HPI_ANCCA
ID HPI_ANCCA Reviewed; 198 AA.
AC Q962V9; A0A368H209; A0A368H5V4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Hookworm platelet inhibitor 1 {ECO:0000303|PubMed:10191228, ECO:0000303|PubMed:12850261, ECO:0000303|PubMed:26057788};
DE Short=HPI-1 {ECO:0000303|PubMed:10191228, ECO:0000303|PubMed:12850261, ECO:0000303|PubMed:26057788};
DE Flags: Precursor;
GN ORFNames=ANCCAN_03259 {ECO:0000312|EMBL:RCN50646.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-47 AND 126-132,
RP RECOMBINANT EXPRESSION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12850261; DOI=10.1016/s0166-6851(03)00121-x;
RA Del Valle A., Jones B.F., Harrison L.M., Chadderdon R.C., Cappello M.;
RT "Isolation and molecular cloning of a secreted hookworm platelet inhibitor
RT from adult Ancylostoma caninum.";
RL Mol. Biochem. Parasitol. 129:167-177(2003).
RN [2] {ECO:0000312|EMBL:AAK81732.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-198.
RA DelValle A., Harrison L.M., Cappello M.;
RT "Cloning of the hookworm platelet inhibitor (HPI) from adult Ancylostoma
RT caninum.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:RCN50646.1, ECO:0000312|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore;
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10191228; DOI=10.1086/314724;
RA Chadderdon R.C., Cappello M.;
RT "The hookworm platelet inhibitor: functional blockade of integrins
RT GPIIb/IIIa (alphaIIbbeta3) and GPIa/IIa (alpha2beta1) inhibits platelet
RT aggregation and adhesion in vitro.";
RL J. Infect. Dis. 179:1235-1241(1999).
RN [5] {ECO:0007744|PDB:4TPV}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 20-198, DISULFIDE BONDS,
RP RECOMBINANT EXPRESSION, AND FUNCTION.
RX PubMed=26057788; DOI=10.1107/s2053230x1500271x;
RA Ma D., Francischetti I.M., Ribeiro J.M., Andersen J.F.;
RT "The structure of hookworm platelet inhibitor (HPI), a CAP superfamily
RT member from Ancylostoma caninum.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:643-649(2015).
CC -!- FUNCTION: Hookworms inhibitor of platelet aggregation and adhesion
CC (PubMed:10191228). Native protein inhibits platelet aggregation induced
CC by ADP, epinephrine, and thrombin (PubMed:10191228). In addition, it
CC prevents adhesion of resting platelets to immobilized fibrinogen and
CC collagen (PubMed:10191228). May act by binding to glycoprotein IIb/IIIa
CC (ITGA2B/ITGB3) and integrin alpha-2/beta-1 (ITGA1/ITGB1), respectively
CC (PubMed:10191228). It is noteworthy that the recombinant protein fails
CC to inhibit binding to fibrinogen (through ITGA2B/ITGB3) and collagen
CC (through ITGA1/ITGB1) (PubMed:10191228, PubMed:26057788).
CC {ECO:0000269|PubMed:10191228, ECO:0000269|PubMed:26057788}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:10191228,
CC ECO:0000305|PubMed:12850261, ECO:0000305|PubMed:26057788}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10191228,
CC ECO:0000269|PubMed:12850261}.
CC -!- TISSUE SPECIFICITY: Detected in cephalic glands.
CC {ECO:0000269|PubMed:12850261}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult stage.
CC {ECO:0000305|PubMed:12850261}.
CC -!- MISCELLANEOUS: The RGD motif is not positioned at the apex of a tight
CC turn, making it unlikely to interact with the integrin.
CC {ECO:0000305|PubMed:26057788}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=RCN50646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=RCN50647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF399709; AAK81732.1; -; mRNA.
DR EMBL; JOJR01000021; RCN50646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JOJR01000021; RCN50647.1; ALT_SEQ; Genomic_DNA.
DR PDB; 4TPV; X-ray; 1.60 A; A/B=20-198.
DR PDBsum; 4TPV; -.
DR SMR; Q962V9; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR001283; CRISP-related.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..198
FT /note="Hookworm platelet inhibitor 1"
FT /evidence="ECO:0000305|PubMed:12850261"
FT /id="PRO_0000456093"
FT DISULFID 24..65
FT /evidence="ECO:0000269|PubMed:26057788,
FT ECO:0007744|PDB:4TPV"
FT DISULFID 78..146
FT /evidence="ECO:0000269|PubMed:26057788,
FT ECO:0007744|PDB:4TPV"
FT DISULFID 141..154
FT /evidence="ECO:0000269|PubMed:26057788,
FT ECO:0007744|PDB:4TPV"
FT DISULFID 174..186
FT /evidence="ECO:0000269|PubMed:26057788,
FT ECO:0007744|PDB:4TPV"
FT DISULFID 177..195
FT /evidence="ECO:0000269|PubMed:26057788,
FT ECO:0007744|PDB:4TPV"
FT CONFLICT 63..65
FT /note="YDC -> SRH (in Ref. 3; RCN50647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22147 MW; 480DE1CFF2DF8EDE CRC64;
MSSYLLVLVA ILGFAYAEGD YSLCQQREKL DDDMREMFTE LHNGYRAAFA RNYKTSKMRT
MVYDCTLEEK AYKSAEKCSE EPSSEEENVD VFSAATLNIP LEAGNSWWSE IFELRGKVYN
KNGKTSNIAN MVWDSHDKLG CAVVDCSGKT HVVCQYGPEA KGDGKTIYEE GAPCSRCSDY
GAGVTCDDDW QNLLCIGH
