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Protein

Metallocarboxypeptidase inhibitor

Gene
N/A
Organism
Hirudo medicinalis (Medicinal leech)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Protein family/group databases

MEROPSiI46.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallocarboxypeptidase inhibitor
Alternative name(s):
Leech carboxypeptidase inhibitor
Short name:
LCI
OrganismiHirudo medicinalis (Medicinal leech)
Taxonomic identifieri6421 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Chaini16 – 8166Metallocarboxypeptidase inhibitorPRO_0000026725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 48
Disulfide bondi32 ↔ 76
Disulfide bondi33 ↔ 57
Disulfide bondi36 ↔ 72

Keywords - PTMi

Disulfide bond

Interactioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei80 – 801Interaction with carboxypeptidaseBy similarity

Protein-protein interaction databases

MINTiMINT-125639.

Structurei

Secondary structure

1
81
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 266Combined sources
Beta strandi31 – 388Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 504Combined sources
Helixi55 – 606Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 778Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTDX-ray1.65B20-80[»]
1DTVNMR-A16-81[»]
1ZFINMR-A16-81[»]
1ZFLNMR-A16-81[»]
2ABZX-ray2.16C/D/E/F16-81[»]
ProteinModelPortaliP81511.
SMRiP81511. Positions 16-81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81511.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.1040.10. 1 hit.
InterProiIPR024063. Prot_inh_LCI.
[Graphical view]
SUPFAMiSSF57620. SSF57620. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLVFLCCL HLVISSHTPD ESFLCYQPDQ VCCFICRGAA PLPSEGECNP
60 70 80
HPTAPWCREG AVEWVPYSTG QCRTTCIPYV E
Length:81
Mass (Da):9,068
Last modified:July 15, 1999 - v1
Checksum:i7D7E175E6933922A
GO

Mass spectrometryi

Molecular mass is 7326 Da from positions 16 - 81. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010948 mRNA. Translation: CAA09422.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010948 mRNA. Translation: CAA09422.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTDX-ray1.65B20-80[»]
1DTVNMR-A16-81[»]
1ZFINMR-A16-81[»]
1ZFLNMR-A16-81[»]
2ABZX-ray2.16C/D/E/F16-81[»]
ProteinModelPortaliP81511.
SMRiP81511. Positions 16-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-125639.

Protein family/group databases

MEROPSiI46.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81511.

Family and domain databases

Gene3Di3.30.1040.10. 1 hit.
InterProiIPR024063. Prot_inh_LCI.
[Graphical view]
SUPFAMiSSF57620. SSF57620. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization."
    Reverter D., Vendrell J., Canals F., Horstmann J., Aviles F.X., Fritz H., Sommerhoff C.P.
    J. Biol. Chem. 273:32927-32933(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-81, MASS SPECTROMETRY.
  2. "Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2."
    Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R., Bode W., Vendrell J., Holak T.A., Aviles F.X.
    Nat. Struct. Biol. 7:322-328(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH HUMAN CPA2.

Entry informationi

Entry nameiMCPI_HIRME
AccessioniPrimary (citable) accession number: P81511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: May 11, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.