PRS33_HUMAN
ID PRS33_HUMAN Reviewed; 280 AA.
AC Q8NF86; A6NNQ3; Q8N171;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine protease 33;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease EOS;
DE Flags: Precursor;
GN Name=PRSS33;
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 [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12795636; DOI=10.1042/bj20030242;
RA Chen C., Darrow A.L., Qi J.-S., D'Andrea M.R., Andrade-Gordon P.;
RT "A novel serine protease predominately expressed in macrophages.";
RL Biochem. J. 374:97-107(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine protease that has amidolytic activity, cleaving its
CC substrates before Arg residues. {ECO:0000269|PubMed:12795636}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 mM for H-DL-Val-Leu-Arg-pNA {ECO:0000269|PubMed:12795636};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in macrophages. Present in
CC the spleen, small and large intestine, lung and brain (at protein
CC level). Highly expressed in peripheral leukocytes, ovary, retina,
CC spleen and stomach. Moderately expressed in thymus, uterus and
CC platelets, as well as some brain tissues, such as thalamus and fetal
CC brain. {ECO:0000269|PubMed:12795636}.
CC -!- INDUCTION: Up-regulated by phorbol myristate acetate (PMA).
CC {ECO:0000269|PubMed:12795636}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN04055.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF536382; AAN04055.1; ALT_FRAME; mRNA.
DR EMBL; AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85469.1; -; Genomic_DNA.
DR EMBL; BC036846; AAH36846.2; -; mRNA.
DR EMBL; BC062334; AAH62334.1; -; mRNA.
DR CCDS; CCDS42110.1; -.
DR RefSeq; NP_690851.2; NM_152891.2.
DR RefSeq; XP_011520753.1; XM_011522451.2.
DR RefSeq; XP_011520754.1; XM_011522452.2.
DR AlphaFoldDB; Q8NF86; -.
DR SMR; Q8NF86; -.
DR BioGRID; 129278; 46.
DR IntAct; Q8NF86; 5.
DR STRING; 9606.ENSP00000293851; -.
DR MEROPS; S01.075; -.
DR iPTMnet; Q8NF86; -.
DR PhosphoSitePlus; Q8NF86; -.
DR BioMuta; PRSS33; -.
DR DMDM; 212286047; -.
DR jPOST; Q8NF86; -.
DR MassIVE; Q8NF86; -.
DR PaxDb; Q8NF86; -.
DR PeptideAtlas; Q8NF86; -.
DR PRIDE; Q8NF86; -.
DR ProteomicsDB; 73267; -.
DR Antibodypedia; 62205; 88 antibodies from 22 providers.
DR DNASU; 260429; -.
DR Ensembl; ENST00000293851.9; ENSP00000293851.5; ENSG00000103355.14.
DR Ensembl; ENST00000570702.5; ENSP00000458369.1; ENSG00000103355.14.
DR Ensembl; ENST00000682474.1; ENSP00000507560.1; ENSG00000103355.14.
DR GeneID; 260429; -.
DR KEGG; hsa:260429; -.
DR MANE-Select; ENST00000682474.1; ENSP00000507560.1; NM_152891.3; NP_690851.2.
DR UCSC; uc002cro.1; human.
DR CTD; 260429; -.
DR DisGeNET; 260429; -.
DR GeneCards; PRSS33; -.
DR HGNC; HGNC:30405; PRSS33.
DR HPA; ENSG00000103355; Tissue enriched (fallopian).
DR MIM; 613797; gene.
DR neXtProt; NX_Q8NF86; -.
DR OpenTargets; ENSG00000103355; -.
DR PharmGKB; PA134987813; -.
DR VEuPathDB; HostDB:ENSG00000103355; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162519; -.
DR HOGENOM; CLU_006842_1_2_1; -.
DR InParanoid; Q8NF86; -.
DR OMA; WIQAHVS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8NF86; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; Q8NF86; -.
DR SignaLink; Q8NF86; -.
DR BioGRID-ORCS; 260429; 13 hits in 1061 CRISPR screens.
DR ChiTaRS; PRSS33; human.
DR GenomeRNAi; 260429; -.
DR Pharos; Q8NF86; Tbio.
DR PRO; PR:Q8NF86; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NF86; protein.
DR Bgee; ENSG00000103355; Expressed in pigmented layer of retina and 52 other tissues.
DR ExpressionAtlas; Q8NF86; baseline and differential.
DR Genevisible; Q8NF86; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..280
FT /note="Serine protease 33"
FT /id="PRO_0000299316"
FT DOMAIN 37..279
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 77
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 62..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 160..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 193..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 227..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 57
FT /note="R -> P (in Ref. 1; AAN04055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29787 MW; FCE00004DB1CFBF1 CRC64;
MRGVSCLQVL LLLVLGAAGT QGRKSAACGQ PRMSSRIVGG RDGRDGEWPW QASIQHRGAH
VCGGSLIAPQ WVLTAAHCFP RRALPAEYRV RLGALRLGST SPRTLSVPVR RVLLPPDYSE
DGARGDLALL QLRRPVPLSA RVQPVCLPVP GARPPPGTPC RVTGWGSLRP GVPLPEWRPL
QGVRVPLLDS RTCDGLYHVG ADVPQAERIV LPGSLCAGYP QGHKDACQGD SGGPLTCLQS
GSWVLVGVVS WGKGCALPNR PGVYTSVATY SPWIQARVSF
