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Database: UniProt
Entry: A0A2A4JK18_HELVI
LinkDB: A0A2A4JK18_HELVI
Original site: A0A2A4JK18_HELVI 
ID   A0A2A4JK18_HELVI        Unreviewed;       996 AA.
AC   A0A2A4JK18;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Kazal-like domain-containing protein {ECO:0000259|PROSITE:PS51465};
GN   ORFNames=B5V51_1200 {ECO:0000313|EMBL:PCG72068.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG72068.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG72068.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG72068.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG72068.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG72068.1}.
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DR   EMBL; NWSH01001221; PCG72068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4JK18; -.
DR   STRING; 7102.A0A2A4JK18; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd00104; KAZAL_FS; 2.
DR   Gene3D; 3.30.60.30; -; 3.
DR   Gene3D; 3.15.10.30; Haemolymph juvenile hormone binding protein; 1.
DR   InterPro; IPR010562; Haemolymph_juvenile_hormone-bd.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR039932; Spink4-like.
DR   InterPro; IPR038606; To_sf.
DR   PANTHER; PTHR21179:SF0; SERINE PROTEASE INHIBITOR KAZAL-TYPE 4; 1.
DR   PANTHER; PTHR21179; SERINE-TYPE ENDOPEPTIDASE INHIBITOR; 1.
DR   Pfam; PF06585; JHBP; 1.
DR   Pfam; PF00050; Kazal_1; 2.
DR   Pfam; PF07648; Kazal_2; 2.
DR   SMART; SM00700; JHBP; 1.
DR   SMART; SM00280; KAZAL; 4.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 4.
DR   PROSITE; PS51465; KAZAL_2; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..996
FT                   /note="Kazal-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013195562"
FT   DOMAIN          368..421
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          453..506
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          535..588
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          612..665
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   REGION          28..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..442
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  108359 MW;  337F535C63014BD0 CRC64;
     MNNFVYIALL ICLGIVVVQG YGPKIYRKHH GNSHKSSHGS KQRPSHGSSQ HRSSQKGDSH
     HGSSRRGDSH HESSQRRGSH HGPPQKRPFH NGFNDRGSND HGPFPKLALR KRPFSPSKDT
     PFREVGHWDN SPVWTDDQGS FEISRERSGS FDNDDSDYDS RGSNDGYGPG DDSSYSRGDS
     SGPDDSGSDS GDSGYGPESG SSEEFGPSRE DGSFYSHFHS KVPCKRPNTQ PPRRTTTMKP
     TRRPRPPRPT PQPETTTTEA PTPRPTRRPT PGPTPRPTRW PTPGPTPGPT PRPTRWPTPE
     PTPRPTPGPR PNPTSRPSRS TPRPSRGTES TGTVWHPNTH TEGTTHWETT TSLPETTTEG
     EEEITTISPE ITNCIASCAS TPEYNPVCGS DGVTYDNEGK LFCANSCGVS VTLRRRSVCP
     PPSFDYEDDN DQPPPTPPPT TTLNPSVGRT TSLSGFQRCM RLCRITASFT PVCGTDLVTY
     MNMDRLKCAQ SCGEVVQVLC EKPCAACGYN PVTPKTTTLP PTTTSSSNVG RTTLVPNTKE
     CVDACPATQE YNPVCGSNSV TYKNPGHLIC AQLCGIAVTI RRFGGCSPTT ASTTTTTTTT
     TTTTTEASVT YSPAVVNCIR RCPVTSEYNP VCGTDDLTYS NLGNLECAKY CGADVELKYS
     TRCIDEFDLG PDGTTTTSST TPNINGQKDV LTTTVKSTSL FTSPTTVRTT TTKTTPITTT
     LSTSTLSSRT TATPISSTTL GFSIPQDVLD TIFKPTTTGL PLTTRTTTID PDADEDLDLD
     ARRPCRDMSP ECLKQSLQTA LPAFANGIPE LGIESLDPYI LKEISLNLPG GIEIHFINGH
     AKGLKKCIVD FARYDEDTFE TQLHCNLTIK GKYKSSGRLL VFPIDGDGES TIKCNNIKLH
     SILKLGTTVK SDGQSYLYVK SSSIDHSYDG RVSYTMTNLF KGSPEISNAV LDFMNSNWKM
     VAEEFGTPMV DFGVNSVMKN IRRLFEVVPI SELKKL
//
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