LOCUS       NP_001295138             282 aa            linear   PRI 29-APR-2025
DEFINITION  serine protease 57 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001295138 XP_011526315
VERSION     NP_001295138.2
DBSOURCE    REFSEQ: accession NM_001308209.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Lin,X., Sha,Z., Trimpert,J., Kunec,D., Jiang,C., Xiong,Y., Xu,B.,
            Zhu,Z., Xue,W. and Wu,H.
  TITLE     The NSP4 T492I mutation increases SARS-CoV-2 infectivity by
            altering non-structural protein cleavage
  JOURNAL   Cell Host Microbe 31 (7), 1170-1184 (2023)
   PUBMED   37402373
  REMARK    GeneRIF: The NSP4 T492I mutation increases SARS-CoV-2 infectivity
            by altering non-structural protein cleavage.
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wysocka,M., Gruba,N., Grzywa,R., Gieldon,A., Bachor,R.,
            Brzozowski,K., Sienczyk,M., Dieter,J., Szewczuk,Z., Rolka,K. and
            Lesner,A.
  TITLE     PEGylated substrates of NSP4 protease: A tool to study protease
            specificity
  JOURNAL   Sci Rep 6, 22856 (2016)
   PUBMED   26955973
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Kasperkiewicz,P., Poreba,M., Snipas,S.J., Lin,S.J., Kirchhofer,D.,
            Salvesen,G.S. and Drag,M.
  TITLE     Design of a Selective Substrate and Activity Based Probe for Human
            Neutrophil Serine Protease 4
  JOURNAL   PLoS One 10 (7), e0132818 (2015)
   PUBMED   26172376
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lin,S.J., Dong,K.C., Eigenbrot,C., van Lookeren Campagne,M. and
            Kirchhofer,D.
  TITLE     Structures of neutrophil serine protease 4 reveal an unusual
            mechanism of substrate recognition by a trypsin-fold protease
  JOURNAL   Structure 22 (9), 1333-1340 (2014)
   PUBMED   25156428
  REMARK    GeneRIF: Structural insights in to substrate recognition by the
            trypsin-fold protease NSP4.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Perera,N.C., Wiesmuller,K.H., Larsen,M.T., Schacher,B.,
            Eickholz,P., Borregaard,N. and Jenne,D.E.
  TITLE     NSP4 is stored in azurophil granules and released by activated
            neutrophils as active endoprotease with restricted specificity
  JOURNAL   J Immunol 191 (5), 2700-2707 (2013)
   PUBMED   23904161
  REMARK    GeneRIF: cathepsin C was identified as the activator of NSP4 in
            vivo, as cathepsin C deficiency resulted in a complete absence of
            NSP4 in a Papillon-Lefevre patient
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Perera,N.C., Schilling,O., Kittel,H., Back,W., Kremmer,E. and
            Jenne,D.E.
  TITLE     NSP4, an elastase-related protease in human neutrophils with
            arginine specificity
  JOURNAL   Proc Natl Acad Sci U S A 109 (16), 6229-6234 (2012)
   PUBMED   22474388
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Polikoff,D., Kuo,W.L., Cochran,J.F., Wernick,M., Kowbel,D.,
            Myambo,K. and Collins,C.C.
  TITLE     Assignment of protease, serine-like 1 (PRSSL1) to human chromosome
            19q13 by in situ hybridization and radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 147-148 (1997)
   PUBMED   9533035
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Okubo,K., Itoh,K., Fukushima,A., Yoshii,J. and Matsubara,K.
  TITLE     Monitoring cell physiology by expression profiles and discovering
            cell type-specific genes by compiled expression profiles
  JOURNAL   Genomics 30 (2), 178-186 (1995)
   PUBMED   8586417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112708.3 and AC004156.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 2, 2019 this sequence version replaced NP_001295138.1.
            
            Summary: This gene encodes an arginine-specific serine protease and
            member of the peptidase S1 family of proteins. The encoded protein
            may undergo proteolytic activation before storage in azurophil
            granules, in neutrophil cells of the immune system. Following
            neutrophil activation, the protease is released into the
            pericellular environment, where it may play a role in defense
            against microbial pathogens. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1. It encodes isoform 2, which is
            shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144505.1, ERR3456259.176623.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329267.9/ ENSP00000327386.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..282
                     /product="serine protease 57 isoform 2 precursor"
                     /note="serine protease 1-like protein 1; neutrophil serine
                     protease 4; protease, serine 57"
                     /calculated_mol_wt=27148
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3133
     mat_peptide     31..282
                     /product="Serine protease 57. /id=PRO_0000295853"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWY2.2)"
                     /calculated_mol_wt=27148
     Region          33..257
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            33
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(73,121,217)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PDB:4Q7X, ECO:0007744|PDB:4Q7Y,
                     ECO:0007744|PDB:4Q7Z, ECO:0007744|PDB:4Q80; propagated
                     from UniProtKB/Swiss-Prot (Q6UWY2.2)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PDB:4Q7Y, ECO:0007744|PDB:4Q7Z,
                     ECO:0007744|PDB:4Q80; propagated from UniProtKB/Swiss-Prot
                     (Q6UWY2.2)"
     Site            order(211,232,235)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..282
                     /gene="PRSS57"
                     /gene_synonym="NSP4; PRSSL1; UNQ782"
                     /coded_by="NM_001308209.2:23..871"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS77203.1"
                     /db_xref="GeneID:400668"
                     /db_xref="HGNC:HGNC:31397"
ORIGIN      
        1 mglglrgwgr plltvatalm lpvkppgswg aqiigghevt phsrpymasv rfggqhhcgg
       61 fllrarwvvs aahcfshrdl rtglvvlgah vlstaeptqq vfgidaltth pdyhpmthan
      121 dicllrlngs avlgpavgll rppgrrarpp tagtrcrvag wgfvsdfeel ppglmeakvr
      181 vldpdvcnss wkghltltml ctrsgdshrr gfcsadsggp lvcrnrahgl vsfsglwcgd
      241 pktpdvytqv safvawiwdv vrrsspqpgp lpgttrppge aa
//
