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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: TRY2_HUMAN Q5NV56_HUMAN Q6PK75_HUMAN
LinkDB: TRY2_HUMAN Q5NV56_HUMAN Q6PK75_HUMAN
Original site: TRY2_HUMAN Q5NV56_HUMAN Q6PK75_HUMAN 
ID   TRY2_HUMAN              Reviewed;         247 AA.
AC   P07478;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   27-SEP-2017, entry version 173.
DE   RecName: Full=Trypsin-2;
DE            EC=3.4.21.4;
DE   AltName: Full=Anionic trypsinogen;
DE   AltName: Full=Serine protease 2;
DE   AltName: Full=Trypsin II;
DE   Flags: Precursor;
GN   Name=PRSS2; Synonyms=TRY2, TRYP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3011602; DOI=10.1016/0378-1119(86)90111-3;
RA   Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T.,
RA   Matsubara K.;
RT   "Cloning, characterization and nucleotide sequences of two cDNAs
RT   encoding human pancreatic trypsinogens.";
RL   Gene 41:305-310(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-49.
RX   PubMed=2598466; DOI=10.1016/0009-8981(89)90254-4;
RA   Kimland M., Russick C., Marks W.H., Borgstroem A.;
RT   "Immunoreactive anionic and cationic trypsin in human serum.";
RL   Clin. Chim. Acta 184:31-46(1989).
RN   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12021776; DOI=10.1038/ni797;
RA   Ghosh D., Porter E., Shen B., Lee S.K., Wilk D., Drazba J.,
RA   Yadav S.P., Crabb J.W., Ganz T., Bevins C.L.;
RT   "Paneth cell trypsin is the processing enzyme for human defensin-5.";
RL   Nat. Immunol. 3:583-590(2002).
RN   [4]
RP   SULFATION.
RX   PubMed=17087724; DOI=10.1111/j.1742-4658.2006.05501.x;
RA   Sahin-Toth M., Kukor Z., Nemoda Z.;
RT   "Human cationic trypsinogen is sulfated on Tyr154.";
RL   FEBS J. 273:5044-5050(2006).
RN   [5]
RP   SULFATION AT TYR-154.
RX   PubMed=25010489; DOI=10.1371/journal.pone.0102063;
RA   Szabo A., Salameh M.A., Ludwig M., Radisky E.S., Sahin-Toth M.;
RT   "Tyrosine sulfation of human trypsin steers S2' subsite selectivity
RT   towards basic amino acids.";
RL   PLoS ONE 9:E102063-E102063(2014).
RN   [6]
RP   VARIANT HIS-153, AND CHARACTERIZATION OF VARIANT HIS-153.
RX   PubMed=18986305; DOI=10.1042/BJ20081848;
RA   Ronai Z., Witt H., Rickards O., Destro-Bisol G., Bradbury A.R.,
RA   Sahin-Toth M.;
RT   "A common African polymorphism abolishes tyrosine sulfation of human
RT   anionic trypsinogen (PRSS2).";
RL   Biochem. J. 418:155-161(2009).
CC   -!- FUNCTION: In the ileum, may be involved in defensin processing,
CC       including DEFA5. {ECO:0000269|PubMed:12021776}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Expressed in Paneth cells, at the base of
CC       small intestinal crypts. {ECO:0000269|PubMed:12021776}.
CC   -!- PTM: Sulfated on tyrosine. {ECO:0000269|PubMed:17087724}.
CC   -!- PTM: Sulfation at Tyr-154 increases selectivity towards basic
CC       versus apolar residues at the P2' position of inhibitors that bind
CC       in a substrate-like fashion. Although the increase in selectivity
CC       is relatively small, it may facilitate digestion of a broader
CC       range of dietary proteins. {ECO:0000269|PubMed:25010489}.
CC   -!- POLYMORPHISM: His-153 variation is a common polymorphism in
CC       African populations with a minor allele frequency of 9.2%, it
CC       eliminates sulfation at Tyr-154, with no consequences on digestive
CC       physiology. {ECO:0000269|PubMed:18986305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; M27602; AAA61232.1; -; mRNA.
DR   CCDS; CCDS83236.1; -.
DR   PIR; B25852; B25852.
DR   RefSeq; NP_002761.1; NM_002770.3.
DR   UniGene; Hs.449281; -.
DR   UniGene; Hs.726742; -.
DR   UniGene; Hs.728780; -.
DR   ProteinModelPortal; P07478; -.
DR   SMR; P07478; -.
