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Protein

Nitrophorin-4

Gene
N/A
Organism
Rhodnius prolixus (Triatomid bug)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing. NO release is pH dependent and linked to loop dynamics.5 Publications

Catalytic activityi

3 nitrite + 2 H+ = 2 nitric oxide + nitrate + H2O.1 Publication

Cofactori

heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi80Iron (heme proximal ligand); via tele nitrogen9 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Vasoactive, Vasodilator

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.7.6.1. 5379.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrophorin-41 Publication (EC:1.7.6.11 Publication)
Short name:
NP41 Publication
Alternative name(s):
Nitrite dismutaseCurated
OrganismiRhodnius prolixus (Triatomid bug)
Taxonomic identifieri13249 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraEuhemipteraHeteropteraPanheteropteraCimicomorphaReduviidaeTriatominaeRhodnius
Proteomesi
  • UP000015103 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi51D → A or N: Loss of NO-induced conformational change and strongly reduced pH dependence for NO release. Stabilization of the ferric-NO heme center and decreased nitrite disproportionation. 3 Publications1
Mutagenesisi76E → Q: Stabilization of the ferric-NO heme center. 1 Publication1
Mutagenesisi142T → V: No effect on NO-induced conformational change or on pH dependence for NO release. Increased NO association rates. 1 Publication1
Mutagenesisi150 – 151DL → AA: Loss of NO-induced conformational change and loss of pH dependence for NO release. 1 Publication2
Mutagenesisi151L → R: Coordination of the heme iron center and inhibition of nitrite disproportionation. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000002182622 – 205Nitrophorin-4Add BLAST184

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi23 ↔ 1432 Publications
Disulfide bondi62 ↔ 1922 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the salivary glands.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 38Combined sources4
Beta strandi40 – 53Combined sources14
Helixi54 – 56Combined sources3
Beta strandi62 – 70Combined sources9
Beta strandi73 – 81Combined sources9
Turni83 – 85Combined sources3
Beta strandi88 – 99Combined sources12
Beta strandi102 – 110Combined sources9
Beta strandi116 – 118Combined sources3
Beta strandi124 – 133Combined sources10
Beta strandi135 – 146Combined sources12
Beta strandi153 – 161Combined sources9
Helixi168 – 176Combined sources9
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Helixi188 – 190Combined sources3
Helixi196 – 202Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2UX-ray1.15A22-205[»]
1D3SX-ray1.40A22-205[»]
1EQDX-ray1.60A22-205[»]
1ERXX-ray1.40A22-205[»]
1IKEX-ray1.50A22-205[»]
1IKJX-ray1.27A22-205[»]
1KOIX-ray1.08A22-205[»]
1ML7X-ray1.25A22-205[»]
1NP4X-ray1.50A22-205[»]
1SXUX-ray1.40A22-205[»]
1SXWX-ray1.05A22-205[»]
1SXXX-ray1.01A22-205[»]
1SXYX-ray1.07A22-205[»]
1SY0X-ray1.15A22-205[»]
1SY1X-ray1.01A22-205[»]
1SY2X-ray1.00A22-205[»]
1SY3X-ray1.00A22-205[»]
1U0XX-ray1.45A22-205[»]
1X8NX-ray1.08A22-205[»]
1X8OX-ray1.01A22-205[»]
1X8PX-ray0.85A22-205[»]
1X8QX-ray0.85A22-205[»]
1YWAX-ray0.89A22-205[»]
1YWBX-ray0.97A22-205[»]
1YWCX-ray1.00A22-205[»]
1YWDX-ray1.08A22-205[»]
2AT0X-ray1.00X22-205[»]
2AT3X-ray1.00X22-205[»]
2AT5X-ray1.22X22-205[»]
2AT6X-ray1.22X22-205[»]
2AT8X-ray1.00X22-205[»]
2OFMX-ray1.11X22-205[»]
2OFRX-ray1.00X22-205[»]
3C76X-ray1.07X22-205[»]
3C77X-ray1.08X22-205[»]
3C78X-ray0.98X22-205[»]
3FLLX-ray1.50A22-205[»]
3MVFX-ray1.40A22-205[»]
3TGAX-ray1.30A22-205[»]
3TGBX-ray1.35A22-205[»]
3TGCX-ray1.40A22-205[»]
4GNWX-ray1.15A/B22-205[»]
4GRJX-ray1.15A/B22-205[»]
4HPAX-ray1.50A22-205[»]
4HPBX-ray1.60A22-205[»]
4HPCX-ray1.40A22-205[»]
4HPDX-ray1.30A22-205[»]
5HWZX-ray1.45A22-205[»]
ProteinModelPortaliQ94734.
SMRiQ94734.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ94734.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Nitrophorin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR023613. Nitrophorin.
IPR002351. Nitrophorin_domain.
[Graphical view]
PfamiPF02087. Nitrophorin. 1 hit.
[Graphical view]
PRINTSiPR00788. NITROPHORIN.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q94734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSYTSLLAV AILCLFGGVN GACTKNAIAQ TGFNKDKYFN GDVWYVTDYL
60 70 80 90 100
DLEPDDVPKR YCAALAAGTA SGKLKEALYH YDPKTQDTFY DVSELQVESL
110 120 130 140 150
GKYTANFKKV DKNGNVKVAV TAGNYYTFTV MYADDSSALI HTCLHKGNKD
160 170 180 190 200
LGDLYAVLNR NKDAAAGDKV KSAVSAATLE FSKFISTKEN NCAYDNDSLK

