NETR_PANTR
ID NETR_PANTR Reviewed; 875 AA.
AC Q5G271;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Neurotrypsin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 12;
DE Flags: Precursor;
GN Name=PRSS12;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY862976; AAW57538.1; -; Genomic_DNA.
DR EMBL; AY862892; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862899; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862906; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862913; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862920; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862927; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862934; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862941; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862948; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862955; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862962; AAW57538.1; JOINED; Genomic_DNA.
DR EMBL; AY862969; AAW57538.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001065275.1; NM_001071807.2.
DR AlphaFoldDB; Q5G271; -.
DR SMR; Q5G271; -.
DR STRING; 9598.ENSPTRP00000028150; -.
DR MEROPS; S01.237; -.
DR PaxDb; Q5G271; -.
DR Ensembl; ENSPTRT00000030484; ENSPTRP00000028150; ENSPTRG00000016390.
DR GeneID; 471291; -.
DR KEGG; ptr:471291; -.
DR CTD; 8492; -.
DR VGNC; VGNC:2965; PRSS12.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158131; -.
DR HOGENOM; CLU_013656_0_0_1; -.
DR InParanoid; Q5G271; -.
DR OMA; KQDIGKH; -.
DR OrthoDB; 158600at2759; -.
DR TreeFam; TF329295; -.
DR Proteomes; UP000002277; Chromosome 4.
DR Bgee; ENSPTRG00000016390; Expressed in lung and 20 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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_0000027666"
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 29..88
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; 97160 MW; B67AE6EB6D512921 CRC64;
MTLARFVLAL MLGALPEVVG FDSVLNDSLH HSHRHSPPPG PHYPYYLPTQ QRPPRTRPPP
PLPRFPRPPR ALPAQRPHAL QAGHTPRPHP WGCPAGEPWV SVTDFGAPCL RWAEVPPFLE
RSPPASWAQL RGQRHNFCRS PDGAGRPWCF YGDARGKVDW GYCDCRHGSV RLRGGKNEFE
GTVEVYASGV WGTVCSSHWD DSDASVICHQ LQLGGKGIAK QTPFSGLGLI PIYWSNVRCR
GDEENILLCE KDIWQGGVCP QKMAAAVTCS FSHGPTFPII RLAGGSSVHE GRVELYHAGQ
WGTVCDDQWD DADAEVICRQ LGLSGIAKAW HQAYFGEGSG PVMLDEVRCT GNELSIEQCP
KSSWGEHNCG HKEDAGVSCT PLTDGVIRLA GGKGSHEGRL EVYYRGQWGT VCDDGWTELN
TYVVCRQLGF KYGKQASANH FEESTGPIWL DDVSCSGKET RFLQCSRRQW GRHDCSHRED
VSIACYPGGE GHRLSLGFPV RLVDGENKKE GRVEVFINGQ WGTICDDGWT DKDAAVICRQ
LGYKGPARAR TMAYFGEGKG PIHVDNVKCT GNERSLADCI KQDIGRHNCR HSEDAGVICD
YFGKKASGNS NKESLSSVCG LRLLHRRQKR IIGGKNSLRG GWPWQVSLRL KSSHGDGRLL
CGATLLSSCW VLTAAHCFKR YGNSTRSYAV RVGDYHTLVP EEFEEEIGVQ QIVIHREYRP
DRSDYDIALV RLQGPEEQCA RFSSHVLPAC LPLWRERPQK TASNCYITGW GDTGRAYSRT
LQQAAIPLLP KRFCEERYKR RFTGRMLCAG NLHEHKRVDS CQGDSGGPLM CERPGESWVV
YGVTSWGYGC GVKDSPGVYT KVSAFVPWIK SVTKL
