ID   NETR_MOUSE              Reviewed;         761 AA.
AC   O08762;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Neurotrypsin;
DE            EC=3.4.21.-;
DE   AltName: Full=Brain-specific serine protease 3;
DE            Short=BSSP-3;
DE   AltName: Full=Motopsin;
DE   AltName: Full=Serine protease 12;
DE   Flags: Precursor;
GN   Name=Prss12; Synonyms=Bssp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9245503; DOI=10.1006/mcne.1997.0616;
RA   Gschwend T.P., Krueger S.R., Kozlov S.V., Wolfer D.P., Sonderegger P.;
RT   "Neurotrypsin, a novel multidomain serine protease expressed in the nervous
RT   system.";
RL   Mol. Cell. Neurosci. 9:207-219(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9344839; DOI=10.1006/bbrc.1997.7417;
RA   Yamamura Y., Yamashiro K., Tsuruoka N., Nakazato H., Tsujimura A.,
RA   Yamaguchi N.;
RT   "Molecular cloning of a novel brain-specific serine protease with a
RT   kringle-like structure and three scavenger receptor cysteine-rich motifs.";
RL   Biochem. Biophys. Res. Commun. 239:386-392(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in neuronal plasticity and the proteolytic
CC       action may subserve structural reorganizations associated with learning
CC       and memory operations.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Most abundant in cerebral cortex, hippocampus and
CC       amygdala.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; Y13192; CAA73646.1; -; mRNA.
DR   EMBL; D89871; BAA23986.1; -; mRNA.
DR   EMBL; BC031429; AAH31429.1; -; mRNA.
DR   CCDS; CCDS17817.1; -.
DR   PIR; JC5759; JC5759.
DR   RefSeq; NP_032965.1; NM_008939.2.
DR   PDB; 6H8M; X-ray; 1.70 A; A/B=383-494.
DR   PDBsum; 6H8M; -.
DR   AlphaFoldDB; O08762; -.
DR   BMRB; O08762; -.
DR   SASBDB; O08762; -.
DR   SMR; O08762; -.
DR   BioGRID; 202403; 2.
DR   STRING; 10090.ENSMUSP00000029603; -.
DR   MEROPS; S01.237; -.
DR   GlyCosmos; O08762; 3 sites, No reported glycans.
DR   GlyGen; O08762; 3 sites.
DR   PhosphoSitePlus; O08762; -.
DR   SwissPalm; O08762; -.
DR   MaxQB; O08762; -.
DR   PaxDb; 10090-ENSMUSP00000029603; -.
DR   PeptideAtlas; O08762; -.
DR   ProteomicsDB; 287382; -.
DR   Antibodypedia; 26601; 149 antibodies from 25 providers.
DR   DNASU; 19142; -.
DR   Ensembl; ENSMUST00000029603.10; ENSMUSP00000029603.9; ENSMUSG00000027978.10.
DR   GeneID; 19142; -.
DR   KEGG; mmu:19142; -.
DR   UCSC; uc008rfl.2; mouse.
DR   AGR; MGI:1100881; -.
DR   CTD; 8492; -.
DR   MGI; MGI:1100881; Prss12.
DR   VEuPathDB; HostDB:ENSMUSG00000027978; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000158131; -.
DR   HOGENOM; CLU_013656_0_0_1; -.
DR   InParanoid; O08762; -.
DR   OMA; GPIHADN; -.
DR   OrthoDB; 3035117at2759; -.
DR   PhylomeDB; O08762; -.
DR   TreeFam; TF329295; -.
DR   BioGRID-ORCS; 19142; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Prss12; mouse.
DR   PRO; PR:O08762; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; O08762; Protein.
DR   Bgee; ENSMUSG00000027978; Expressed in sciatic nerve and 178 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0043083; C:synaptic cleft; IDA:MGI.
DR   GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR   GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR   GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:MGI.
DR   GO; GO:0031638; P:zymogen activation; IDA:MGI.
