KUNIH_RHIMP
ID KUNIH_RHIMP Reviewed; 142 AA.
AC Q8WPI2;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Boophilin-H2 {ECO:0000303|PubMed:18286181};
DE Flags: Precursor;
OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Boophilus.
OX NCBI_TaxID=6941;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY
RP (2.35 ANGSTROMS) OF 16-142 IN COMPLEX WITH BOVINE THROMBIN, DISULFIDE
RP BONDS, INTERACTION WITH HOST THROMBIN AND TRYPSIN, FUNCTION, PROBABLE
RP PYROGLUTAMATE FORMATION AT GLN-16, AND RECOMBINANT EXPRESSION.
RX PubMed=18286181; DOI=10.1371/journal.pone.0001624;
RA Macedo-Ribeiro S., Almeida C., Calisto B.M., Friedrich T., Mentele R.,
RA Sturzebecher J., Fuentes-Prior P., Pereira P.J.;
RT "Isolation, cloning and structural characterisation of boophilin, a
RT multifunctional Kunitz-type proteinase inhibitor from the cattle tick.";
RL PLoS ONE 3:E1624-E1624(2008).
CC -!- FUNCTION: Midgut thrombin inhibitor that plays a major role in keeping
CC the midgut microenvironment at low hemostatic and inflammatory tonus
CC (PubMed:18286181) (By similarity). Also inhibits FXIa (F11), kallikrein
CC (KLK1), neutrophil elastase (ELANE) and cathepsin G (CTSG), which play
CC a role in the contact pathway of the coagulation cascade
CC (PubMed:18286181) (By similarity). Also abrogates platelet aggregation
CC by cathepsin G and plasmin, and attenuates tissue factor (F3) pathway
CC inhibitor cleavage by elastase (PubMed:18286181) (By similarity). In
CC vivo, inhibits thrombosis and promotes bleeding in mice (By
CC similarity). {ECO:0000250|UniProtKB:Q8WPI3,
CC ECO:0000269|PubMed:18286181}.
CC -!- SUBUNIT: Interacts with host thrombin and trypsin.
CC {ECO:0000269|PubMed:18286181}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18286181}.
CC -!- TISSUE SPECIFICITY: Expressed in the midgut.
CC {ECO:0000250|UniProtKB:Q8WPI3}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:18286181}.
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DR EMBL; AJ304447; CAC82583.1; -; mRNA.
DR PDB; 2ODY; X-ray; 2.35 A; E/F=16-142.
DR PDBsum; 2ODY; -.
DR AlphaFoldDB; Q8WPI2; -.
DR SMR; Q8WPI2; -.
DR MEROPS; I02.020; -.
DR VEuPathDB; VectorBase:LOC119167388; -.
DR EvolutionaryTrace; Q8WPI2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR CDD; cd00109; KU; 2.
DR Gene3D; 4.10.410.10; -; 2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; SSF57362; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Protease inhibitor;
KW Pyrrolidone carboxylic acid; Repeat; Secreted; Serine protease inhibitor;
KW Signal; Toxin.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..142
FT /note="Boophilin-H2"
FT /id="PRO_5000066993"
FT DOMAIN 21..71
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 89..139
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:18286181"
FT DISULFID 21..71
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT DISULFID 30..54
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT DISULFID 46..67
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT DISULFID 89..139
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT DISULFID 98..122
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT DISULFID 114..135
FT /evidence="ECO:0000269|PubMed:18286181,
FT ECO:0007744|PDB:2ODY"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2ODY"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2ODY"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:2ODY"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2ODY"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2ODY"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2ODY"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:2ODY"
SQ SEQUENCE 142 AA; 15538 MW; 88BF0008BBD42010 CRC64;
MKCIILLAVL GTAFAQRNGF CRLPADEGIC KALIPRFYFN TETGKCTMFS YGGCGGNENN
FETIEECQKA CGAPERVNDF ESADFKTGCE PAADSGSCAG QLERWFYNVQ SGECETFVYG
GCGGNDNNYE SEEECELVCK NM
