NETR_GORGO
ID NETR_GORGO Reviewed; 876 AA.
AC Q5G270;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Neurotrypsin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 12;
DE Flags: Precursor;
GN Name=PRSS12;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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; AY862977; AAW57539.1; -; Genomic_DNA.
DR EMBL; AY862893; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862900; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862907; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862914; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862921; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862928; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862935; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862942; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862949; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862956; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862963; AAW57539.1; JOINED; Genomic_DNA.
DR EMBL; AY862970; AAW57539.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q5G270; -.
DR SMR; Q5G270; -.
DR STRING; 9593.ENSGGOP00000002772; -.
DR MEROPS; S01.237; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5G270; -.
DR Proteomes; UP000001519; Unplaced.
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..876
FT /note="Neurotrypsin"
FT /id="PRO_0000027662"
FT DOMAIN 94..166
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 171..272
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 281..382
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 388..488
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 501..602
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 632..875
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 29..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..631
FT /note="Zymogen activation region"
FT COMPBIAS 53..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 677
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 727
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 826
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 631..632
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..166
FT /evidence="ECO:0000250"
FT DISULFID 110..150
FT /evidence="ECO:0000250"
FT DISULFID 139..164
FT /evidence="ECO:0000250"
FT DISULFID 196..260
FT /evidence="ECO:0000250"
FT DISULFID 209..270
FT /evidence="ECO:0000250"
FT DISULFID 240..250
FT /evidence="ECO:0000250"
FT DISULFID 306..370
FT /evidence="ECO:0000250"
FT DISULFID 319..380
FT /evidence="ECO:0000250"
FT DISULFID 350..360
FT /evidence="ECO:0000250"
FT DISULFID 413..476
FT /evidence="ECO:0000250"
FT DISULFID 426..486
FT /evidence="ECO:0000250"
FT DISULFID 456..466
FT /evidence="ECO:0000250"
FT DISULFID 526..590
FT /evidence="ECO:0000250"
FT DISULFID 539..600
FT /evidence="ECO:0000250"
FT DISULFID 570..580
FT /evidence="ECO:0000250"
FT DISULFID 620..751
FT /evidence="ECO:0000255"
FT DISULFID 662..678
FT /evidence="ECO:0000250"
FT DISULFID 766..832
FT /evidence="ECO:0000250"
FT DISULFID 795..809
FT /evidence="ECO:0000250"
FT DISULFID 822..851
FT /evidence="ECO:0000250"
SQ SEQUENCE 876 AA; 97259 MW; 6DA823C6732EB519 CRC64;
MTLARFVLAL MLGALPEVVG FDSVLNDSLH HSHRHSPPPG PHYPSYYLPT QQRPPRTRPP
PPLPRFPRPP RALPAQRPHA LQAGHTPRPH PWGCPAGEPW VSVTDFGARC LRWAEVPPFL
ERSPPASWAQ LRGQRHNFCR SPDGAGRPWC FYGDARGKVD WGYCDCRHGS VRLRGGKNEF
EGTVEVYASG VWGTVCSSHW DDSDASVICH QLQLGGKGIA KQTPFSGLGL IPVYWSNVRC
RGDEENILLC EKDIWQGGVC PQKMAAAVTC SFSHGPTFPI IRLAGGSSVH EGRVELYHAG
QWGTVCDDQW DDADAEVICR QLGLSGIAKA WHQAYFGEGS GPVMLDEVRC TGNELSIEQC
PKSSWGEHNC GHKEDAGVSC TPLTDGVIRL AGGKGSHEGR LEVYYRGQWG TVCDDGWTEL
NTYVVCRQLG FKYGKQASAN HFEESTGPIW LDDVSCSGKE TRFLQCSRRQ WGRHDCSHRE
DVSIACYPGG EGHRLSLGFP VRLMDGENKK EGRVEVFING QWGTICDDGW TDKDAAVICR
QLGYKGPARA RTMAYFGEGK GPIHVDNVKC TGNERSLADC IKQDIGRHNC RHSEDAGVIC
DYFGKKASGN SNKESLSSVC GLRLLHRRQK RIIGGKNSLR GGWPWQVSLR LKSYHGDGRL
LCGATLLSSC WVLTAAHCFK RYGNSTRNYA VRVGDYHTLV PEEFEEEIGV QQIVIHREYR
PDSSDYDIAL VRLQGPEEQC ARFSSHVLPA CLPLWRERPQ KTASNCYITG WGDTGRAYSR
TLQQAAIPLL PKRFCEERYK GRFTGRMLCA GNLHEHKRVD SCQGDSGGPL MCERPGESWV
VYGVTSWGYG CGVKDSPGVY TKVSAFVPWI KSVTKL
