HBP3_RHIAP
ID HBP3_RHIAP Reviewed; 200 AA.
AC O77422;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Male-specific histamine-binding salivary protein {ECO:0000303|PubMed:10360182};
DE Short=MS-HBP {ECO:0000303|PubMed:10360182};
DE AltName: Full=RaHBP3 {ECO:0000303|PubMed:10360182, ECO:0000303|PubMed:11058751};
DE Flags: Precursor;
OS Rhipicephalus appendiculatus (Brown ear tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Rhipicephalus.
OX NCBI_TaxID=34631;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION, AND RECOMBINANT EXPRESSION.
RC TISSUE=Salivary gland;
RX PubMed=10360182; DOI=10.1016/s1097-2765(00)80359-7;
RA Paesen G.C., Adams P.L., Harlos K., Nuttall P.A., Stuart D.I.;
RT "Tick histamine-binding proteins: isolation, cloning, and three-dimensional
RT structure.";
RL Mol. Cell 3:661-671(1999).
RN [2]
RP REVIEW.
RX PubMed=11058751; DOI=10.1016/s0167-4838(00)00168-0;
RA Paesen G.C., Adams P.L., Nuttall P.A., Stuart D.L.;
RT "Tick histamine-binding proteins: lipocalins with a second binding
RT cavity.";
RL Biochim. Biophys. Acta 1482:92-101(2000).
CC -!- FUNCTION: Salivary tick protein that acts by scavenging histamine at
CC the wound site, outcompeting histamine receptors for histamine, thereby
CC overcoming host inflammatory responses (PubMed:10360182). Binds
CC histamine with a high-affinity (Kd=1.2 nM) (PubMed:10360182). Contains
CC two binding histamine sites (H and L), that appear to bind histamine
CC with differing affinities (By similarity).
CC {ECO:0000250|UniProtKB:O77421, ECO:0000269|PubMed:10360182}.
CC -!- SUBUNIT: Homodimer; disulcde-linked. {ECO:0000305|PubMed:10360182}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10360182}.
CC -!- TISSUE SPECIFICITY: Expressed by salivary glands.
CC {ECO:0000305|PubMed:10360182}.
CC -!- DEVELOPMENTAL STAGE: Exclusively secreted by larvae, nymphs and adult
CC male ticks. {ECO:0000269|PubMed:10360182}.
CC -!- DOMAIN: Contains 2 sites/pockets that bind histamine with different
CC affinities. Site H (high affinity) is indicated here as binding to
CC histamine 1, and site L (low affinity) is indicated as binding to
CC histamine 2. {ECO:0000250|UniProtKB:O77421}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:10360182}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Histamine-binding
CC salivary protein family. {ECO:0000305}.
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DR EMBL; U96082; AAC63108.1; -; mRNA.
DR AlphaFoldDB; O77422; -.
DR SMR; O77422; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043176; F:amine binding; IEA:InterPro.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002970; Tick_his-bd.
DR Pfam; PF02098; His_binding; 1.
DR PRINTS; PR01220; HISBINDING.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..200
FT /note="Male-specific histamine-binding salivary protein"
FT /id="PRO_0000021401"
FT BINDING 37
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 37
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 41
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 56
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 59
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 97
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 115
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 125
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 138
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 138
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 154
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT BINDING 156
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 65..193
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT DISULFID 137..169
FT /evidence="ECO:0000250|UniProtKB:O77421"
FT DISULFID 168
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22852 MW; C46A1C8C6BCAA008 CRC64;
MKVLLLVLGA ALCQNADANP TWANEAKLGS YQDAWKSLQQ DQNKRYYLAQ ATQTTDGVWG
EEFTCVSVTA EKIGKKKLNA TILYKNKHLT DLKESHETIT VWKAYDYTTE NGIKYETQGT
RTQTFEDVFV FSDYKNCDVI FVPKERGSDE GDYELWVSED KIDKIPDCCK FTMAYFAQQQ
EKTVRNVYTD SSCKPAPAQN
