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Protein

Sweet protein mabinlin-2

Gene
N/A
Organism
Capparis masaikai (Mabinlang)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Heat stable 2S seed storage protein having sweetness-inducing activity.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein, Taste-modifying protein

Names & Taxonomyi

Protein namesi
Recommended name:
Sweet protein mabinlin-2
Alternative name(s):
Mabinlin II
Short name:
MAB II
Cleaved into the following 2 chains:
OrganismiCapparis masaikai (Mabinlang)
Taxonomic identifieri13395 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCapparaceaeCapparis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000003213721 – 351 PublicationAdd BLAST15
ChainiPRO_000003213836 – 68Sweet protein mabinlin-2 chain AAdd BLAST33
PropeptideiPRO_000003213969 – 821 PublicationAdd BLAST14
ChainiPRO_000003214083 – 154Sweet protein mabinlin-2 chain BAdd BLAST72
PropeptideiPRO_00000321411551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36Pyrrolidone carboxylic acid1
Disulfide bondi40 ↔ 103Interchain (between A and B chains)
Disulfide bondi53 ↔ 92Interchain (between A and B chains)
Modified residuei83Pyrrolidone carboxylic acid1
Disulfide bondi93 ↔ 141
Disulfide bondi105 ↔ 149

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Heterodimer of a small A and a large B chain linked by disulfide bonds.

Structurei

Secondary structure

1155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 46Combined sources7
Helixi47 – 50Combined sources4
Helixi51 – 62Combined sources12
Helixi88 – 96Combined sources9
Helixi101 – 103Combined sources3
Helixi104 – 118Combined sources15
Helixi124 – 140Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DS2X-ray1.70A/C36-68[»]
B/D83-154[»]
ProteinModelPortaliP30233.
SMRiP30233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30233.

Family & Domainsi

Sequence similaritiesi

Belongs to the 2S seed storage albumins family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00496. NAPIN.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P30233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLIFLFAT LALFVLLANA SIQTTVIEVD EEEDNQLWRC QRQFLQHQRL
60 70 80 90 100
RACQRFIHRR AQFGGQPDEL EDEVEDDNDD ENQPRRPALR QCCNQLRQVD
110 120 130 140 150
RPCVCPVLRQ AAQQVLQRQI IQGPQQLRRL FDAARNLPNI CNIPNIGACP

FRAWP
Length:155
Mass (Da):18,089
Last modified:February 21, 2001 - v3
Checksum:i72E885DEDCC2D46A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti148A → T in BAA12204 (PubMed:8973336).Curated1
Sequence conflicti153A → T in BAA12204 (PubMed:8973336).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83997 mRNA. Translation: BAA12204.1.
PIRiJC5379.
S28842.
S28843.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83997 mRNA. Translation: BAA12204.1.
PIRiJC5379.
S28842.
S28843.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DS2X-ray1.70A/C36-68[»]
B/D83-154[»]
ProteinModelPortaliP30233.
SMRiP30233.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30233.

Family and domain databases

InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00496. NAPIN.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry namei2SS2_CAPMA
AccessioniPrimary (citable) accession number: P30233
Secondary accession number(s): O04774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 21, 2001
Last modified: November 2, 2016
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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.