DR   BioGrid; 111627; 15.
DR   IntAct; P07478; 1.
DR   BindingDB; P07478; -.
DR   ChEMBL; CHEMBL3159; -.
DR   DrugBank; DB04325; 2-Phenylethylamine.
DR   DrugBank; DB04410; 3-Phenylpropylamine.
DR   DrugBank; DB03127; Benzamidine.
DR   DrugBank; DB02464; Benzylamine.
DR   DrugBank; DB02325; Isopropyl Alcohol.
DR   DrugBank; DB01805; Monoisopropylphosphorylserine.
DR   DrugBank; DB01973; O-Benzylsulfonyl-Serine.
DR   DrugBank; DB03976; Phosphorylisopropane.
DR   MEROPS; S01.258; -.
DR   iPTMnet; P07478; -.
DR   PhosphoSitePlus; P07478; -.
DR   DMDM; 136413; -.
DR   EPD; P07478; -.
DR   PeptideAtlas; P07478; -.
DR   PRIDE; P07478; -.
DR   TopDownProteomics; P07478; -.
DR   DNASU; 5645; -.
DR   Ensembl; ENST00000539842; ENSP00000488338; ENSG00000275896.
DR   Ensembl; ENST00000632112; ENSP00000487952; ENSG00000282049.
DR   GeneID; 5645; -.
DR   KEGG; hsa:5645; -.
DR   CTD; 5645; -.
DR   DisGeNET; 5645; -.
DR   EuPathDB; HostDB:ENSG00000275896.4; -.
DR   GeneCards; PRSS2; -.
DR   HGNC; HGNC:9483; PRSS2.
DR   HPA; HPA062452; -.
DR   HPA; HPA063471; -.
DR   MalaCards; PRSS2; -.
DR   MIM; 601564; gene.
DR   neXtProt; NX_P07478; -.
DR   OpenTargets; ENSG00000275896; -.
DR   Orphanet; 676; Hereditary chronic pancreatitis.
DR   PharmGKB; PA33833; -.
DR   GeneTree; ENSGT00760000118862; -.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P07478; -.
DR   KO; K01312; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1462054; Alpha-defensins.
DR   Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-6803157; Antimicrobial peptides.
DR   GenomeRNAi; 5645; -.
DR   PRO; PR:P07478; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000275896; -.
DR   CleanEx; HS_PRSS2; -.
DR   ExpressionAtlas; P07478; baseline and differential.
DR   Genevisible; P07478; HS.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; TAS:Reactome.
DR   GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
DR   GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
DR   GO; GO:0007586; P:digestion; IBA:GO_Central.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; TAS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   1: Evidence at protein level;
KW   Calcium; Complete proteome; Digestion; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Metal-binding; Polymorphism; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Sulfation;
KW   Zymogen.
FT   SIGNAL        1     15       {ECO:0000269|PubMed:2598466}.
FT   PROPEP       16     23       Activation peptide.
FT                                /FTId=PRO_0000028199.
FT   CHAIN        24    247       Trypsin-2.
FT                                /FTId=PRO_0000028200.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     63     63       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    107    107       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    200    200       Charge relay system. {ECO:0000250}.
FT   METAL        75     75       Calcium. {ECO:0000250}.
FT   METAL        77     77       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        80     80       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        85     85       Calcium. {ECO:0000250}.
FT   SITE        194    194       Required for specificity. {ECO:0000250}.
FT   MOD_RES     154    154       Sulfotyrosine.
FT                                {ECO:0000305|PubMed:17087724,
FT                                ECO:0000305|PubMed:25010489}.
FT   DISULFID     30    160       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     48     64       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    171    185       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    196    220       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   VARIANT     117    117       A -> V (in dbSNP:rs11547028).
FT                                /FTId=VAR_051858.
FT   VARIANT     153    153       D -> H (abolishes tyrosine sulfation;
FT                                dbSNP:rs1804564).
FT                                {ECO:0000269|PubMed:18986305}.
FT                                /FTId=VAR_071761.
