ID A0A2U9CMT8_SCOMX Unreviewed; 958 AA.
AC A0A2U9CMT8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Neurotrypsin {ECO:0000256|ARBA:ARBA00017669};
DE AltName: Full=Serine protease 12 {ECO:0000256|ARBA:ARBA00030576};
GN ORFNames=SMAX5B_017320 {ECO:0000313|EMBL:AWP17944.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17944.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17944.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026260; AWP17944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CMT8; -.
DR STRING; 52904.ENSSMAP00000008683; -.
DR Proteomes; UP000246464; Chromosome 18.
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; 2.
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 PANTHER; PTHR48071:SF4; NEUROTRYPSIN; 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; 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; 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.
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:UP000246464}.
FT DOMAIN 85..152
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 154..254
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 263..363
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 370..470
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 491..589
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 612..861
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 925..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 179..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 192..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 223..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 288..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 301..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 332..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 395..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 408..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 439..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 558..568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 958 AA; 103520 MW; 3D71D6896D608710 CRC64;
MRLALHVVIR SVIHVHRYTC DVSSPLFCGL IFSHCDVGSL SELHSHIPPA RPLTEDYLEY
LDTAVLNKGG VPLSCSEGFT ELGYYNGTVS QTDSGAPCLK WTEFPDYVMQ YPGRGLGDHS
YCRNPDRESN PWCFFRQNSG AIGWAYCDCH QGAARLVGSS FSGSGRVEVY LNGQWGAVCD
SHWTDRDASV VCRQLGLSDI GTALQHSQFG SGSGLFHYER LGCRGDENAL SNCRSRTFVT
GDCSHGNEAA VLCAPPEGSG PPLRLVGGEE DFEGRVEVFH AGRWGSVCDD QWDDRDAEVV
CRQLGFGGVA KAWSWAHFGQ GSGPILLDAV RCTGNELFLD QCPHGDWEQH NCDHMEDAGV
SCSPYTDGVV RLVGGDSPWE GRVEVLHNGD WGTVCDDHWT QQHAEVVCRQ LGYRGHAEVV
SDGTFGEGVG LILLDDVHCA GSETSLLDCP HGIWGRTDCS HGEDVGVRCR ARSGLETNEV
PVIAPSTGPL VRLVGGGSRK EGRVEVYLHG DWGSICDSGW NDLNAAVVCR QLGHSGGAVA
ARGFGQGKGP IHLDQVRCTG KEEFLGECPS LGQSFQSCRR REDAGARCDA APTQESAAQA
KPEERSCGLR KLVVGEGEGS KGRSQGEENT LRTTWPWQVS VWLQSQEKDG GPLCSGTLIS
PCWALTSAHC VSRFGSDPSR YVVRVGASER TLTPERVVVH RKYKGQSGGH DLALMKLPSA
KGHCLTFDPN TNAACLSAAD TESGGNAPSS CVVMVTAAWT GPDSVLASWV PLMSSWQCKK
RYGDSFSSHG TLCAGSPPDT SLLHGNSCQG NSGGGLLCQG ETGRWVLTGL VAGGYSCADP
SSPALYTRVS RFRSWIDEVV GVREEPQAHT QTRGDLTHND LTHAREERAH GEGKDEYFHT
HGKVKPAHDQ QQTNEIGEIK QKHAHAHHPH TDQHVDVHTK STHAHHVGES DTNTQILV
//
