NP2_RHOPR
ID NP2_RHOPR Reviewed; 202 AA.
AC Q26241;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Nitrophorin-2;
DE Short=NP2;
DE AltName: Full=Prolixin-S;
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].
RC TISSUE=Salivary gland;
RX PubMed=8743181;
RA Sun J., Yamaguchi M., Yuda M., Miura K., Takeya H., Hirai M., Matsuoka H.,
RA Ando K., Watanabe T., Suzuki K., Chinzei Y.;
RT "Purification, characterization and cDNA cloning of a novel anticoagulant
RT of the intrinsic pathway, (prolixin-S) from salivary glands of the blood
RT sucking bug, Rhodnius prolixus.";
RL Thromb. Haemost. 75:573-577(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RA Champagne D.E., Ribeiro J.M.C.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=10692472; DOI=10.1074/jbc.275.9.6636;
RA Isawa H., Yuda M., Yoneda K., Chinzei Y.;
RT "The insect salivary protein, prolixin-S, inhibits factor IXa generation
RT and Xase complex formation in the blood coagulation pathway.";
RL J. Biol. Chem. 275:6636-6641(2000).
RN [4] {ECO:0000312|PDB:1EUO}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=10884386; DOI=10.1074/jbc.m002857200;
RA Andersen J.F., Montfort W.R.;
RT "The crystal structure of nitrophorin 2: a trifunctional antihemostatic
RT protein from the saliva of Rhodnius prolixus.";
RL J. Biol. Chem. 275:30496-30503(2000).
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 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Specifically inhibits factor IXa-catalyzed activation of
CC factor X in the presence of calcium and phospholipids irrespective of
CC the presence or absence of factor VIIIa.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the salivary glands.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Nitrophorin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U61144; AAB41587.1; -; mRNA.
DR EMBL; U70582; AAB09588.1; -; mRNA.
DR PDB; 1EUO; X-ray; 2.00 A; A=24-202.
DR PDB; 1PEE; X-ray; 1.50 A; A=24-202.
DR PDB; 1PM1; X-ray; 1.10 A; X=24-202.
DR PDB; 1T68; X-ray; 1.45 A; X=24-202.
DR PDB; 2A3F; X-ray; 1.40 A; X=24-202.
DR PDB; 2ACP; X-ray; 1.40 A; X=24-202.
DR PDB; 2AH7; X-ray; 1.70 A; X=24-202.
DR PDB; 2AL0; X-ray; 1.60 A; X=24-202.
DR PDB; 2ALL; X-ray; 1.47 A; X=24-202.
DR PDB; 2AMM; X-ray; 1.90 A; X=24-202.
DR PDB; 2ASN; X-ray; 1.70 A; X=25-202.
DR PDB; 2EU7; X-ray; 1.20 A; X=24-202.
DR PDB; 2GTF; X-ray; 1.40 A; X=24-202.
DR PDB; 2HYS; X-ray; 1.20 A; A=24-202.
DR PDBsum; 1EUO; -.
DR PDBsum; 1PEE; -.
DR PDBsum; 1PM1; -.
DR PDBsum; 1T68; -.
DR PDBsum; 2A3F; -.
DR PDBsum; 2ACP; -.
DR PDBsum; 2AH7; -.
DR PDBsum; 2AL0; -.
DR PDBsum; 2ALL; -.
DR PDBsum; 2AMM; -.
DR PDBsum; 2ASN; -.
DR PDBsum; 2EU7; -.
DR PDBsum; 2GTF; -.
DR PDBsum; 2HYS; -.
DR AlphaFoldDB; Q26241; -.
DR BMRB; Q26241; -.
DR SMR; Q26241; -.
DR STRING; 13249.RPRC000072-PA; -.
DR VEuPathDB; VectorBase:RPRC000072; -.
DR HOGENOM; CLU_117833_0_0_1; -.
DR EvolutionaryTrace; Q26241; -.
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; Disulfide bond; Heme; Iron; Metal-binding;
KW Reference proteome; Secreted; Signal; Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..202
FT /note="Nitrophorin-2"
FT /id="PRO_0000021824"
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:0000269|PubMed:10884386,
FT ECO:0007744|PDB:1EUO"
FT DISULFID 25..144
FT /evidence="ECO:0000269|PubMed:10884386,
FT ECO:0007744|PDB:1EUO"
FT DISULFID 62..193
FT /evidence="ECO:0000269|PubMed:10884386,
FT ECO:0007744|PDB:1EUO"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2AL0"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1PM1"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 99..111
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 150..162
FT /evidence="ECO:0007829|PDB:1PM1"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:1PM1"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1PM1"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1PM1"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1PM1"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1PM1"
SQ SEQUENCE 202 AA; 22292 MW; 312E96CB165D385C CRC64;
MELYTALLAV TILCLTSTMG VSGDCSTNIS PKQGLDKAKY FSGKWYVTHF LDKDPQVTDQ
YCSSFTPRES DGTVKEALYH YNANKKTSFY NIGEGKLESS GLQYTAKYKT VDKKKAVLKE
ADEKNSYTLT VLEADDSSAL VHICLREGSK DLGDLYTVLT HQKDAEPSAK VKSAVTQAGL
QLSQFVGTKD LGCQYDDQFT SL
