NP7_RHOPR
ID NP7_RHOPR Reviewed; 205 AA.
AC Q6PQK2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Nitrophorin-7 {ECO:0000303|PubMed:15170336};
DE Short=NP7 {ECO:0000303|PubMed:15170336};
DE EC=1.7.6.1 {ECO:0000269|PubMed:20524697};
DE AltName: Full=Nitrite dismutase {ECO:0000305};
DE Flags: Precursor;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS94228.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15170336; DOI=10.1021/bi049655t;
RA Andersen J.F., Gudderra N.P., Francischetti I.M.B., Valenzuela J.G.,
RA Ribeiro J.M.C.;
RT "Recognition of anionic phospholipid membranes by an antihemostatic protein
RT from a blood-feeding insect.";
RL Biochemistry 43:6987-6994(2004).
RN [2]
RP FUNCTION.
RX PubMed=15598503; DOI=10.1016/j.jinorgbio.2004.10.009;
RA Walker F.A.;
RT "Nitric oxide interaction with insect nitrophorins and thoughts on the
RT electron configuration of the {FeNO}6 complex.";
RL J. Inorg. Biochem. 99:216-236(2005).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17958381; DOI=10.1021/bi7014986;
RA Knipp M., Yang F., Berry R.E., Zhang H., Shokhirev M.N., Walker F.A.;
RT "Spectroscopic and functional characterization of nitrophorin 7 from the
RT blood-feeding insect Rhodnius prolixus reveals an important role of its
RT isoform-specific N-terminus for proper protein function.";
RL Biochemistry 46:13254-13268(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17428677; DOI=10.1016/j.pep.2007.02.017;
RA Knipp M., Zhang H., Berry R.E., Walker F.A.;
RT "Overexpression in Escherichia coli and functional reconstitution of the
RT liposome binding ferriheme protein nitrophorin 7 from the bloodsucking bug
RT Rhodnius prolixus.";
RL Protein Expr. Purif. 54:183-191(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=19655755; DOI=10.1021/ja9040362;
RA He C., Knipp M.;
RT "Formation of nitric oxide from nitrite by the ferriheme b protein
RT nitrophorin 7.";
RL J. Am. Chem. Soc. 131:12042-12043(2009).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20524697; DOI=10.1021/bi100324z;
RA He C., Ogata H., Knipp M.;
RT "Formation of the complex of nitrite with the ferriheme b beta-barrel
RT proteins nitrophorin 4 and nitrophorin 7.";
RL Biochemistry 49:5841-5851(2010).
RN [7]
RP DISULFIDE BOND.
RX PubMed=21955842; DOI=10.1016/j.jinorgbio.2011.07.009;
RA Knipp M., Taing J.J., He C.;
RT "Reduction of the lipocalin type heme containing protein nitrophorin
RT -- sensitivity of the fold-stabilizing cysteine disulfides toward routine
RT heme-iron reduction.";
RL J. Inorg. Biochem. 105:1405-1412(2011).
CC -!- FUNCTION: Converts nitrite as the sole substrate to form nitric oxide
CC gas (NO). NO(2-) serves both as an electron donor and as an electron
CC acceptor. Binds to negatively charged cell surfaces of activated
CC platelets; binds to L-a-phosphatidyl-L-serine (PS)-bearing phospholipid
CC membranes. Once bound on an activated platelet, NP7 releases its stored
CC nitric oxide gas (NO) into the victim's tissues while feeding,
CC resulting in vasodilation and inhibition of platelet aggregation. Also
CC acts as an anticoagulant by blocking coagulation-factor binding sites.
CC Has antihistamine activity; binds histamine with high affinity.
CC {ECO:0000269|PubMed:15170336, ECO:0000269|PubMed:15598503,
CC ECO:0000269|PubMed:17428677, ECO:0000269|PubMed:17958381,
CC ECO:0000269|PubMed:19655755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 3 nitrite = H2O + nitrate + 2 nitric oxide;
CC Xref=Rhea:RHEA:31367, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632; EC=1.7.6.1;
CC Evidence={ECO:0000269|PubMed:19655755, ECO:0000269|PubMed:20524697};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:19655755};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:19655755};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17958381};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15170336,
CC ECO:0000269|PubMed:17428677}.
CC -!- TISSUE SPECIFICITY: Expressed in the endothelial cells of the salivary
CC glands. {ECO:0000269|PubMed:15170336, ECO:0000269|PubMed:17428677}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Nitrophorin family.
CC {ECO:0000255}.
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DR EMBL; AY585746; AAS94228.1; -; mRNA.
DR PDB; 4XMC; X-ray; 1.42 A; A=22-205.
DR PDB; 4XMD; X-ray; 1.60 A; A=22-205.
DR PDB; 4XME; X-ray; 1.29 A; A=22-205.
DR PDB; 4XMF; X-ray; 1.60 A; A=22-205.
DR PDB; 4XMG; X-ray; 1.80 A; A=22-205.
DR PDB; 4XMH; X-ray; 1.29 A; A=21-205.
DR PDB; 5M6J; X-ray; 1.70 A; A=22-205.
DR PDB; 5M6K; X-ray; 1.60 A; A=22-205.
DR PDBsum; 4XMC; -.
DR PDBsum; 4XMD; -.
DR PDBsum; 4XME; -.
DR PDBsum; 4XMF; -.
DR PDBsum; 4XMG; -.
DR PDBsum; 4XMH; -.
DR PDBsum; 5M6J; -.
DR PDBsum; 5M6K; -.
DR AlphaFoldDB; Q6PQK2; -.
DR SMR; Q6PQK2; -.
DR KEGG; ag:AAS94228; -.
DR VEuPathDB; VectorBase:RPRC000072; -.
DR BioCyc; MetaCyc:MON-16509; -.
DR BRENDA; 1.7.6.1; 5379.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0051381; F:histamine binding; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070026; F:nitric oxide binding; IMP:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0050819; P:negative regulation of coagulation; IMP:UniProtKB.
DR GO; GO:0033484; P:nitric oxide homeostasis; IMP:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR GO; GO:0034776; P:response to histamine; IMP:UniProtKB.
DR GO; GO:0044552; P:vasodilation in another organism; IMP:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR023613; Nitrophorin.
DR InterPro; IPR002351; Nitrophorin_domain.
DR Pfam; PF02087; Nitrophorin; 1.
DR PRINTS; PR00788; NITROPHORIN.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Disulfide bond; Heme; Hemostasis; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal;
KW Vasoactive; Vasodilator.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..205
FT /note="Nitrophorin-7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386434"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q26241"
FT DISULFID 25..144
FT /evidence="ECO:0000269|PubMed:21955842"
FT DISULFID 62..193
FT /evidence="ECO:0000269|PubMed:21955842"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4XME"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 150..162
FT /evidence="ECO:0007829|PDB:4XME"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:4XME"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4XME"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4XME"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:4XME"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4XME"
SQ SEQUENCE 205 AA; 22901 MW; 8846C9FB8141F2D2 CRC64;
MELYTALLAV TILSPSSIVG LPGECSVNVI PKKNLDKAKF FSGTWYETHY LDMDPQATEK
FCFSFAPRES GGTVKEALYH FNVDSKVSFY NTGTGPLESN GAKYTAKFNT VDKKGKEIKP
ADEKYSYTVT VIEAAKQSAL IHICLQEDGK DIGDLYSVLN RNKNALPNKK IKKALNKVSL
VLTKFVVTKD LDCKYDDKFL SSWQK
