NETR_MACMU
ID NETR_MACMU Reviewed; 875 AA.
AC Q5G267;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Neurotrypsin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 12;
DE Flags: Precursor;
GN Name=PRSS12;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15627749; DOI=10.1159/000081523;
RA Xu H.L., Su B.;
RT "Genetic evidence of a strong functional constraint of neurotrypsin during
RT primate evolution.";
RL Cytogenet. Genome Res. 108:303-309(2005).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY862980; AAW57542.1; -; Genomic_DNA.
DR EMBL; AY862896; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862903; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862910; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862917; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862924; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862931; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862938; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862945; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862952; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862959; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862966; AAW57542.1; JOINED; Genomic_DNA.
DR EMBL; AY862973; AAW57542.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q5G267; -.
DR SMR; Q5G267; -.
DR STRING; 9544.ENSMMUP00000020010; -.
DR MEROPS; S01.237; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5G267; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; -; 4.
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; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 4.
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; 4.
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; Glycoprotein; Hydrolase; Kringle; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..875
FT /note="Neurotrypsin"
FT /id="PRO_0000027665"
FT DOMAIN 93..165
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 170..271
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 280..381
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 387..487
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 500..601
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 631..874
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 30..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..630
FT /note="Zymogen activation region"
FT COMPBIAS 38..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 676
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 726
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 825
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 630..631
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..165
FT /evidence="ECO:0000250"
FT DISULFID 109..149
FT /evidence="ECO:0000250"
FT DISULFID 138..163
FT /evidence="ECO:0000250"
FT DISULFID 195..259
FT /evidence="ECO:0000250"
FT DISULFID 208..269
FT /evidence="ECO:0000250"
FT DISULFID 239..249
FT /evidence="ECO:0000250"
FT DISULFID 305..369
FT /evidence="ECO:0000250"
FT DISULFID 318..379
FT /evidence="ECO:0000250"
FT DISULFID 349..359
FT /evidence="ECO:0000250"
FT DISULFID 412..475
FT /evidence="ECO:0000250"
FT DISULFID 425..485
FT /evidence="ECO:0000250"
FT DISULFID 455..465
FT /evidence="ECO:0000250"
FT DISULFID 525..589
FT /evidence="ECO:0000250"
FT DISULFID 538..599
FT /evidence="ECO:0000250"
FT DISULFID 569..579
FT /evidence="ECO:0000250"
FT DISULFID 619..750
FT /evidence="ECO:0000255"
FT DISULFID 661..677
FT /evidence="ECO:0000250"
FT DISULFID 765..831
FT /evidence="ECO:0000250"
FT DISULFID 794..808
FT /evidence="ECO:0000250"
FT DISULFID 821..850
FT /evidence="ECO:0000250"
SQ SEQUENCE 875 AA; 97187 MW; F9D918396F70464E CRC64;
MTLARFVLAL VLGALPEVVG FDSVLNDSFH HRHRHSPPPG PQYPYYLPTH QRPPRTRPPP
PLPRFPRPPR ALPAQRPHAL QAGHTPRPHP WGCPAGELWV SVTDFGAPCL RWAEVPPFLE
RSPPANWAQL RGQRHNFCRS PDGTGRPWCF YGDARGKVDW GYCDCRHGSV RLRGGKNEFE
GTVEVYASGA WGTVCSSHWD DSDASVICHQ LQLGGKGIAK QTPFSGLGLI PIYWSNVRCR
GDEENILLCE KDIWQGGVCP QKMAAAVTCS FSRGPAFPII RLVGGSSVHE GRVELYHAGQ
WGTICDDQWD DADAEVICRQ LGLSGIAKAW HQAYFGEGSG PVMLDEVRCT GNELSIEQCP
KSSWGEHNCG HKEDAGVSCT PLTDGVIRLA GGKGSHEGRL EVYYRGQWGT VCDDGWTELN
TYVVCRQLGF KYGKQASANH FEESTGPIWL DDVSCSGKET RFLQCSRRQW GQHDCSHHED
VSIACYPGSE GHRLSLGFPV RLMDGENKKE GRVEVFINGQ WGTICDDGWT DKDAAVICRQ
LGYKGPARAR TMAYFGEGKG PIHVDNVKCT GNERSLADCI KQDIGRHNCR HSEDAGVICD
YFGKKASGNS NKESLSSVCG LRLLHRRQKR IIGGKNSLRG GWPWQVSLRL KSSHGDGRLL
CGATLLSSCW VLTAAHCFKR YGNSTRNYAV RVGDYHTLVP EEFEEEIGVQ QIVIHREYRP
DSSDYDIALV RLQGPEEQCA RFSSHVLPAC LPFWRERPQK TASNCYITGW GDTGRAYSRT
LQQAAIPLLP KRFCEERYKG RFTGRMLCAG NLHEHKRVDS CQGDSGGPLM CERPGESWAV
YGVTSWGYGC GVKDSPGVYT KVSAFVPWIK SVTKL
