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Q16651 (PRSS8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostasin

EC=3.4.21.-
Alternative name(s):
Channel-activating protease 1
Short name=CAP1
Serine protease 8

Cleaved into the following 2 chains:

  1. Prostasin light chain
  2. Prostasin heavy chain
Gene names
Name:PRSS8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). Ref.4 Ref.5

Subunit structure

Heterodimer of two chains, light and heavy, held by a disulfide bond.

Subcellular location

Prostasin: Cell membrane; Single-pass membrane protein.

Prostasin light chain: Secretedextracellular space. Note: Found in the seminal fluid. Secreted after cleavage of its C-terminus.

Prostasin heavy chain: Secretedextracellular space. Note: Found in the seminal fluid. Secreted after cleavage of its C-terminus.

Tissue specificity

Found in prostate, liver, salivary gland, kidney, lung, pancreas, colon, bronchus and renal proximal tubular cells. In the prostate gland it may be synthesized in epithelial cells, secreted into the ducts, and excreted into the seminal fluid.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 323Activation peptide
PRO_0000028027
Chain33 – 343311Prostasin
PRO_0000240511
Chain33 – 4412Prostasin light chain
PRO_0000028028
Chain45 – 322278Prostasin heavy chain
PRO_0000028029
Propeptide323 – 34321
PRO_0000028030

Regions

Transmembrane320 – 34021Helical; Potential
Domain45 – 286242Peptidase S1

Sites

Active site851Charge relay system
Active site1341Charge relay system
Active site2381Charge relay system

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...) Potential
Disulfide bond37 ↔ 154Interchain (between light and heavy chains) By similarity
Disulfide bond70 ↔ 86 Ref.6
Disulfide bond168 ↔ 244 Ref.6
Disulfide bond201 ↔ 223 Ref.6
Disulfide bond234 ↔ 262 Ref.6

Secondary structure

................................................ 343
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16651 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 98DD6447F5A8C1B2

FASTA34336,431
        10         20         30         40         50         60 
MAQKGVLGPG QLGAVAILLY LGLLRSGTGA EGAEAPCGVA PQARITGGSS AVAGQWPWQV 

        70         80         90        100        110        120 
SITYEGVHVC GGSLVSEQWV LSAAHCFPSE HHKEAYEVKL GAHQLDSYSE DAKVSTLKDI 

       130        140        150        160        170        180 
IPHPSYLQEG SQGDIALLQL SRPITFSRYI RPICLPAANA SFPNGLHCTV TGWGHVAPSV 

       190        200        210        220        230        240 
SLLTPKPLQQ LEVPLISRET CNCLYNIDAK PEEPHFVQED MVCAGYVEGG KDACQGDSGG 

       250        260        270        280        290        300 
PLSCPVEGLW YLTGIVSWGD ACGARNRPGV YTLASSYASW IQSKVTELQP RVVPQTQESQ 

       310        320        330        340 
PDSNLCGSHL AFSSAPAQGL LRPILFLPLG LALGLLSPWL SEH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, tissue-specific expression, and cellular localization of human prostasin mRNA."
Yu J.X., Chao L., Chao J.
J. Biol. Chem. 270:13483-13489(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Prostate.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"Prostasin is a novel human serine proteinase from seminal fluid. Purification, tissue distribution, and localization in prostate gland."
Yu J.X., Chao L., Chao J.
J. Biol. Chem. 269:18843-18848(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-64.
Tissue: Semen.
[4]"Prostasin, a membrane-anchored serine peptidase, regulates sodium currents in JME/CF15 cells, a cystic fibrosis airway epithelial cell line."
Tong Z., Illek B., Bhagwandin V.J., Verghese G.M., Caughey G.H.
Am. J. Physiol. 287:L928-L935(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SODIUM CHANNELS ACTIVATION.
[5]"Biochemical characterization of prostasin, a channel activating protease."
Shipway A., Danahay H., Williams J.A., Tully D.C., Backes B.J., Harris J.L.
Biochem. Biophys. Res. Commun. 324:953-963(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
[6]"Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations."
Spraggon G., Hornsby M., Shipway A., Tully D.C., Bursulaya B., Danahay H., Harris J.L., Lesley S.A.
Protein Sci. 18:1081-1094(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 45-305 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41351 mRNA. Translation: AAC41759.1.
U33446 Genomic DNA. Translation: AAB19071.1.
BC001462 mRNA. Translation: AAH01462.1.
CCDSCCDS45469.1.
PIRA57014.
RefSeqNP_002764.1. NM_002773.3.
UniGeneHs.75799.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DFJX-ray1.45A45-289[»]
3DFLX-ray2.00A45-289[»]
3E0NX-ray1.70B45-305[»]
3E0PX-ray1.70B45-305[»]
3E16X-ray1.60B45-305[»]
3E1XX-ray1.70B45-305[»]
3FVFX-ray1.60B45-305[»]
3GYLX-ray1.30B45-305[»]
3GYMX-ray2.80A/B45-305[»]
ProteinModelPortalQ16651.
SMRQ16651. Positions 45-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ16651. 1 interaction.
MINTMINT-5000236.
STRING9606.ENSP00000319730.

Chemistry

BindingDBQ16651.
ChEMBLCHEMBL5610.

Protein family/group databases

MEROPSS01.159.

Polymorphism databases

DMDM2833277.

Proteomic databases

MaxQBQ16651.
PaxDbQ16651.
PRIDEQ16651.

Protocols and materials databases

DNASU5652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317508; ENSP00000319730; ENSG00000052344.
GeneID5652.
KEGGhsa:5652.
UCSCuc002ebc.4. human.

Organism-specific databases

CTD5652.
GeneCardsGC16M031142.
HGNCHGNC:9491. PRSS8.
HPAHPA030436.
MIM600823. gene.
neXtProtNX_Q16651.
PharmGKBPA33840.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidQ16651.
KOK08664.
OMAPHFVQED.
OrthoDBEOG75B84T.
PhylomeDBQ16651.
TreeFamTF351676.

Gene expression databases

ArrayExpressQ16651.
BgeeQ16651.
CleanExHS_PRSS8.
GenevestigatorQ16651.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRSS8. human.
EvolutionaryTraceQ16651.
GeneWikiPRSS8.
GenomeRNAi5652.
NextBio21962.
PROQ16651.
SOURCESearch...

Entry information

Entry namePRSS8_HUMAN
AccessionPrimary (citable) accession number: Q16651
Secondary accession number(s): Q9UCA3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM