TRY6_HUMAN
ID TRY6_HUMAN Reviewed; 247 AA.
AC Q8NHM4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative trypsin-6;
DE EC=3.4.21.4;
DE AltName: Full=Serine protease 3 pseudogene 2;
DE AltName: Full=Trypsinogen C;
DE Flags: Precursor;
GN Name=PRSS3P2; Synonyms=T6, TRY6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8650574; DOI=10.1126/science.272.5269.1755;
RA Rowen L., Koop B.F., Hood L.;
RT "The complete 685-kilobase DNA sequence of the human beta T cell receptor
RT locus.";
RL Science 272:1755-1762(1996).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15313892; DOI=10.1158/0008-5472.can-04-2004;
RA Diederichs S., Bulk E., Steffen B., Ji P., Tickenbrock L., Lang K.,
RA Zanker K.S., Metzger R., Schneider P.M., Gerke V., Thomas M., Berdel W.E.,
RA Serve H., Muller-Tidow C.;
RT "S100 family members and trypsinogens are predictors of distant metastasis
RT and survival in early-stage non-small cell lung cancer.";
RL Cancer Res. 64:5564-5569(2004).
CC -!- FUNCTION: May regulate cell migration. {ECO:0000269|PubMed:15313892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Overexpressed in metastasing in non small cell lung
CC tumors, leading to an enhanced cell migration.
CC {ECO:0000269|PubMed:15313892}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Could be the product of a pseudogene. However, some data
CC suggest that it could be a protein-coding gene (PubMed:15313892).
CC {ECO:0000305|PubMed:15313892}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC231380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L36092; AAC80208.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NHM4; -.
DR SMR; Q8NHM4; -.
DR IntAct; Q8NHM4; 2.
DR MEROPS; S01.298; -.
DR iPTMnet; Q8NHM4; -.
DR PhosphoSitePlus; Q8NHM4; -.
DR BioMuta; HGNC:43788; -.
DR DMDM; 74760358; -.
DR jPOST; Q8NHM4; -.
DR MassIVE; Q8NHM4; -.
DR PeptideAtlas; Q8NHM4; -.
DR PRIDE; Q8NHM4; -.
DR ProteomicsDB; 73722; -.
DR GeneCards; PRSS3P2; -.
DR HGNC; HGNC:43788; PRSS3P2.
DR neXtProt; NX_Q8NHM4; -.
DR InParanoid; Q8NHM4; -.
DR PathwayCommons; Q8NHM4; -.
DR SignaLink; Q8NHM4; -.
DR Pharos; Q8NHM4; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q8NHM4; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 5: Uncertain;
KW Calcium; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..247
FT /note="Putative trypsin-6"
FT /id="PRO_0000337059"
FT DOMAIN 24..244
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 139..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 171..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 196..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 103
FT /note="I -> T (in Ref. 2; AAC80208)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="N -> K (in Ref. 2; AAC80208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26537 MW; 4F93CA1C93803264 CRC64;
MNPLLILAFV GAAVAVPFDD DDKIVGGYTC EENSVPYQVS LNSGSHFCGG SLISEQWVVS
AGHCYKPHIQ VRLGEHNIEV LEGNEQFINA AKIIRHPKYN RIILNNDIML IKLSTPAVIN
AHVSTISLPT APPAAGTECL ISGWGNTLSS GADYPDELQC LDAPVLTQAK CKASYPLKIT
SNMFCVGFLE GGKDSCQGDS GGPVVCNGQL QGIVSWGYGC AQKRRPGVYT KVYNYVDWIK
DTIAANS
