NETR_PONPY
ID NETR_PONPY Reviewed; 877 AA.
AC Q5G269;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Neurotrypsin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 12;
DE Flags: Precursor;
GN Name=PRSS12;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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; AY862978; AAW57540.1; -; Genomic_DNA.
DR EMBL; AY862894; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862901; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862908; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862915; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862922; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862929; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862936; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862943; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862950; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862957; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862964; AAW57540.1; JOINED; Genomic_DNA.
DR EMBL; AY862971; AAW57540.1; JOINED; Genomic_DNA.
DR MEROPS; S01.237; -.
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; 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Kringle; Protease; Repeat;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..877
FT /note="Neurotrypsin"
FT /id="PRO_0000027667"
FT DOMAIN 95..167
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 172..273
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 282..383
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 389..489
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 502..603
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 633..876
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 31..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..632
FT /note="Zymogen activation region"
FT COMPBIAS 53..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 678
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 728
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 827
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 632..633
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..167
FT /evidence="ECO:0000250"
FT DISULFID 111..151
FT /evidence="ECO:0000250"
FT DISULFID 140..165
FT /evidence="ECO:0000250"
FT DISULFID 197..261
FT /evidence="ECO:0000250"
FT DISULFID 210..271
FT /evidence="ECO:0000250"
FT DISULFID 241..251
FT /evidence="ECO:0000250"
FT DISULFID 307..371
FT /evidence="ECO:0000250"
FT DISULFID 320..381
FT /evidence="ECO:0000250"
FT DISULFID 351..361
FT /evidence="ECO:0000250"
FT DISULFID 414..477
FT /evidence="ECO:0000250"
FT DISULFID 427..487
FT /evidence="ECO:0000250"
FT DISULFID 457..467
FT /evidence="ECO:0000250"
FT DISULFID 527..591
FT /evidence="ECO:0000250"
FT DISULFID 540..601
FT /evidence="ECO:0000250"
FT DISULFID 571..581
FT /evidence="ECO:0000250"
FT DISULFID 621..752
FT /evidence="ECO:0000255"
FT DISULFID 663..679
FT /evidence="ECO:0000250"
FT DISULFID 767..833
FT /evidence="ECO:0000250"
FT DISULFID 796..810
FT /evidence="ECO:0000250"
FT DISULFID 823..852
FT /evidence="ECO:0000250"
SQ SEQUENCE 877 AA; 97373 MW; EF96B3E7EEE587C6 CRC64;
MTLARFVLAL VLGALPEVVS FDSVLNDSLH HRHRHRHSPP PGLQYPYYLP TQQRPPRTRP
PPPLPRFPRP PRALPAQRPH ALQAGHTPRP HPWGCPAGEP WVSVTDFGAP CLQWAEVPPF
LERSPPASWA QLRGQRHNFC RSPDGAGRPW CFYGDARGKV DWGYCDCRHG SVRLRGGKNE
FEGTVEVYAS GVWGTVCSSH WDDSDASVIC HQLQLGGKGI AKQTPFSGLG LIPIYWSNVR
CQGDEENILL CEKDIWQGGV CPQKMAAAVT CSFSHGPTFP IIRLVGGSSV HEGRVELYHA
GQWGTVCDDQ WDDADAEVIC RQLSLSGIAK AWHQAYFGEG SGPVMLDEVR CTGNELSIEQ
CPKSSWGEHN CGHKEDAGVS CTPLTDGVIR LAGGKGSHEG RLEVYYRGQW GTVCDDGWTE
LNTYVVCRQL GFKFGKQASA NHFEESTGPI WLDDVSCSGK ETRFLQCSRR QWGRHDCSHR
EDVSIACYPG GEGHRLSLGF PVRLMDGENK KEGRVEVFIN GQWGTICDDG WTDKDAAVIC
RQLGYKGPAR ARTMAYFGEG KGPIHVDNVR CTGNERSLAD CIKQDIGRHN CRHSEDAGVI
CDYFGKKASG NSNKESLSSV CGLRLLHRRQ KRIIGGKNSL RGGWPWQVSL RLKSSHGDGR
LLCGATLLSS CWVLTAAHCF KRYGNSTRNY AVRVGDYHTL VPEEFEEEVG VQQIVIHREY
RPDSSDYDIA LVRLQGPEEQ CARFSSHVLP ACLPLWRERP QKTASNCYIT GWGDTGRAYS
RTLQQAAIPL LPKRFCEERY KGXFTGRMLC AGNLHEHKRV DSCQGDSGGP LMCERPGESW
VVYGVTSWGY GCGVKDSPGV YTKVSAFVPW IKSVTKL
