NETR_MOUSE
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 03-AUG-2022, entry version 177.
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 GlyGen; O08762; 3 sites.
DR PhosphoSitePlus; O08762; -.
DR MaxQB; O08762; -.
DR PaxDb; O08762; -.
DR PeptideAtlas; O08762; -.
DR PRIDE; O08762; -.
DR ProteomicsDB; 287382; -.
DR Antibodypedia; 26601; 135 antibodies from 25 providers.
DR DNASU; 19142; -.
DR Ensembl; ENSMUST00000029603; ENSMUSP00000029603; ENSMUSG00000027978.
DR GeneID; 19142; -.
DR KEGG; mmu:19142; -.
DR UCSC; uc008rfl.2; mouse.
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; KQDIGKH; -.
DR OrthoDB; 158600at2759; -.
DR PhylomeDB; O08762; -.
DR TreeFam; TF329295; -.
DR BioGRID-ORCS; 19142; 3 hits in 71 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 175 other tissues.
DR Genevisible; O08762; MM.
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:0005044; F:scavenger receptor activity; IEA:InterPro.
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; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 3.10.250.10; -; 3.
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 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 3.
DR SUPFAM; SSF57440; SSF57440; 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.
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