SQ   SEQUENCE   247 AA;  26488 MW;  82B0F41EB8E3D5DB CRC64;
     MNLLLILTFV AAAVAAPFDD DDKIVGGYIC EENSVPYQVS LNSGYHFCGG SLISEQWVVS
     AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPKYN SRTLDNDILL IKLSSPAVIN
     SRVSAISLPT APPAAGTESL ISGWGNTLSS GADYPDELQC LDAPVLSQAE CEASYPGKIT
     NNMFCVGFLE GGKDSCQGDS GGPVVSNGEL QGIVSWGYGC AQKNRPGVYT KVYNYVDWIK
     DTIAANS
//
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Ontology (16)   
   GO (16)   
Disease (1)   
   OMIM (1)   
Drug (9)   
   DrugBank (8)   
   CHEMBL-UP (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (13)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (3)   
   HGNC (1)   
   ENSEMBL-UP (6)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
Literature (6)   
   PubMed (6)   
All databases (58)   

Download RDF
ID   Q5NV56_HUMAN            Unreviewed;       247 AA.
AC   Q5NV56;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-SEP-2017, entry version 122.
DE   SubName: Full=Anionic trypsinogen {ECO:0000313|EMBL:AAC13351.1};
DE   SubName: Full=Protease, serine, 2 (Trypsin 2) {ECO:0000313|EMBL:AAI07785.1};
DE   SubName: Full=Protease, serine, 2 (Trypsin 2), isoform CRA_a {ECO:0000313|EMBL:EAW51922.1};
DE   SubName: Full=Trypsinogen E {ECO:0000313|EMBL:AAC80209.1};
GN   Name=TRY8 {ECO:0000313|EMBL:AAC80209.1};
GN   Synonyms=PRSS2 {ECO:0000313|EMBL:AAI07785.1}, trypsinogen 8
GN   {ECO:0000313|EMBL:AAC13351.1};
GN   ORFNames=hCG_1770551 {ECO:0000313|EMBL:EAW51922.1}, tcag7.1285
GN   {ECO:0000313|EMBL:EAL23774.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAC80209.1};
RN   [1] {ECO:0000313|EMBL:AAC80209.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8020962; DOI=10.1006/geno.1994.1149;
RA   Slightom J.L., Siemieniak D.R., Sieu L.C., Koop B.F., Hood L.;
RT   "Nucleotide sequence analysis of 77.7 kb of the human V beta T-cell
RT   receptor gene locus: direct primer-walking using cosmid template
RT   DNAs.";
RL   Genomics 20:149-168(1994).
RN   [2] {ECO:0000313|EMBL:AAC80209.1}
RP   NUCLEOTIDE SEQUENCE.
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
RT   receptor locus.";
RL   Science 272:1755-1762(1996).
RN   [3] {ECO:0000313|EMBL:AAC13351.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rowen L., Seto J., Smit A., Acharya C., Ahearn M.E., Ankener M.,
RA   Baskin D., Bumgarner R., Chen L., Chen N., Deshpende P., Faust J.,
RA   Howard S., Jerome N., Koop B.F., Lee H., Loretz C., Paeper B.,
RA   Zackrone K., Hood L.;
RT   "Sequence determination of the human T cell receptor beta locus:
RT   Strategy and error analysis.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AAC80209.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rowen L., Seto J., Smit A., Acharya C., Ahearn M.E., Ankener M.,
RA   Baskin D., Bumgarner R., Chen L., Chen N., Deshpande P., Faust J.,
RA   Howard S., Jerome N., Koop B.F., Lee H., Loretz C., Paeper B.,
RA   Zackrone K., Hood L.;
RT   "Sequence determination of the human T cell receptor beta locus:
RT   Strategy and error analysis.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AAC80209.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rowen L., Wang K., Boysen C., Ahearn M.E., Charmley P., Paeper B.,
RA   Lee I., Chen L., Trask B., Nickerson D., Seto D., Hood L.;
RT   "Sequence variation among several haplotypes in the human T cell
RT   receptor beta locus.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:EAW51922.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
RA   Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
RA   Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
RA   Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
RA   Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
RA   Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
RA   Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
RA   Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
RA   Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
RA   Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
RA   Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
RA   Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
RA   Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
RA   Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
RA   Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
RA   Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
RA   Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
RA   Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
RA   Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
RA   Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
RA   Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
RA   Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
RA   Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
RA   Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
RA   McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
RA   Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
RA   Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
RA   Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
RA   Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
RA   Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
RA   Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
RA   Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
RA   Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
RA   Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
RA   Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
RA   Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
RA   Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
RA   Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
RA   McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
RA   Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [7] {ECO:0000313|EMBL:EAL23774.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D., Zhang Q., Gu Z., Lu F.,
RA   Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J., Grzeschik K.H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Dohner H., Dohner K.,
RA   Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8] {ECO:0000313|EMBL:AAI07785.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate {ECO:0000313|EMBL:AAI07785.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9] {ECO:0000313|EMBL:EAL23774.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Nusskern D., Zhang Q., Gu Z., Lu F.,
RA   Zeesman S., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P., Lococo F., Belloni E.,
RA   Shaffer L.G., Morton C.C., Pober B., Gusella J., Bruns G., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M.,
RA   Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H.,
RA   Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.Angel.,
RA   Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E.,
RA   Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E.,
RA   Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M.,
RA   Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D.,
RA   Tsui L.-C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:EAW51922.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
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DR   EMBL; AF009664; AAC13351.1; -; Genomic_DNA.
