NETR_SAGLB
ID NETR_SAGLB Reviewed; 875 AA.
AC Q5G265;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Neurotrypsin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 12;
DE Flags: Precursor;
GN Name=PRSS12;
OS Saguinus labiatus (Red-chested mustached tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=78454;
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; AY862982; AAW57544.1; -; Genomic_DNA.
DR EMBL; AY862898; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862905; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862912; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862919; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862926; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862933; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862940; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862947; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862954; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862961; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862968; AAW57544.1; JOINED; Genomic_DNA.
DR EMBL; AY862975; AAW57544.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q5G265; -.
DR SMR; Q5G265; -.
DR MEROPS; S01.237; -.
DR PRIDE; Q5G265; -.
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..875
FT /note="Neurotrypsin"
FT /id="PRO_0000027668"
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 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..630
FT /note="Zymogen activation region"
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; 97180 MW; 2E860166E779E109 CRC64;
MTLARFALAL LFGVLPEVVG FESVLNDSLH HRHRHSPPPG LLYPHYLPTE QRHRRTRPPP
PLPRFPRPPR ALPALRPHAL QAGHTPEPHP RGCPAGEPWV SVTDFGAPCL RWAEVPPSLE
RSSPAGWAQL RGQRHNFCRS PDGAGRPWCF YGDARGKVDW GYCDCRHGSV RLRGSKNEFE
GTVEVYANGV WGTVCSSHWD DSDASVICHQ LQLGGKGIAK QTPFSGLGLI PVYWSNVRCR
GDEENILLCE KDIWQGGVCP QKMAAAVMCS FSHGPAFPII RLVGGSSVHE GRVELYHAGQ
WGTICDDQWD DADAEVICRQ LSLSGIAKAW HQAYFGEGSG PVMLDEVRCT GNELSIEQCP
KSSWGEHNCG HKEDAGVSCT PLTDGVIRLA GGKGSHEGRL EVYYSGQWGT VCDDGWTELN
TYVVCRQLGF KYGKQASANH FEESAGPIWL DDVSCSGKET RFLQCSRRQW GRHDCSHRED
VGIACYPGSE GHRLSLGFPV RLMDGENKKE GRVEVFINGQ WGTICDDGWT DKDAAVICRQ
LGYKGPARAR TMAYFGEGKG PIHVDNVKCT GNERSLADCI KQDIGRHNCR HSEDAGVICD
YFGKKASGNS NKESLSSVCG LRLLHRRQKR IIGGKNSLRG GWPWQVSLRL KSSHRDGRLL
CGATLLSSCW VLTAAHCFKR YGNSTRNYAV RVGDYHTLVP EEFEEEIGVQ EIVIHREYRP
DSSDYDIALV RLQGPEEQCA RFNSHVLPAC LPLWRERPQK TASNCYITGW GDTGQAYSRT
LQQAAIHLLP KRFCEERYKG RFTGRMLCAG NLHEHKHVDS CQGDSGGPLM CERPGESWVV
YGVTSWGYGC GVKDSPGVYT KVSAFVPWIK SVTKL
