MCPI_SOLLC
ID MCPI_SOLLC Reviewed; 77 AA.
AC P01076;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Metallocarboxypeptidase inhibitor;
DE Short=Carboxypeptidase inhibitor;
DE Short=MCPI;
DE Flags: Precursor;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. UC82B;
RX PubMed=1715974; DOI=10.1007/bf00282477;
RA Martineau B., McBride K.E., Houck C.M.;
RT "Regulation of metallocarboxypeptidase inhibitor gene expression in
RT tomato.";
RL Mol. Gen. Genet. 228:281-286(1991).
RN [2]
RP PROTEIN SEQUENCE OF 33-69, AND PYROGLUTAMATE FORMATION AT GLN-33.
RX PubMed=7236596; DOI=10.1021/bi00511a029;
RA Hass G.M., Hermodson M.A.;
RT "Amino acid sequence of a carboxypeptidase inhibitor from tomato fruit.";
RL Biochemistry 20:2256-2260(1981).
CC -!- FUNCTION: May play a defensive role against insect attacks.
CC -!- TISSUE SPECIFICITY: Ovaries.
CC -!- DEVELOPMENTAL STAGE: Present at very high levels during anthesis in
CC ovaries, decreases rapidly during fruit development.
CC -!- INDUCTION: The MCPI RNA, but not its protein, is highly induced by
CC wounding the leaves.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- SIMILARITY: To potato MCPI. {ECO:0000305}.
CC -!- CAUTION: Besides the signal peptide, the N-terminal 32 AA may contain a
CC propeptide sequence. {ECO:0000305}.
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DR EMBL; X59282; CAA41973.1; -; mRNA.
DR PIR; S16558; XKTO.
DR RefSeq; NP_001233934.1; NM_001247005.3.
DR AlphaFoldDB; P01076; -.
DR SMR; P01076; -.
DR STRING; 4081.Solyc07g007250.2.1; -.
DR MEROPS; I37.001; -.
DR PaxDb; P01076; -.
DR PRIDE; P01076; -.
DR EnsemblPlants; Solyc07g007250.3.1; Solyc07g007250.3.1; Solyc07g007250.3.
DR GeneID; 544286; -.
DR Gramene; Solyc07g007250.3.1; Solyc07g007250.3.1; Solyc07g007250.3.
DR KEGG; sly:544286; -.
DR eggNOG; ENOG502R6I7; Eukaryota.
DR HOGENOM; CLU_198582_0_0_1; -.
DR OMA; CGPYVGR; -.
DR OrthoDB; 1635319at2759; -.
DR PhylomeDB; P01076; -.
DR Proteomes; UP000004994; Chromosome 7.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR InterPro; IPR004231; COpept_A_inh-like.
DR InterPro; IPR011052; Proteinase_amylase_inhib_sf.
DR Pfam; PF02977; CarbpepA_inh; 1.
DR SUPFAM; SSF57027; SSF57027; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin;
KW Metalloenzyme inhibitor; Pyrrolidone carboxylic acid; Reference proteome;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:7236596"
FT CHAIN 33..69
FT /note="Metallocarboxypeptidase inhibitor"
FT /id="PRO_0000021662"
FT PROPEP 70..77
FT /note="Hydrophobic peptide"
FT /id="PRO_0000021663"
FT SITE 69
FT /note="Interaction with carboxypeptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7236596"
FT DISULFID 39..55
FT /evidence="ECO:0000250"
FT DISULFID 43..58
FT /evidence="ECO:0000250"
FT DISULFID 49..65
FT /evidence="ECO:0000250"
SQ SEQUENCE 77 AA; 8354 MW; FF6A09CD2D4970AA CRC64;
MAQKFTILFT ILLVVIAAQD VMAQDATLTK LFQQYDPVCH KPCSTQDDCS GGTFCQACWR
FAGTCGPYVG RAMAIGV
