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Protein

Serine protease 57

Gene

PRSS57

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease that cleaves preferentially after Arg residues (PubMed:22474388, PubMed:23904161, PubMed:25156428). Can also cleave after citrulline (deimidated arginine) and methylarginine residues (PubMed:25156428).3 Publications

Enzyme regulationi

Inhibited by SERPINA1, SERPINC1 and SERPING1.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei74Charge relay system1 Publication1
Active sitei122Charge relay system1 Publication1
Active sitei218Charge relay system1 Publication1

GO - Molecular functioni

  • heparin binding Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease 57 (EC:3.4.21.-3 Publications)
Alternative name(s):
Neutrophil serine protease 42 Publications
Short name:
NSP43 Publications
Serine protease 1-like protein 1
Gene namesi
Name:PRSS57
Synonyms:PRSSL1
ORF Names:UNQ782/PRO1599
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:31397. PRSS57.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule lumen Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi213F → A: Decreases enzyme activity tenfold. 1 Publication1
Mutagenesisi215S → A: Decreases enzyme activity tenfold. Decreases enzyme activity twentyfold; when associated with G-236. 1 Publication1
Mutagenesisi235S → G: Decreases enzyme activity tenfold. Decreases enzyme activity twentyfold; when associated with A-215. 1 Publication1

Organism-specific databases

DisGeNETi400668.
OpenTargetsiENSG00000185198.
PharmGKBiPA164742285.

Polymorphism and mutation databases

BioMutaiPRSS57.
DMDMi296452873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000029585332 – 283Serine protease 57Add BLAST252

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 75PROSITE-ProRule annotationCombined sources
Glycosylationi129N-linked (GlcNAc...)Combined sources1
Disulfide bondi157 ↔ 224PROSITE-ProRule annotationCombined sources
Disulfide bondi188 ↔ 202PROSITE-ProRule annotationCombined sources
Glycosylationi189N-linked (GlcNAc...)Combined sources1
Disulfide bondi214 ↔ 239PROSITE-ProRule annotationCombined sources

Post-translational modificationi

After cleavage of the signal peptide, the N-terminus is probably further processed by CTSC (PubMed:22474388, PubMed:23904161). Processing by CTSC is probably required for accumulation in cytoplasmic granules; in the absence of CTSC the protein does not accumulate (PubMed:23904161).1 Publication1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ6UWY2.
PaxDbiQ6UWY2.
PeptideAtlasiQ6UWY2.
PRIDEiQ6UWY2.

Expressioni

Tissue specificityi

Detected in peripheral blood neutrophil granulocytes, but not in other types of leukocytes. Detected in neutrophils and neutrophil precursors in bone marrow (at protein level) (PubMed:22474388, PubMed:23904161). Detected in myeloblasts and promyelocytes in bone marrow (PubMed:23904161).2 Publications

Gene expression databases

BgeeiENSG00000185198.
CleanExiHS_PRSSL1.
ExpressionAtlasiQ6UWY2. baseline and differential.

Organism-specific databases

HPAiHPA005894.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000327386.

Structurei

Secondary structure

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 53Combined sources6
Beta strandi56 – 65Combined sources10
Beta strandi68 – 71Combined sources4
Helixi73 – 76Combined sources4
Helixi81 – 83Combined sources3
Beta strandi84 – 89Combined sources6
Beta strandi101 – 103Combined sources3
Beta strandi105 – 110Combined sources6
Turni116 – 118Combined sources3
Beta strandi124 – 130Combined sources7
Beta strandi135 – 137Combined sources3
Beta strandi156 – 163Combined sources8
Beta strandi176 – 183Combined sources8
Helixi185 – 191Combined sources7
Turni192 – 194Combined sources3
Beta strandi200 – 204Combined sources5
Beta strandi206 – 209Combined sources4
Beta strandi221 – 224Combined sources4
Beta strandi227 – 234Combined sources8
Beta strandi247 – 250Combined sources4
Helixi251 – 254Combined sources4
Helixi255 – 264Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q7XX-ray2.55A/B34-283[»]
4Q7YX-ray2.70A34-283[»]
4Q7ZX-ray1.40A34-283[»]
4Q80X-ray3.07A/B34-283[»]
ProteinModelPortaliQ6UWY2.
SMRiQ6UWY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 263Peptidase S1PROSITE-ProRule annotationAdd BLAST230

