ID A0A3Q1ENH5_9TELE Unreviewed; 834 AA.
AC A0A3Q1ENH5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Neurotrypsin {ECO:0000256|ARBA:ARBA00017669};
DE AltName: Full=Serine protease 12 {ECO:0000256|ARBA:ARBA00030576};
GN Name=PRSS12 {ECO:0000313|Ensembl:ENSAPOP00000005002.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000005002.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000005002.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002744}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A3Q1ENH5; -.
DR STRING; 80966.ENSAPOP00000005002; -.
DR Ensembl; ENSAPOT00000009091.1; ENSAPOP00000005002.1; ENSAPOG00000006675.1.
DR GeneTree; ENSGT00940000158131; -.
DR InParanoid; A0A3Q1ENH5; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
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; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR48071:SF18; LCCL_LECTIN ADHESIVE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00530; SRCR; 4.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00130; KR; 1.
DR SMART; SM00202; SR; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56487; SRCR-like; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00420; SRCR_1; 4.
DR PROSITE; PS50287; SRCR_2; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..834
FT /note="Neurotrypsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018688070"
FT DOMAIN 32..110
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 112..210
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 220..320
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 327..434
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 448..548
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 580..828
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 137..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 181..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 245..309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 258..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 289..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 403..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 473..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 486..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 517..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 834 AA; 91529 MW; 1E2349154A9FE827 CRC64;
MNFLALTAAL WAAMSGGGDS SSVPSFILPF TDCVRSRGKD GFYRGAIDVT ESGSRCMNWT
EVAGFTERYP GKGIGEHNHC RNPDGRIRPW CFFRSVRGRV DWGYCDCKQG SVRLQGGRSK
LDGRVEVYLG GVWGSVCSDE WGDEDAAVVC RQLGKGISGC ARAVPLFNPS MARLHWMAVH
CQGDEQDLLQ CPKTTWNGGE CSLAAAVTCT QQKAAVQLPV RLVGGRSGSE GTVEVFHAGQ
WGSICDDQWD NSDAEVVCRQ LGLSGFARAW RQAHFGKGSG RVWLDEVRCT GNELTLDQCP
KGAWGEHNCL HSEDAGVSCN PLTDGTTRLV GGAGSHEGRL EIFYHGQWGT VCDDGWTDSN
TQVVCRQLGY RLGETLLSEG LDITPVPRFG VGSGPILLDD VSCTGKEPSL LLCKRREWLR
HDCTHHEDVN IACSPERSGE SLPTSVPVRL MGGESPREGR VELYLSGQWG TVCDDGWTDH
DAEVVCRQLG FSGVAKARVM AYFGEGTGPI HVDNVKCSGE ERSLADCIKQ VPGTHNCRHS
EDAGVICDYG ESQPHNTKEV KDPVNSICGL RLIHIRQRRI IGGENSLRGG WPWQAAIRLR
GSRGDGRLVC GATLIDTCWV LTSAHCFKRY GNSTKQYKVR VGDYHSLVPE EYEEEYGVDQ
IVLHPSYHSH SNDYDLALVR LSPGALGQMP GECVSFSRHV LPACLPMRKE RVVKQASNCH
ITGWGDTGRS YSKTLQQAPL SLLPRRHCQQ HFHGAFTSRM LCAGSIQSER RVDSCRGDSG
GPLVCERPGG GWVVYGVTSW GHACRTQQSP GVYTKVSAFS SWIRKVIERE EKQR
//
