P83326 (PMEI_ACTDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase inhibitor

Alternative name(s):
AdPMEI
Short name=PMEI
Pectin methylesterase inhibitor

Gene names

Name:

PMEI

Organism

Actinidia deliciosa (Kiwi)

Taxonomic identifier

3627 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › Ericales › Actinidiaceae › Actinidia

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibits pectin methylesterase; may be involved in the regulation of fruit ripening.
Subcellular location	Cytoplasm. Note: Concentrated in a layer close to the cell membrane. Ref.2
Tissue specificity	Fruit. Ref.1
Developmental stage	Expression increases as fruit matures. Ref.1
Sequence similarities	Belongs to the PMEI family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Signal
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	negative regulation of catalytic activity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	enzyme inhibitor activity Inferred from electronic annotation. Source: InterPro pectinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Ref.2

Chain

33 – 184

152

Pectinesterase inhibitor

PRO_0000217197

Propeptide

185

1

PRO_0000300246

Amino acid modifications

Disulfide bond

41 ↔ 50

Ref.2

Disulfide bond

106 ↔ 146

Ref.2

Experimental info

Sequence conflict

55

1

E → K in BAC54966. Ref.1

Sequence conflict

88

1

A → S in BAC54966. Ref.1

Sequence conflict

110

1

Y → F in BAC54965. Ref.1

Sequence conflict

174

1

V → I in BAC54965. Ref.1

Sequence conflict

174

1

V → I in BAC54966. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

185

Helix Strand Turn

Details...

Helix

35 – 40

6

Helix

41 – 43

3

Helix

47 – 55

9

Helix

60 – 62

3

Helix

65 – 91

27

Helix

97 – 126

30

Helix

129 – 149

21

Beta strand

152 – 154

3

Helix

158 – 180

23

Sequences

	Sequence		Length	Mass (Da)
	P83326 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: ED5B2BA8EFDEDCD2	FASTA	185	19,893
	10 20 30 40 50 60 MAFSYCSSSL FVSLLLVILF ISPLSQRPSV KAENHLISEI CPKTRNPSLC LQALESDPRS 70 80 90 100 110 120 ASKDLKGLGQ FSIDIAQASA KQTSKIIASL TNQATDPKLK GRYETCSENY ADAIDSLGQA 130 140 150 160 170 180 KQFLTSGDYN SLNIYASAAF DGAGTCEDSF EGPPNIPTQL HQADLKLEDL CDIVLVISNL LPGSK

References

[1]	"Pectin methylesterase inhibitor cDNA from kiwi fruit." Irifune K., Nishida T., Egawa H., Nagatani A. Plant Cell Rep. 23:333-338(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: cv. Hayward. Tissue: Fruit.
[2]	"Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and structural importance of two disulfide bridges." Camardella L., Carratore V., Ciardiello M.A., Servillo L., Balestrieri C., Giovane A. Eur. J. Biochem. 267:4561-4565(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-184, SUBCELLULAR LOCATION, DISULFIDE BONDS, CIRCULAR DICHROISM ANALYSIS. Tissue: Fruit.
[3]	"Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein." Di Matteo A., Giovane A., Raiola A., Camardella L., Bonivento D., De Lorenzo G., Cervone F., Bellincampi D., Tsernoglou D. Plant Cell 17:849-858(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-184 IN COMPLEX WITH TOMATO PME1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB091088 mRNA. Translation: BAC54964.1.
AB091089 mRNA. Translation: BAC54965.1.
AB091090 mRNA. Translation: BAC54966.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XG2	X-ray	1.90	B	33-184	[»]

ProteinModelPortal

P83326.

SMR

P83326. Positions 33-182.

ModBase

Search...

Protein family/group databases

Allergome

3548. Act d 6.
3977. Act d 6.0101.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.20.140.40. 1 hit.

InterPro

IPR006501. Pectinesterase_inhib.
[Graphical view]

Pfam

PF04043. PMEI. 1 hit.
[Graphical view]

SMART

SM00856. PMEI. 1 hit.
[Graphical view]

SUPFAM

SSF101148. Pectinesterase_inhib. 1 hit.

TIGRFAMs

TIGR01614. PME_inhib. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P83326.

Entry information

Entry name

PMEI_ACTDE

Accession

Primary (citable) accession number: P83326
Secondary accession number(s): Q852R5, Q852R6, Q852R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	September 11, 2007
Last modified:	April 3, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program