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOVERGENiHBG013304.
InParanoidiQ6UWY2.
OMAiRARWVVS.
OrthoDBiEOG091G0GHJ.
PhylomeDBiQ6UWY2.
TreeFamiTF333630.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UWY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLGLRGWGR PLLTVATALM LPVKPPAGSW GAQIIGGHEV TPHSRPYMAS
60 70 80 90 100
VRFGGQHHCG GFLLRARWVV SAAHCFSHRD LRTGLVVLGA HVLSTAEPTQ
110 120 130 140 150
QVFGIDALTT HPDYHPMTHA NDICLLRLNG SAVLGPAVGL LRPPGRRARP
160 170 180 190 200
PTAGTRCRVA GWGFVSDFEE LPPGLMEAKV RVLDPDVCNS SWKGHLTLTM
210 220 230 240 250
LCTRSGDSHR RGFCSADSGG PLVCRNRAHG LVSFSGLWCG DPKTPDVYTQ
260 270 280
VSAFVAWIWD VVRRSSPQPG PLPGTTRPPG EAA
Length:283
Mass (Da):30,334
Last modified:May 18, 2010 - v2
Checksum:i62A09B03C20CBDDA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051839143P → L.2 PublicationsCorresponds to variant rs8102982dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358594 mRNA. Translation: AAQ88957.1.
AC004156 Genomic DNA. No translation available.
AC112708 Genomic DNA. No translation available.
BC137161 mRNA. Translation: AAI37162.1.
CCDSiCCDS12041.1.
RefSeqiNP_999875.1. NM_214710.4.
UniGeneiHs.245146.

Genome annotation databases

EnsembliENST00000613411; ENSP00000482358; ENSG00000185198.
GeneIDi400668.
KEGGihsa:400668.
UCSCiuc002lpl.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358594 mRNA. Translation: AAQ88957.1.
AC004156 Genomic DNA. No translation available.
AC112708 Genomic DNA. No translation available.
BC137161 mRNA. Translation: AAI37162.1.
CCDSiCCDS12041.1.
RefSeqiNP_999875.1. NM_214710.4.
UniGeneiHs.245146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q7XX-ray2.55A/B34-283[»]
4Q7YX-ray2.70A34-283[»]
4Q7ZX-ray1.40A34-283[»]
4Q80X-ray3.07A/B34-283[»]
ProteinModelPortaliQ6UWY2.
SMRiQ6UWY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000327386.

Polymorphism and mutation databases

BioMutaiPRSS57.
DMDMi296452873.

Proteomic databases

EPDiQ6UWY2.
PaxDbiQ6UWY2.
PeptideAtlasiQ6UWY2.
PRIDEiQ6UWY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000613411; ENSP00000482358; ENSG00000185198.
GeneIDi400668.
KEGGihsa:400668.
UCSCiuc002lpl.2. human.

Organism-specific databases

CTDi400668.
DisGeNETi400668.
GeneCardsiPRSS57.
HGNCiHGNC:31397. PRSS57.
HPAiHPA005894.
neXtProtiNX_Q6UWY2.
OpenTargetsiENSG00000185198.
PharmGKBiPA164742285.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOVERGENiHBG013304.
InParanoidiQ6UWY2.
OMAiRARWVVS.
OrthoDBiEOG091G0GHJ.
PhylomeDBiQ6UWY2.
TreeFamiTF333630.

Miscellaneous databases

GenomeRNAii400668.
PROiQ6UWY2.

Gene expression databases

BgeeiENSG00000185198.
CleanExiHS_PRSSL1.
ExpressionAtlasiQ6UWY2. baseline and differential.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRS57_HUMAN
AccessioniPrimary (citable) accession number: Q6UWY2
Secondary accession number(s): B2RNW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.