SLLTK
Length:205
Mass (Da):22,406
Last modified:February 1, 1997 - v1
Checksum:i9BAACA12001527F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70584 mRNA. Translation: AAB09590.1.
PIRiD56385.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70584 mRNA. Translation: AAB09590.1.
PIRiD56385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2UX-ray1.15A22-205[»]
1D3SX-ray1.40A22-205[»]
1EQDX-ray1.60A22-205[»]
1ERXX-ray1.40A22-205[»]
1IKEX-ray1.50A22-205[»]
1IKJX-ray1.27A22-205[»]
1KOIX-ray1.08A22-205[»]
1ML7X-ray1.25A22-205[»]
1NP4X-ray1.50A22-205[»]
1SXUX-ray1.40A22-205[»]
1SXWX-ray1.05A22-205[»]
1SXXX-ray1.01A22-205[»]
1SXYX-ray1.07A22-205[»]
1SY0X-ray1.15A22-205[»]
1SY1X-ray1.01A22-205[»]
1SY2X-ray1.00A22-205[»]
1SY3X-ray1.00A22-205[»]
1U0XX-ray1.45A22-205[»]
1X8NX-ray1.08A22-205[»]
1X8OX-ray1.01A22-205[»]
1X8PX-ray0.85A22-205[»]
1X8QX-ray0.85A22-205[»]
1YWAX-ray0.89A22-205[»]
1YWBX-ray0.97A22-205[»]
1YWCX-ray1.00A22-205[»]
1YWDX-ray1.08A22-205[»]
2AT0X-ray1.00X22-205[»]
2AT3X-ray1.00X22-205[»]
2AT5X-ray1.22X22-205[»]
2AT6X-ray1.22X22-205[»]
2AT8X-ray1.00X22-205[»]
2OFMX-ray1.11X22-205[»]
2OFRX-ray1.00X22-205[»]
3C76X-ray1.07X22-205[»]
3C77X-ray1.08X22-205[»]
3C78X-ray0.98X22-205[»]
3FLLX-ray1.50A22-205[»]
3MVFX-ray1.40A22-205[»]
3TGAX-ray1.30A22-205[»]
3TGBX-ray1.35A22-205[»]
3TGCX-ray1.40A22-205[»]
4GNWX-ray1.15A/B22-205[»]
4GRJX-ray1.15A/B22-205[»]
4HPAX-ray1.50A22-205[»]
4HPBX-ray1.60A22-205[»]
4HPCX-ray1.40A22-205[»]
4HPDX-ray1.30A22-205[»]
5HWZX-ray1.45A22-205[»]
ProteinModelPortaliQ94734.
SMRiQ94734.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.7.6.1. 5379.

Miscellaneous databases

EvolutionaryTraceiQ94734.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR023613. Nitrophorin.
IPR002351. Nitrophorin_domain.
[Graphical view]
PfamiPF02087. Nitrophorin. 1 hit.
[Graphical view]
PRINTSiPR00788. NITROPHORIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNP4_RHOPR
AccessioniPrimary (citable) accession number: Q94734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Superposition of the structures of NP4 in the presence of ammonia or nitrite shows a conformational change of the protein upon NO2- binding.5 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.