; Q852R5; Q852R6; Q852R7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Pectinesterase inhibitor;
DE   AltName: Full=AdPMEI;
DE            Short=PMEI;
DE   AltName: Full=Pectin methylesterase inhibitor;
DE   Flags: Precursor;
GN   Name=PMEI;
OS   Actinidia deliciosa (Kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=3627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Hayward; TISSUE=Fruit;
RX   PubMed=15365757; DOI=10.1007/s00299-004-0835-6;
RA   Irifune K., Nishida T., Egawa H., Nagatani A.;
RT   "Pectin methylesterase inhibitor cDNA from kiwi fruit.";
RL   Plant Cell Rep. 23:333-338(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-184, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND
RP   CIRCULAR DICHROISM ANALYSIS.
RC   TISSUE=Fruit;
RX   PubMed=10880981; DOI=10.1046/j.1432-1327.2000.01510.x;
RA   Camardella L., Carratore V., Ciardiello M.A., Servillo L., Balestrieri C.,
RA   Giovane A.;
RT   "Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and
RT   structural importance of two disulfide bridges.";
RL   Eur. J. Biochem. 267:4561-4565(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-184 IN COMPLEX WITH TOMATO
RP   PME1.
RX   PubMed=15722470; DOI=10.1105/tpc.104.028886;
RA   Di Matteo A., Giovane A., Raiola A., Camardella L., Bonivento D.,
RA   De Lorenzo G., Cervone F., Bellincampi D., Tsernoglou D.;
RT   "Structural basis for the interaction between pectin methylesterase and a
RT   specific inhibitor protein.";
RL   Plant Cell 17:849-858(2005).
CC   -!- FUNCTION: Inhibits pectin methylesterase; may be involved in the
CC       regulation of fruit ripening.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880981}.
CC       Note=Concentrated in a layer close to the cell membrane.
CC   -!- TISSUE SPECIFICITY: Fruit. {ECO:0000269|PubMed:15365757}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases as fruit matures.
CC       {ECO:0000269|PubMed:15365757}.
CC   -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB091088; BAC54964.1; -; mRNA.
DR   EMBL; AB091089; BAC54965.1; -; mRNA.
DR   EMBL; AB091090; BAC54966.1; -; mRNA.
DR   PDB; 1XG2; X-ray; 1.90 A; B=33-184.
DR   PDBsum; 1XG2; -.
DR   AlphaFoldDB; P83326; -.
DR   SMR; P83326; -.
DR   Allergome; 3548; Act d 6.
DR   Allergome; 3977; Act d 6.0101.
DR   EvolutionaryTrace; P83326; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046910; F:pectinesterase inhibitor activity; IEA:InterPro.
DR   CDD; cd15797; PMEI; 1.
DR   Gene3D; 1.20.140.40; -; 1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
DR   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   InterPro; IPR034086; PMEI_plant.
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   3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:10880981"
FT   CHAIN           33..184
FT                   /note="Pectinesterase inhibitor"
FT                   /id="PRO_0000217197"
FT   PROPEP          185
FT                   /id="PRO_0000300246"
FT   DISULFID        41..50
FT                   /evidence="ECO:0000269|PubMed:10880981"
FT   DISULFID        106..146
FT                   /evidence="ECO:0000269|PubMed:10880981"
FT   CONFLICT        55
FT                   /note="E -> K (in Ref. 1; BAC54966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="A -> S (in Ref. 1; BAC54966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="Y -> F (in Ref. 1; BAC54965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="V -> I (in Ref. 1; BAC54965/BAC54966)"
FT                   /evidence="ECO:0000305"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           47..55
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           65..91
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           97..126
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           129..149
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:1XG2"
FT   HELIX           158..180
FT                   /evidence="ECO:0007829|PDB:1XG2"
SQ   SEQUENCE   185 AA;  19893 MW;  ED5B2BA8EFDEDCD2 CRC64;
     MAFSYCSSSL FVSLLLVILF ISPLSQRPSV KAENHLISEI CPKTRNPSLC LQALESDPRS
     ASKDLKGLGQ FSIDIAQASA KQTSKIIASL TNQATDPKLK GRYETCSENY ADAIDSLGQA
     KQFLTSGDYN SLNIYASAAF DGAGTCEDSF EGPPNIPTQL HQADLKLEDL CDIVLVISNL
     LPGSK