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Protein

Napin-1A

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The small, basic, water-soluble napins are one of the two major kinds of storage proteins synthesized in the seed during its maturation.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein

Names & Taxonomyi

Protein namesi
Recommended name:
Napin-1A
Alternative name(s):
Napin BnIa
Cleaved into the following 2 chains:
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3131Napin-1A small chainPRO_0000032131Add
BLAST
Chaini32 – 11079Napin-1A large chainPRO_0000032132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi5 ↔ 56Interchain (between small and large chains)1 Publication
Disulfide bondi18 ↔ 45Interchain (between small and large chains)1 Publication
Modified residuei32 – 321Pyrrolidone carboxylic acid1 Publication
Disulfide bondi46 ↔ 931 Publication
Disulfide bondi58 ↔ 1011 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

The mature protein consists of a small and a large chain linked by disulfide bonds.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi19 – 246Combined sources
Helixi43 – 508Combined sources
Helixi54 – 563Combined sources
Helixi58 – 6912Combined sources
Helixi71 – 733Combined sources
Helixi79 – 857Combined sources
Turni96 – 983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PNBNMR-A1-31[»]
B32-106[»]
ProteinModelPortaliP24565.
SMRiP24565. Positions 1-106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24565.

Family & Domainsi

Sequence similaritiesi

Belongs to the 2S seed storage albumins family.Curated

Family and domain databases

Gene3Di1.10.120.10. 1 hit.
InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
IPR013771. Trypsin/amylase_inhib.
[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.

P24565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QPQKCQREFQ QEQHLRACQQ WIRQQLAGSP FQSGPQEGPW LREQCCNELY
60 70 80 90 100
QEDQVCVCPT LKQAAKSVRV QGQHGPFQST RIYQIAKNLP NVCNMKQIGT
110
CPFIAIPFFP
Length:110
Mass (Da):12,691
Last modified:March 1, 1992 - v1
Checksum:i3A2938ADA2C1E995
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi31 – 322Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311Missing in minor form SM, less than 7%.
Natural varianti37 – 371E → Q in napin-1B.
Natural varianti107 – 1104Missing in napin-1B.

Sequence databases

PIRiS20350.
S26636.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRiS20350.
S26636.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PNBNMR-A1-31[»]
B32-106[»]
ProteinModelPortaliP24565.
SMRiP24565. Positions 1-106.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP24565.

Family and domain databases

Gene3Di1.10.120.10. 1 hit.
InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000617. Napin.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00496. NAPIN.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A new distinct group of 2 S albumins from rapeseed. Amino acid sequence of two low molecular weight napins."
    Monsalve R.I., Lopez-Otin C., Villalba M., Rodriguez R.
    FEBS Lett. 295:207-210(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-32.
    Tissue: Seed.
  2. "1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein."
    Rico M., Bruix M., Gonzalez C., Monsalve R.I., Rodriguez R.
    Biochemistry 35:15672-15682(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-106, DISULFIDE BONDS.

Entry informationi

Entry namei2SSI_BRANA
AccessioniPrimary (citable) accession number: P24565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: October 14, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Napin 1A and 1B are minor component of the seed 2S albumin.
The sequence shown is that of napin IA.

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.