ID A0A3B4H4D3_9CICH Unreviewed; 729 AA.
AC A0A3B4H4D3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Neurotrypsin {ECO:0000256|ARBA:ARBA00017669};
DE AltName: Full=Serine protease 12 {ECO:0000256|ARBA:ARBA00030576};
GN Name=PRSS12 {ECO:0000313|Ensembl:ENSPNYP00000030065.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000030065.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000030065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4H4D3; -.
DR STRING; 303518.ENSPNYP00000030065; -.
DR Ensembl; ENSPNYT00000030797.1; ENSPNYP00000030065.1; ENSPNYG00000022664.1.
DR GeneTree; ENSGT00940000158131; -.
DR Proteomes; UP000261460; 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; 3.
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:SF5; NEUROTRYPSIN; 1.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00530; SRCR; 3.
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; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56487; SRCR-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00420; SRCR_1; 2.
DR PROSITE; PS50287; SRCR_2; 3.
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}.
FT DOMAIN 59..137
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 142..242
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 249..339
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 350..450
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 475..723
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 167..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 180..241
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 211..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 308..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 375..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 388..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 419..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 729 AA; 80715 MW; 471FEE4709091C65 CRC64;
MWLHSPFALP HPLLCPLLQI RHSPNMNVPF FVLKAALLAA ISTRCYASSV PSFILPFTDC
AGSRGKDGFY RGAIDVTESG TRCMNWTEVS GFDERYPGKG IGEHNHCRNP DGRIRPWCFF
RNHRGRVDWG YCDCKQGVSL PIRLVGGRSK SEGRVEVLHA GEWGSICDDQ WDDSDAEVVC
RQLGLSGVAR AWGQAHFGKG SGRLWLDEVR CTGNELTLEQ CPKSAWGEHN CLHSEDAGVS
CNPLTDGTIR LVGGAGSHEG RLEIFYRGQW GTVCDDGWTN SNTQVVCRQL VPRFGVGLGP
ILLDDVSCTG KEPSLLLCNR REWLHHDCTH QEDVNIACSP EHNGEGLPIM RLVGGESPRE
GRVELYLSGQ WGTVCDDGWT DHDAEVVCRQ LGYSGVAKAR VMAYFGEGTG PIHVDNVKCT
GEELSLADCI KEVPGTHNCR HSEDAGVICD YGAPQPNPVD SICGLRLIHT RQRRIIGGEN
SLRGGWPWQA AIRLRGSRVD GRLVCGATLI DTCWVLTSAH CFKRYGNSTK QYKVRVGDYH
SLVPEEYEEE YGVDQIVLHP SYHTHSNDYD LALVHLSQGA VDKMPGECVS FSRHVLPACL
PMRKERVLKQ ASNCHITGWG DTGRSYSKTL QQAPLSLFPR RHCQEHFHTA FTSRMLCAGS
IHSERRVDSC RGDSGGPLVC ERPGGGWVVY GVTSWGQACR TQQSPGVYTK VSAFSSWIRK
VIGRDEKKK
//