DR   EMBL; L36092; AAC80209.1; -; Genomic_DNA.
DR   EMBL; BC107784; AAI07785.1; -; mRNA.
DR   EMBL; CH236959; EAL23774.1; -; Genomic_DNA.
DR   EMBL; CH471198; EAW51922.1; -; Genomic_DNA.
DR   RefSeq; NP_002761.1; NM_002770.3.
DR   UniGene; Hs.449281; -.
DR   UniGene; Hs.726742; -.
DR   UniGene; Hs.728780; -.
DR   SMR; Q5NV56; -.
DR   IntAct; Q5NV56; 1.
DR   MaxQB; Q5NV56; -.
DR   DNASU; 5645; -.
DR   GeneID; 5645; -.
DR   KEGG; hsa:5645; -.
DR   CTD; 5645; -.
DR   EuPathDB; HostDB:ENSG00000275896.4; -.
DR   PharmGKB; PA33833; -.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01312; -.
DR   GenomeRNAi; 5645; -.
DR   Bgee; ENSG00000275896; -.
DR   ExpressionAtlas; Q5NV56; baseline and differential.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:AAI07785.1};
KW   Serine protease {ECO:0000256|RuleBase:RU363034,
KW   ECO:0000256|SAAS:SAAS00860018}.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
SQ   SEQUENCE   247 AA;  26488 MW;  82B0F41EB8E3D5DB CRC64;
     MNLLLILTFV AAAVAAPFDD DDKIVGGYIC EENSVPYQVS LNSGYHFCGG SLISEQWVVS
     AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPKYN SRTLDNDILL IKLSSPAVIN
     SRVSAISLPT APPAAGTESL ISGWGNTLSS GADYPDELQC LDAPVLSQAE CEASYPGKIT
     NNMFCVGFLE GGKDSCQGDS GGPVVSNGEL QGIVSWGYGC AQKNRPGVYT KVYNYVDWIK
     DTIAANS
//
  All links  
Ontology (1)   
   GO (1)   
Gene (6)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (5)   
   EMBL (5)   
Protein domain (10)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
Literature (5)   
   PubMed (5)   
All databases (28)   

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ID   Q6PK75_HUMAN            Unreviewed;       187 AA.
AC   Q6PK75;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 86.
DE   SubName: Full=PRSS2 protein {ECO:0000313|EMBL:AAH05814.1};
DE   Flags: Fragment;
GN   Name=PRSS2 {ECO:0000313|EMBL:AAH05814.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAH05814.1};
RN   [1] {ECO:0000313|EMBL:AAH05814.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary {ECO:0000313|EMBL:AAH05814.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC005814; AAH05814.1; -; mRNA.
DR   RefSeq; NP_001290343.1; NM_001303414.1.
DR   RefSeq; NP_002761.1; NM_002770.3.
DR   UniGene; Hs.449281; -.
DR   UniGene; Hs.726742; -.
DR   UniGene; Hs.728780; -.
DR   ProteinModelPortal; Q6PK75; -.
DR   SMR; Q6PK75; -.
DR   PeptideAtlas; Q6PK75; -.
DR   PRIDE; Q6PK75; -.
DR   GeneID; 5645; -.
DR   KEGG; hsa:5645; -.
DR   CTD; 5645; -.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01312; -.
DR   GenomeRNAi; 5645; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407}.
FT   DOMAIN       24    187       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   NON_TER     187    187       {ECO:0000313|EMBL:AAH05814.1}.
SQ   SEQUENCE   187 AA;  20105 MW;  CAFD01BB2D02BAD7 CRC64;
     MNLLLILTFV AAAVAAPFDD DDKIVGGYIC EENSVPYQVS LNSGYHFCGG SLISEQWVVS
     AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPKYN SRTLDNDILL IKLSSPAVIN
     SRVSAISLPT APPAAGTESL ISGWGNTLSS GADYPDELQC LDAPVLSQAE CEASYPGKIT
     NNMFCVG
//
  All links  
Ontology (1)   
   GO (1)   
Gene (6)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (3)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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