ID G3UPC7_MELGA Unreviewed; 848 AA.
AC G3UPC7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Neurotrypsin {ECO:0000256|ARBA:ARBA00017669};
DE AltName: Full=Serine protease 12 {ECO:0000256|ARBA:ARBA00030576};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000017422.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000017422.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000017422.2}
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; G3UPC7; -.
DR Ensembl; ENSMGAT00000019046.2; ENSMGAP00000017422.2; ENSMGAG00000006507.3.
DR GeneTree; ENSGT00940000166242; -.
DR InParanoid; G3UPC7; -.
DR TreeFam; TF329295; -.
DR Proteomes; UP000001645; Chromosome 8.
DR Bgee; ENSMGAG00000006507; Expressed in duodenum and 10 other cell types or tissues.
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:UniProtKB-KW.
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; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
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; 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; 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 84..160
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 143..249
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 253..353
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 360..460
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 474..574
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 603..846
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 219..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 278..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 291..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 322..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 385..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 398..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 429..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 499..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 512..573
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 543..553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 848 AA; 92917 MW; 729C4B6587FFF4B2 CRC64;
MFQDLTTITV KNFFPISSLN LPSSSLKPFP LVLSLHALVK SPFQISCRPP SSTGRLLSGP
PMPSFLQAEE PQLSACPYRG TSSGCGIGPL GYYNGSLAVT EAGAECLNWA EFPDYVQQYP
DRGLGNHNHC RNPDGGTTPW CFFRLASGAI SWANCDCNQG AVRLAEDSSV ELYFGGLWGT
ICADLWTDWD ASVVCRQLAG KKNRPGLWPI PLHLQSANCH GDEKTLLQCG YQEAVSGTCN
QGSAMVTCVG APLRLVGGKE SFEGRVEVYH DGKWGTICDD QWDDRDAEVV CRQLGLSGNP
KALSWAHYGQ GSGPILLDEV ECSGNELSLD QCKKSDWGQQ NCDHIEDAGV SCNPFTEGTV
RLTGGRSPSE GRVEVYYNGD WGTVCDDGWT DLSAQVVCRQ LGFSGPATLA SEADYAAGQG
FILLDDVACV GTELSLLDCP HSNWGQHDCS HAEDVGVHCS PESNTVTGSL GPPVRLVDGE
STKEGRVEVF LNGQWGSICD DGWTDRDATV VCRQLGFSGA AKARAMAYFG EGQGPIHLDS
IECRGTEHAL GQCVRPDTGI HSCWHSEDAG VICDYVEEKV QDIRRTESSV CGMRLLHRRK
KRIIGGNKSL RGGWPWQASL RLKGFQRDTR LLCGATLISS CWVVTAAHCF KRFGVDVRRY
LLRVGDYHTG VKDEFERELP VERIVLHRNY WAGSNDNDIA LVRMRGREGH CLSFNSHVLP
ICLPDKKEKS DINRQACIIS GWGDTGKSYS RTLLQGVVPL LPREDCEVRY GQKFTNRMIC
AGNLSEDKRV DSCQGDSGGP LMCQKSNGRW IILGITSWGY GCGRKDSPGV YTKVSRYIPW
IKKVTKLK
//
