MCPI_SOLTU
ID MCPI_SOLTU Reviewed; 39 AA.
AC P01075;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Metallocarboxypeptidase inhibitor;
DE Short=Carboxypeptidase inhibitor;
DE Short=MCPI;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RX PubMed=1122280; DOI=10.1021/bi00677a036;
RA Hass G.M., Nau H., Biemann K., Grahn D.T., Ericsson L.H., Neurath H.;
RT "The amino acid sequence of a carboxypeptidase inhibitor from potatoes.";
RL Biochemistry 14:1334-1342(1975).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=942094; DOI=10.1016/0003-2697(76)90152-4;
RA Nau H., Biemann K.;
RT "Amino acid sequencing by gas chromatography -- mass spectrometry using
RT trifluoro-dideuteroalkylated peptide derivatives. C. The primary structure
RT of the carboxypeptidase inhibitor from potatoes.";
RL Anal. Biochem. 73:175-186(1976).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=444453; DOI=10.1021/bi00578a018;
RA Leary T.R., Grahn D.T., Neurath H., Hass G.M.;
RT "Structure of potato carboxypeptidase inhibitor: disulfide pairing and
RT exposure of aromatic residues.";
RL Biochemistry 18:2252-2256(1979).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7154070; DOI=10.1016/0022-2836(82)90309-6;
RA Rees D.C., Lipscomb W.N.;
RT "Refined crystal structure of the potato inhibitor complex of
RT carboxypeptidase A at 2.5-A resolution.";
RL J. Mol. Biol. 160:475-498(1982).
CC -!- FUNCTION: May play a defensive role against insect attacks.
CC -!- TISSUE SPECIFICITY: Highly concentrated in tubers. Closely related but
CC distinct forms of MCPI are present in leaves, stems and buds.
CC -!- INDUCTION: By wounding; in leaves.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
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DR PDB; 1H20; NMR; -; A=2-39.
DR PDB; 4CPA; X-ray; 2.50 A; I/J=3-38.
DR PDB; 7EQZ; X-ray; 2.20 A; I=3-38.
DR PDBsum; 1H20; -.
DR PDBsum; 4CPA; -.
DR PDBsum; 7EQZ; -.
DR AlphaFoldDB; P01075; -.
DR BMRB; P01075; -.
DR SMR; P01075; -.
DR MINT; P01075; -.
DR MEROPS; I37.001; -.
DR PRIDE; P01075; -.
DR EvolutionaryTrace; P01075; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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 3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW Metalloenzyme inhibitor; Pyrrolidone carboxylic acid; Reference proteome.
FT CHAIN 1..39
FT /note="Metallocarboxypeptidase inhibitor"
FT /id="PRO_0000096302"
FT SITE 38
FT /note="Interaction with carboxypeptidase"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1122280"
FT DISULFID 8..24
FT /evidence="ECO:0000269|PubMed:444453"
FT DISULFID 12..27
FT /evidence="ECO:0000269|PubMed:444453"
FT DISULFID 18..34
FT /evidence="ECO:0000269|PubMed:444453"
FT VARIANT 2
FT /note="Missing (in 50% of the molecules)"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:7EQZ"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:7EQZ"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7EQZ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7EQZ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7EQZ"
SQ SEQUENCE 39 AA; 4300 MW; 82EA0E0762237AFA CRC64;
QQHADPICNK PCKTHDDCSG AWFCQACWNS ARTCGPYVG
