HBP2_RHIAP
ID HBP2_RHIAP Reviewed; 190 AA.
AC O77421;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Female-specific histamine-binding protein 2 {ECO:0000303|PubMed:10360182};
DE Short=FS-HBP2 {ECO:0000303|PubMed:10360182};
DE AltName: Full=RaHBP2 {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] {ECO:0000312|PDB:1QFT, ECO:0000312|PDB:1QFV}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS),
RP FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, 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).
RN [3] {ECO:0000312|PDB:3G7X, ECO:0000312|PDB:3GAQ}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 20-190.
RA Syme N.R., Dennis C.A., Bronowska A., Paesen G., Homans S.W.;
RT "Entropic contributions to binding in a 'Hydrophilic' Ligand-Protein
RT interaction.";
RL Submitted (FEB-2009) to the PDB data bank.
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=1.7 nM) (PubMed:10360182). Contains
CC two binding histamine sites (H and L), that appear to bind histamine
CC with differing affinities (PubMed:10360182).
CC {ECO:0000269|PubMed:10360182}.
CC -!- SUBUNIT: Monomer. {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: Early stage of adult feeding.
CC {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:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Histamine-binding
CC salivary protein family. {ECO:0000305}.
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DR EMBL; U96081; AAC63107.1; -; mRNA.
DR PDB; 1QFT; X-ray; 1.25 A; A/B=20-190.
DR PDB; 1QFV; X-ray; 1.36 A; A/B=20-190.
DR PDB; 3G7X; X-ray; 1.55 A; A/B=20-190.
DR PDB; 3GAQ; X-ray; 2.25 A; A/B=20-190.
DR PDBsum; 1QFT; -.
DR PDBsum; 1QFV; -.
DR PDBsum; 3G7X; -.
DR PDBsum; 3GAQ; -.
DR AlphaFoldDB; O77421; -.
DR SMR; O77421; -.
DR EvolutionaryTrace; O77421; -.
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 3D-structure; Disulfide bond; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..190
FT /note="Female-specific histamine-binding protein 2"
FT /id="PRO_0000021400"
FT BINDING 39
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 39
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 43
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 55
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182"
FT BINDING 58
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182"
FT BINDING 61
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182"
FT BINDING 101
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFV, ECO:0007744|PDB:3G7X"
FT BINDING 117
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182"
FT BINDING 119
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 127
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182"
FT BINDING 139
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 139
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT"
FT BINDING 154
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFV, ECO:0007744|PDB:3G7X"
FT BINDING 156
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10360182"
FT DISULFID 67..188
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT, ECO:0007744|PDB:1QFV,
FT ECO:0007744|PDB:3G7X, ECO:0007744|PDB:3GAQ"
FT DISULFID 138..167
FT /evidence="ECO:0000269|PubMed:10360182,
FT ECO:0007744|PDB:1QFT, ECO:0007744|PDB:1QFV,
FT ECO:0007744|PDB:3G7X, ECO:0007744|PDB:3GAQ"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1QFT"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1QFT"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1QFT"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1QFT"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1QFT"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1QFT"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:1QFT"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1QFT"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1QFT"
SQ SEQUENCE 190 AA; 21464 MW; 6923A3E902552B6F CRC64;
MKLLILSLAL VLALSQVKGN QPDWADEAAN GAHQDAWKSL KADVENVYYM VKATYKNDPV
WGNDFTCVGV MANDVNEDEK SIQAEFLFMN NADTNMQFAT EKVTAVKMYG YNRENAFRYE
TEDGQVFTDV IAYSDDNCDV IYVPGTDGNE EGYELWTTDY DNIPANCLNK FNEYAVGRET
RDVFTSACLE
