DPGN_DIPMA
ID DPGN_DIPMA Reviewed; 351 AA.
AC O96790;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Serine protease inhibitor dipetalogastin;
DE Short=Dipetalin;
DE Flags: Precursor; Fragment;
OS Dipetalogaster maximus (Blood-sucking bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Dipetalogaster.
OX NCBI_TaxID=72496 {ECO:0000312|EMBL:CAA10384.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=10561601; DOI=10.1046/j.1432-1327.1999.00895.x;
RA Mende K., Petoukhova O., Koulitchkova V., Schaub G.A., Lange U.,
RA Kaufmann R., Nowak G.;
RT "Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect
RT Dipetalogaster maximus: cDNA cloning, expression, and characterization.";
RL Eur. J. Biochem. 266:583-590(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 132-154, AND FUNCTION.
RX PubMed=10702701; DOI=10.1159/000022503;
RA Lange U., Keilholz W., Schaub G.A., Landmann H., Markwardt F., Nowak G.;
RT "Biochemical characterization of a thrombin inhibitor from the bloodsucking
RT bug Dipetalogaster maximus.";
RL Haemostasis 29:204-211(1999).
RN [3] {ECO:0000305}
RP STRUCTURE BY NMR OF 133-186.
RX PubMed=12051857; DOI=10.1016/s0022-2836(02)00014-1;
RA Schlott B., Woehnert J., Icke C., Hartmann M., Ramachandran R.,
RA Guehrs K.H., Glusa E., Flemming J., Goerlach M., Grosse F.,
RA Ohlenschlaeger O.;
RT "Interaction of Kazal-type inhibitor domains with serine proteinases:
RT biochemical and structural studies.";
RL J. Mol. Biol. 318:533-546(2002).
CC -!- FUNCTION: Thrombin inhibitor. Prevents blood clotting to allow insect
CC to feed on blood. Also functions as an inhibitor of trypsin and
CC plasmin. {ECO:0000269|PubMed:10561601, ECO:0000269|PubMed:10702701,
CC ECO:0000269|PubMed:12051857}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA10384.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ131524; CAA10384.1; ALT_INIT; mRNA.
DR PDB; 1KMA; NMR; -; A=132-186.
DR PDBsum; 1KMA; -.
DR AlphaFoldDB; O96790; -.
DR SMR; O96790; -.
DR MEROPS; I01.022; -.
DR MEROPS; I01.036; -.
DR MEROPS; I01.038; -.
DR MEROPS; I01.962; -.
DR EvolutionaryTrace; O96790; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0050819; P:negative regulation of coagulation; IDA:UniProtKB.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR039932; Spink4-like.
DR PANTHER; PTHR21179; PTHR21179; 6.
DR Pfam; PF00050; Kazal_1; 4.
DR Pfam; PF07648; Kazal_2; 2.
DR SMART; SM00280; KAZAL; 6.
DR SUPFAM; SSF100895; SSF100895; 6.
DR PROSITE; PS00282; KAZAL_1; 6.
DR PROSITE; PS51465; KAZAL_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Repeat; Secreted; Serine protease inhibitor.
FT PROPEP 1..131
FT /evidence="ECO:0000269|PubMed:10702701"
FT /id="PRO_0000016580"
FT CHAIN 132..351
FT /note="Serine protease inhibitor dipetalogastin"
FT /id="PRO_0000016581"
FT DOMAIN 19..69
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 72..122
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 131..181
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 184..234
FT /note="Kazal-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 240..289
FT /note="Kazal-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 297..347
FT /note="Kazal-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 141..142
FT /note="Reactive bond"
FT /evidence="ECO:0000305"
FT DISULFID 25..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 27..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 35..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 78..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 80..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 88..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 137..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 139..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 147..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 190..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 192..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 200..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 246..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 248..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 256..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 303..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 305..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 313..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT NON_TER 1
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1KMA"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1KMA"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1KMA"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1KMA"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1KMA"
SQ SEQUENCE 351 AA; 38690 MW; 8B46FA8AE4319553 CRC64;
LIKELVNMVI QHAEEEEVKE LKNPCECPRA LHRVCGSDGN TYSNPCMLNC AKHEGNPDLV
QVHKGPCDEH DHDFEDPCKC DNKFEPVCGD DQITYLNLCH LECATFTTSP GVEVAYEGEC
HAETTNAMEV LFQGNPCECP RALHRVCGSD GNTYSNPCML TCAKHEGNPD LVQVHEGPCD
EHDHDFEDTC QCDDTFQPVC GDDEITYRNL CHLECATFTT SPGVEVKHEG ECHPETKVNQ
LILKSCMCPK IYKPVCGTDG RTYPNICVLK CHISSNPGLG LAHLGECKVA VLAKETGEVR
NPCNCFRNFN PVCGTDGKTY GNLCMLGCAA ETKVPGLKLL HNGRCLPKEQ L
