BSSP4_HUMAN
ID BSSP4_HUMAN Reviewed; 317 AA.
AC Q9GZN4; O43342; Q6UXE0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Brain-specific serine protease 4;
DE Short=BSSP-4;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 22;
DE AltName: Full=Serine protease 26;
DE AltName: Full=Tryptase epsilon;
DE Flags: Precursor;
GN Name=PRSS22; Synonyms=BSSP4, PRSS26; ORFNames=SP001LA, UNQ302/PRO343;
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].
RC TISSUE=Brain;
RA Mitsui S., Okui A., Kominami K., Yamaguchi N.;
RT "Cloning and characterization of a human brain-specific serine protease,
RT hBSSP-4.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION AT ASN-70.
RC TISSUE=Pancreas;
RX PubMed=11602603; DOI=10.1074/jbc.m108677200;
RA Wong G.W., Yasuda S., Madhusudhan M.S., Li L., Yang Y., Krilis S.A.,
RA Sali A., Stevens R.L.;
RT "Human tryptase epsilon (PRSS22), a new member of the chromosome 16p13.3
RT family of human serine proteases expressed in airway epithelial cells.";
RL J. Biol. Chem. 276:49169-49182(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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: Preferentially cleaves the synthetic substrate H-D-Leu-Thr-
CC Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA.
CC {ECO:0000269|PubMed:11602603}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11602603}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the epithelial cells of the
CC airways, including trachea, esophagus and fetal lung. Scarce in adult
CC lung. Expressed at low levels in placenta, pancreas, prostate and
CC thyroid gland. {ECO:0000269|PubMed:11602603}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB93671.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAQ88762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB010779; BAB20263.1; -; mRNA.
DR EMBL; AF321182; AAG35070.1; -; mRNA.
DR EMBL; AY358396; AAQ88762.1; ALT_INIT; mRNA.
DR EMBL; AC003965; AAB93671.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC009726; AAH09726.1; -; mRNA.
DR CCDS; CCDS10481.1; -.
DR RefSeq; NP_071402.1; NM_022119.3.
DR RefSeq; XP_005255530.1; XM_005255473.3.
DR AlphaFoldDB; Q9GZN4; -.
DR SMR; Q9GZN4; -.
DR BioGRID; 122036; 25.
DR IntAct; Q9GZN4; 1.
DR STRING; 9606.ENSP00000161006; -.
DR MEROPS; S01.252; -.
DR GlyGen; Q9GZN4; 1 site.
DR iPTMnet; Q9GZN4; -.
DR BioMuta; PRSS22; -.
DR DMDM; 18202927; -.
DR MassIVE; Q9GZN4; -.
DR MaxQB; Q9GZN4; -.
DR PaxDb; Q9GZN4; -.
DR PeptideAtlas; Q9GZN4; -.
DR PRIDE; Q9GZN4; -.
DR ProteomicsDB; 80097; -.
DR TopDownProteomics; Q9GZN4; -.
DR Antibodypedia; 42617; 80 antibodies from 20 providers.
DR DNASU; 64063; -.
DR Ensembl; ENST00000161006.8; ENSP00000161006.3; ENSG00000005001.10.
DR Ensembl; ENST00000642189.2; ENSP00000495133.1; ENSG00000282937.5.
DR Ensembl; ENST00000645000.2; ENSP00000496223.1; ENSG00000282937.5.
DR GeneID; 64063; -.
DR KEGG; hsa:64063; -.
DR MANE-Select; ENST00000161006.8; ENSP00000161006.3; NM_022119.4; NP_071402.1.
DR UCSC; uc002cry.1; human.
DR CTD; 64063; -.
DR DisGeNET; 64063; -.
DR GeneCards; PRSS22; -.
DR HGNC; HGNC:14368; PRSS22.
DR HPA; ENSG00000005001; Tissue enhanced (esophagus, salivary gland, vagina).
DR MIM; 609343; gene.
DR neXtProt; NX_Q9GZN4; -.
DR OpenTargets; ENSG00000005001; -.
DR PharmGKB; PA33835; -.
DR VEuPathDB; HostDB:ENSG00000005001; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160305; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9GZN4; -.
DR OMA; NTSCWIA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9GZN4; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; Q9GZN4; -.
DR SignaLink; Q9GZN4; -.
DR BioGRID-ORCS; 64063; 7 hits in 1060 CRISPR screens.
DR GeneWiki; PRSS22; -.
DR GenomeRNAi; 64063; -.
DR Pharos; Q9GZN4; Tdark.
DR PRO; PR:Q9GZN4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9GZN4; protein.
DR Bgee; ENSG00000005001; Expressed in lower esophagus mucosa and 81 other tissues.
DR ExpressionAtlas; Q9GZN4; baseline and differential.
DR Genevisible; Q9GZN4; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; 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; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..317
FT /note="Brain-specific serine protease 4"
FT /id="PRO_0000027504"
FT DOMAIN 50..290
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11602603"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 208..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 238..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 317 AA; 33732 MW; E2A123BC86E79935 CRC64;
MVVSGAPPAL GGGCLGTFTS LLLLASTAIL NAARIPVPPA CGKPQQLNRV VGGEDSTDSE
WPWIVSIQKN GTHHCAGSLL TSRWVITAAH CFKDNLNKPY LFSVLLGAWQ LGNPGSRSQK
VGVAWVEPHP VYSWKEGACA DIALVRLERS IQFSERVLPI CLPDASIHLP PNTHCWISGW
GSIQDGVPLP HPQTLQKLKV PIIDSEVCSH LYWRGAGQGP ITEDMLCAGY LEGERDACLG
DSGGPLMCQV DGAWLLAGII SWGEGCAERN RPGVYISLSA HRSWVEKIVQ GVQLRGRAQG
GGALRAPSQG SGAAARS
