ID I3K602_ORENI Unreviewed; 830 AA.
AC I3K602;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Neurotrypsin {ECO:0000256|ARBA:ARBA00017669};
DE AltName: Full=Serine protease 12 {ECO:0000256|ARBA:ARBA00030576};
GN Name=LOC100694100 {ECO:0000313|Ensembl:ENSONIP00000016547.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016547.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016547.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in neuronal plasticity and the proteolytic
CC action may subserve structural reorganizations associated with learning
CC and memory operations. {ECO:0000256|ARBA:ARBA00002744}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR RefSeq; XP_005461495.1; XM_005461438.3.
DR AlphaFoldDB; I3K602; -.
DR STRING; 8128.ENSONIP00000016547; -.
DR MEROPS; S01.237; -.
DR Ensembl; ENSONIT00000016562.2; ENSONIP00000016547.1; ENSONIG00000013156.2.
DR GeneID; 100694100; -.
DR KEGG; onl:100694100; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000164412; -.
DR HOGENOM; CLU_013656_0_0_1; -.
DR InParanoid; I3K602; -.
DR OMA; HRNYQSS; -.
DR OrthoDB; 3035117at2759; -.
DR TreeFam; TF329295; -.
DR Proteomes; UP000005207; Linkage group LG13.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
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; PTHR48071:SF4; NEUROTRYPSIN; 1.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00530; SRCR; 4.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00130; KR; 1.
DR SMART; SM00202; SR; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56487; SRCR-like; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00420; SRCR_1; 2.
DR PROSITE; PS50287; SRCR_2; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..830
FT /note="Neurotrypsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003673944"
FT DOMAIN 52..119
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 121..219
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 228..328
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 335..435
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 452..552
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 581..824
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 188..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 253..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 266..327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 297..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 360..424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 373..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 404..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 477..541
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 490..551
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 521..531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 830 AA; 92074 MW; 1F9619A021D4CC41 CRC64;
MEQRKAVSGF VPCCLLVALA VSAEISEWAH FNVVQSAVLL SCSEGLTKLG YYNGSVSHTD
AGSPCLKWTN FPDYMQQYPN RGLGDHNFCR NPDRETKPWC FFRKTSGAIG WAYCDCHQGA
ARLVGGSGNS GRLEVYLNNK WGAVCDTHWT DRDASVICRQ LGLSEIGIAL QHSYFGPSSI
FHYERLGCRG YENSLLECWN RKFATGDCNH GNEAGVLCAE PEGTGIPLRL VGGLEEFEGR
VEVYHNGRWG TICDDQWDDL DAEVVCRQLG LGGVAKAWTR AHFGQVFGPV LLDRVQCTGN
ELSLEDCPHS NWEQHNCKHM EDAGVSCNPY TDGAVRLVGA NSDQEGRVEI YYQGQWGTVC
DDNWTELNAQ VVCRQLGFRG RAEVAHERAY EEGNGLILLD EVQCDGTETS LLACTHSQWR
QHDCSHSEDV GVLCHSDTSE IQSNYPPIGP LVRLVAGETR REGRVEVFIN GQWGSVCDDG
WNDVNAAVVC RQLGFTGVAK ARSMAYFGEG QGPIHLDNVR CLGTETSLGQ CPAEGQEGHD
CRHSEDAGVI CDYTLDPLGN GAKAMQSCGR RLSRQHRQRR IIGGEKSLRG EWPWQVSLWL
RSQSKGSHPL CGASLISSCW LVTAAHCFKR FGRDPARYVL RLGDYHTVEQ DDFERTLSPE
RIIIHRKYHS QSWEYDIALL RLKGTEGNCV AFNPHTGAVC LPEPGDKLEK RLTACVITGW
GITDSEYSHT LLQAWVPLLP ALTCKKRYGD RFTSRMLCAG SLSKHHRVDS CQGDSGGPLV
CQGESGHWVL TGVISWGHGC GNPSFPGVYT HVSRFLRWIN KAINKPYKNQ
//