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; 3.
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:SF5; NEUROTRYPSIN; 1.
DR   PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00530; SRCR; 3.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00202; SR; 3.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF56487; SRCR-like; 3.
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; 3.
DR   PROSITE; PS50287; SRCR_2; 3.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; O08762; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Kringle; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..761
FT                   /note="Neurotrypsin"
FT                   /id="PRO_0000027670"
FT   DOMAIN          85..157
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          166..267
FT                   /note="SRCR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          273..373
FT                   /note="SRCR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          386..487
FT                   /note="SRCR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          517..760
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          25..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..516
FT                   /note="Zymogen activation region"
FT   ACT_SITE        562
FT                   /note="Charge relay system"
FT   ACT_SITE        612
FT                   /note="Charge relay system"
FT   ACT_SITE        711
FT                   /note="Charge relay system"
FT   SITE            516..517
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        85..157
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        130..155
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..255
FT                   /evidence="ECO:0000250"
FT   DISULFID        204..265
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..245
FT                   /evidence="ECO:0000250"
FT   DISULFID        298..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        341..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        411..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        424..485
FT                   /evidence="ECO:0000250"
FT   DISULFID        455..465
FT                   /evidence="ECO:0000250"
FT   DISULFID        505..636
FT                   /evidence="ECO:0000255"
FT   DISULFID        547..563
FT                   /evidence="ECO:0000250"
FT   DISULFID        651..717
FT                   /evidence="ECO:0000250"
FT   DISULFID        680..694
FT                   /evidence="ECO:0000250"
FT   DISULFID        707..736
FT                   /evidence="ECO:0000250"
FT   STRAND          386..390
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          396..403
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          406..411
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   HELIX           417..426
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          433..436
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          448..451
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   HELIX           462..464
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          465..467
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:6H8M"
FT   STRAND          482..486
FT                   /evidence="ECO:0007829|PDB:6H8M"
SQ   SEQUENCE   761 AA;  84118 MW;  DF507B03712164E6 CRC64;
     MALARCVLAV ILGALSVVAR ADPVSRSPLH RPHPSPPRSQ HAHYLPSSRR PPRTPRFPLP
     LRIPAAQRPQ VLSTGHTPPT IPRRCGAGES WGNATNLGVP CLHWDEVPPF LERSPPASWA
     ELRGQPHNFC RSPDGSGRPW CFYRNAQGKV DWGYCDCGQG PALPVIRLVG GNSGHEGRVE
     LYHAGQWGTI CDDQWDNADA DVICRQLGLS GIAKAWHQAH FGEGSGPILL DEVRCTGNEL
     SIEQCPKSSW GEHNCGHKED AGVSCVPLTD GVIRLAGGKS THEGRLEVYY KGQWGTVCDD
     GWTEMNTYVA CRLLGFKYGK QSSVNHFDGS NRPIWLDDVS CSGKEVSFIQ CSRRQWGRHD
     CSHREDVGLT CYPDSDGHRL SPGFPIRLVD GENKKEGRVE VFVNGQWGTI CDDGWTDKHA
     AVICRQLGYK GPARARTMAY FGEGKGPIHM DNVKCTGNEK ALADCVKQDI GRHNCRHSED
     AGVICDYLEK KASSSGNKEM LSSGCGLRLL HRRQKRIIGG NNSLRGAWPW QASLRLRSAH
     GDGRLLCGAT LLSSCWVLTA AHCFKRYGNN SRSYAVRVGD YHTLVPEEFE QEIGVQQIVI
     HRNYRPDRSD YDIALVRLQG PGEQCARLST HVLPACLPLW RERPQKTASN CHITGWGDTG
     RAYSRTLQQA AVPLLPKRFC KERYKGLFTG RMLCAGNLQE DNRVDSCQGD SGGPLMCEKP
     DESWVVYGVT SWGYGCGVKD TPGVYTRVPA FVPWIKSVTS L
//