NP1_RHOPR
ID NP1_RHOPR Reviewed; 207 AA.
AC Q26239;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nitrophorin-1;
DE Short=NP1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Salivary gland;
RX PubMed=7721773; DOI=10.1074/jbc.270.15.8691;
RA Champagne D.E., Nussenzveig R.H., Ribeiro J.M.C.;
RT "Purification, partial characterization, and cloning of nitric oxide-
RT carrying heme proteins (nitrophorins) from salivary glands of the blood-
RT sucking insect Rhodnius prolixus.";
RL J. Biol. Chem. 270:8691-8695(1995).
RN [2] {ECO:0000312|PDB:1NP1, ECO:0000312|PDB:2NP1, ECO:0000312|PDB:3NP1}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Salivary gland;
RX PubMed=9546222; DOI=10.1038/nsb0498-304;
RA Weichsel A., Andersen J.F., Champagne D.E., Walker F.A., Montfort W.R.;
RT "Crystal structures of a nitric oxide transport protein from a blood-
RT sucking insect.";
RL Nat. Struct. Biol. 5:304-309(1998).
RN [3] {ECO:0000312|PDB:4NP1}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND DISULFIDE BONDS.
RA Ding X.D., Weichsel A., Andersen J.F., Shokhireva T.K., Balfour C.,
RA Pierik A., Averill B.A., Montfort W.R., Walker F.A.;
RL Submitted (JUN-1998) to the PDB data bank.
CC -!- FUNCTION: Heme-based protein that deliver nitric oxide gas (NO) to the
CC victim while feeding, resulting in vasodilation and inhibition of
CC platelet aggregation. Also binds tightly to histamine, which is
CC released by the host to induce wound healing.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the salivary glands.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Nitrophorin family.
CC {ECO:0000305}.
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DR EMBL; L39654; AAA74407.1; -; mRNA.
DR PIR; A56385; A56385.
DR PDB; 1NP1; X-ray; 2.00 A; A/B=24-207.
DR PDB; 1U17; X-ray; 1.70 A; A/B=24-207.
DR PDB; 1U18; X-ray; 1.96 A; A/B=24-207.
DR PDB; 2NP1; X-ray; 2.00 A; A/B=24-207.
DR PDB; 3NP1; X-ray; 2.30 A; A/B=24-207.
DR PDB; 4NP1; X-ray; 2.30 A; A/B=24-207.
DR PDBsum; 1NP1; -.
DR PDBsum; 1U17; -.
DR PDBsum; 1U18; -.
DR PDBsum; 2NP1; -.
DR PDBsum; 3NP1; -.
DR PDBsum; 4NP1; -.
DR AlphaFoldDB; Q26239; -.
DR SMR; Q26239; -.
DR VEuPathDB; VectorBase:RPRC000023; -.
DR HOGENOM; CLU_117833_0_0_1; -.
DR EvolutionaryTrace; Q26239; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051381; F:histamine binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070026; F:nitric oxide binding; IEA:InterPro.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond; Heme; Iron;
KW Metal-binding; Reference proteome; Secreted; Signal; Vasoactive;
KW Vasodilator.
FT SIGNAL 1..23
FT CHAIN 24..207
FT /note="Nitrophorin-1"
FT /id="PRO_0000021823"
FT BINDING 82
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 DISULFID 25..145
FT /evidence="ECO:0000269|PubMed:9546222, ECO:0000269|Ref.3"
FT DISULFID 64..194
FT /evidence="ECO:0000269|PubMed:9546222, ECO:0000269|Ref.3"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1U17"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 137..163
FT /evidence="ECO:0007829|PDB:1U17"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:1U17"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1U17"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1U17"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3NP1"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:1U17"
SQ SEQUENCE 207 AA; 22764 MW; 4AB9EE803FDA0EB8 CRC64;
MKSYTALLAV AILCLFAAVG VSGKCTKNAL AQTGFNKDKY FNGDVWYVTD YLDLEPDDVP
KRYCAALAAG TASGKLKEAL YHYDPKTQDT FYDVSELQEE SPGKYTANFK KVEKNGNVKV
DVTSGNYYTF TVMYADDSSA LIHTCLHKGN KDLGDLYAVL NRNKDTNAGD KVKGAVTAAS
LKFSDFISTK DNKCEYDNVS LKSLLTK
