ID A0A0J7KKG3_LASNI Unreviewed; 1394 AA.
AC A0A0J7KKG3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Neurotrypsin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=RF55_9288 {ECO:0000313|EMBL:KMQ90903.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ90903.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ90903.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ90903.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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:KMQ90903.1}.
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DR EMBL; LBMM01006124; KMQ90903.1; -; Genomic_DNA.
DR STRING; 67767.A0A0J7KKG3; -.
DR PaxDb; 67767-A0A0J7KKG3; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 3.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19331; SCAVENGER RECEPTOR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR19331:SF465; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01607; CBM_14; 3.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00530; SRCR; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00494; ChtBD2; 3.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00202; SR; 3.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 3.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF56487; SRCR-like; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 3.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 25..82
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 107..164
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 195..252
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 756..860
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 874..971
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 986..1017
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1045..1125
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1172..1275
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1324..1394
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 830..840
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 989..1012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1030..1045
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1136..1154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1148..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1244..1254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KMQ90903.1"
SQ SEQUENCE 1394 AA; 158497 MW; 2176255C2417F811 CRC64;
KPRKENIVLS SKSHHKVARY DSRLGVQCPD HNSTGQFVYP LDCKFFVNCW QGRAFVQPCA
PNTHFNPDTL ECDFPHKVKC YENKSADLRQ PLDSEFQINR KSQRLTEPKC PPYLIGLLPH
YGDCTKFVQC AHGTTYIMNC GTGTVFNPTV GVCDWPRNVK GCEDTYKSDE DDEIPLASLN
PSSGRDKSAY TEVKRITCPA DFTGLLAHPE TCKKFLQCAN GATYIMDCGP GTAFNPVTTV
CDWPYKVPSC KTDKSVDENY RTGASTWSPS ESGGTTSWST SGRYNHTTNT RNRIFQSKYN
TTMRPTIRPA WKLFTTTPSP RWIPTWTTAR SFYDHSEHVT DYHNRYGHAR EENPYKDHGS
YHSEWKPSGN LGRPSGGNYE FQHHSDRQQV ENQGNDQEPQ GTHHPDRPEG SYAHKNEDHN
YGDGYYPPGH HHHHHHHYYH NYGSNPSENA NWANPAVTSN QKYNQEHYAP NTDSNGRPNY
NYNDNPHYDY RHFEHTTPDK TDERQFQPPG KYDEDNIQFH DRHNETKFDT DGNLPANRKT
GYDFSLNRQN YSRTTPGLYH PSFNRTSPSV GNIFPNSNNK STESWDQIQD GLRQDKLSPP
WRGRENIAWN QPARSNFKPS TWRGQENRGK VQTENQTYPW DRDDYWSASD TKISNVDSGT
PNVIEPEIND YDVDVLDDKN VWKPRLVFEN KTETTTASSV IMKIGPKNTD VELFNIEAAP
YQEEEPPFPV YYIQSVQPLT HSRKFVRPTP ISGQVIRLRG GSGPNDGYVE VQGMLPGWGV
VCDSRNSWTL KEAHILCRQL GYIRGAEMAW QGRNNRNGVP TWIAANTVTC LGNETKFQSC
KFTHNQECRV DRDAIGVRCA LNRIAHCRKD EVPHNGHCYH LARPDSGLNQ AEALEHCTRR
NARLIDVTSQ AENNFVSELL LQSYPEVNSI MTSGFGFTTM NRTLWLWADS ARAKFKFTKW
WPGWMNDTKQ PPWVVNKEVR DKLKMHNYCR NPNPGKESRP WCFVGPGKYE YCDIPACGNI
EECIPSPWVC DGEEDCTNGA DERNCMLDLN LFQKSAKHKL EGYDMEKWLN TPLKSCALRC
KEADFTCRSF NHKSDGNVCL LSNGNIGLTG ALKPDKQFDY YEMRERSIDC NGMYICNNRK
CINQTQVCDG KNDCNDHSDE NICTAENLDY SIRLAGANNS YEGRIEVKIL GHWGQVCDDG
FGMINADVIC KELGFDLGAL EVRSGGFYGN LDPPTRFMVD QLKCRGNETT LRECDFNGWG
IHNCQPEEAV GIVCKTAVNT CQEGHWKCDN SPTCIPTPFI CDEVVDCPDR SDESPEHCDA
PFELRLANGS NSLQGRVEVR HHGVWGTVCD DDFTNATATV ICRSLGYGGI AIAKKDGFFG
PGQGPIWLDE VLHL
//
