ID A0A026WBB7_OOCBI Unreviewed; 2155 AA.
AC A0A026WBB7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Neurotrypsin {ECO:0000313|EMBL:EZA53387.1};
GN ORFNames=X777_06468 {ECO:0000313|EMBL:EZA53387.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA53387.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA53387.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; KK107293; EZA53387.1; -; Genomic_DNA.
DR OMA; IMDCGPG; -.
DR Proteomes; UP000053097; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 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; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR038178; Kringle_sf.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR PANTHER; PTHR24258:SF128; TEQUILA, ISOFORM G; 1.
DR Pfam; PF01607; CBM_14; 3.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00530; SRCR; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00018; KRINGLE.
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 SMART; SM00020; Tryp_SPc; 1.
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 SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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; 3.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 216..273
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 298..355
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 385..442
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1088..1186
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1200..1335
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1354..1435
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1483..1563
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1610..1713
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1762..1862
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1910..2149
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1156..1166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1407..1430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1449..1461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1456..1474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1468..1483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1574..1592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1586..1601
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1682..1692
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1787..1851
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1800..1861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1831..1841
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 2155 AA; 243743 MW; 495757A933D907FC CRC64;
MSCGRGTEFN PAIGTCDYPL RDLTTKPPER RESVLPWHSI DKENVSRIQT GSRSLQWQQP
QDNTSSKLGR KGWSPWRKTG GSGIEQRTQI DTPDYVREQA SAEIPDQERD VKFDKLGQQE
NWKPSLECSE LIESDKNNGR FKDKSKYERC GRPQNEIDFE QKLLPRTDNI KETHVQREND
DLYEGMAIDS TKPRKENILL SQKPQHKVAG YDSQLGVQCP TLDSTGQFVY PPDCKFFVNC
WNGRAFLQPC APGTLFNPDT LECDFPHKVK CYESESASLR EPLSSESQIN KKLQRLQEPK
CPTSFTGLLP HHGDCTKFLQ CAHGATYIMN CGPGTVFNPA IGVCDWPHNV KGCEDTFKSN
EDDRVLIPPH PISGHDKSTY TEIKKITCPA DFTGLLPHPE TCKKFLQCAN GVTYVMDCSP
GTAFNPITTV CDWPYNVPSC KTDKFGGGVH RAGSDTWSPS TDVRSTTSSS GRYNPTDSHG
VLRPETSTTI RPYRPTWKPL TTTPNSRSIP TRTIMPPYFH STRPTYYHDR YGHFREGSQY
EGHRPTHPKW KPTKGLWPPE RGNQDHERDS EHYPPGHHYH HHHHHHHYHG PPVNPPANPN
WNSGNPMATT GDRRYNEGPY QGYTPNVDDT RWHPDHNHHR YPHQDGHHHF GHAAPAGTDQ
RQFPPHFPSG RHDEDNVHGV HNDTRYGIDG NLPANRPDGY DLLPNRQDYG RTSPGLHYPS
FNRTSSPAGN VFLNSTDKFP GSQHRTQEGS RQDRVSFPRP GQEHTTWNQP DGSAFKPSTW
HDQQNRQQVE TDLWDRGTTS SANKVHQWQS GINIDQQSTA DREADIKMTQ WPSKTNVFPD
PKKKVDLGTK NATQHPNTNL YPHGIYVNVN GIQGHYITKE IEDNQGRSKI QPPHDASHQK
PVSWNNTFNS TDRDHSPFHV IITATSVTPT MTQHFPSKQP ELSRRGRDFG NSTHEKELPT
LRNTNVFNTS SVPVEQDEYW SNTDATDVED LEFPEVVEPD IDDEVDILDD KNVWKPRLIF
ENKTETTTAP SVIMRIGPKN LDVELFNIEA APFQKEEPPF PIYFVQPVQP LTHSKKSVRP
TPISGQVIRL RGGSGPNNGY VEVQGVQPGW GIVCDSRNSW TLKEAHLLCK QLGYIRYTKI
YIYRMPTWIA ANTVTCLGNE TKFQSCKFTH KEECRVERDA IGVRCNPNRI AHCRKDEVPH
EGHCYHLAEP DSGLNHAEAL EHCTRRNARL IDITSQAENN FVSEWLLQSH PEVSSIMTSG
FGFTTMNRTL WLWSDSARAK FKFTKWWPGW MNDTMQPPWV GSRPLCILMK RKFPCHEQSE
SICNTDYFFW DVEDCATSSK GHSFICKRPY DNIGCVYGKG NQYTGTANVT LSGKKCLPWA
SDRIAHQLRV TVVNSEVREK LKMHNYCRNP NPARESRPWC FTEDGRHEYC DIPACGNIDP
KRSMLSGQCK PKHFECTPGE CIPSPWVCDG EEDCTNGADE RNCMVDLNLF EKSAKHKLEG
YDVEKWLNTP LKTCALRCKE ADFTCRSFSH KSDGNICLLS DSNIGLTGAL KPDKQFDYYE
MRERSVDCDN MYICSNHKCI NQTQVCDGKN DCNDRSDESI CTIENLDYDI RLAGANNTNE
GRIEVKILGY WGQVCDDGFG MINADVICKE LGFIHGALEV RPGGFYGNLD PPTRFMVDQL
KCRGNETTLR ECDFNGWGVH NCQPEEAVGI VCKIEVDTCQ EGYWKCDNSS TCIPTPFICD
EVTDCPDGSD ESSEHCDAPF ELRLANGSNP MQGRVEVRHH GVWGTVCDDD FTNATAAVIC
RSLGYGGIAI AKKDGFFGPG QGPIWLDEVF CHGNESQLYR CEHNHWGQHN CDHNEDAGVI
CSPGNINNTE IYWTDNSEFT ERSIDELLPT HCGQRAKDFD DDDDLIFQKV VHGSIAPKGT
YPWQASIRVR GHSRSNHWCG AIVISPLHVL TAAHCLEGYN KGTYFVRAGD YNTDIDEGTE
AEANIEDYYV HEEFRKGHRM NNDIALVLLK GRGIPLGKDI MPICLPFENT EYSPGLNCTI
SGFGSIETGK TAKDLRYGWV PLLDQSICRA SYVYGEGAIS EGMMCAGYLE EGNIDTCEGD
SGGPLACYHN GSFTLYGITS WGQHCGKANK PGVYVRVAHY RQWIDKKIRE SLAGR
//
