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Q16651

- PRSS8_HUMAN

UniProt

Q16651 - PRSS8_HUMAN

Protein

Prostasin

Gene

PRSS8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei85 – 851Charge relay system
    Active sitei134 – 1341Charge relay system
    Active sitei238 – 2381Charge relay system

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase activity Source: InterPro
    3. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. positive regulation of sodium ion transport Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.159.

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Gene namesi
    Name:PRSS8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9491. PRSS8.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33840.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Propeptidei30 – 323Activation peptidePRO_0000028027
    Chaini33 – 343311ProstasinPRO_0000240511Add
    BLAST
    Chaini33 – 4412Prostasin light chainPRO_0000028028Add
    BLAST
    Chaini45 – 322278Prostasin heavy chainPRO_0000028029Add
    BLAST
    Propeptidei323 – 34321PRO_0000028030Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi37 ↔ 154Interchain (between light and heavy chains)PROSITE-ProRule annotation
    Disulfide bondi70 ↔ 861 PublicationPROSITE-ProRule annotation
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi168 ↔ 2441 PublicationPROSITE-ProRule annotation
    Disulfide bondi201 ↔ 2231 PublicationPROSITE-ProRule annotation
    Disulfide bondi234 ↔ 2621 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ16651.
    PaxDbiQ16651.
    PRIDEiQ16651.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiQ16651.
    BgeeiQ16651.
    CleanExiHS_PRSS8.
    GenevestigatoriQ16651.

    Organism-specific databases

    HPAiHPA030436.

    Interactioni

    Subunit structurei

    Heterodimer of two chains, light and heavy, held by a disulfide bond.1 Publication

    Protein-protein interaction databases

    IntActiQ16651. 1 interaction.
    MINTiMINT-5000236.
    STRINGi9606.ENSP00000319730.

    Structurei

    Secondary structure

    1
    343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi59 – 646
    Beta strandi67 – 748
    Beta strandi76 – 827
    Helixi84 – 863
    Helixi93 – 953
    Beta strandi96 – 1016
    Beta strandi113 – 1153
    Beta strandi117 – 1226
    Helixi124 – 1285
    Beta strandi130 – 1323
    Beta strandi136 – 1427
    Beta strandi148 – 1503
    Beta strandi167 – 1748
    Beta strandi189 – 1968
    Helixi198 – 2058
    Turni206 – 2083
    Turni218 – 2203
    Beta strandi221 – 2255
    Beta strandi227 – 2304
    Turni235 – 2395
    Beta strandi241 – 2466
    Beta strandi249 – 2568
    Beta strandi260 – 2634
    Beta strandi269 – 2735
    Helixi274 – 2774
    Helixi278 – 28811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ16651.
    SMRiQ16651. Positions 45-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16651.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei320 – 34021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 286242Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ16651.
    KOiK08664.
    OMAiPHFVQED.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ16651.
    TreeFamiTF351676.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [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.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16651-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAQKGVLGPG QLGAVAILLY LGLLRSGTGA EGAEAPCGVA PQARITGGSS    50
    AVAGQWPWQV SITYEGVHVC GGSLVSEQWV LSAAHCFPSE HHKEAYEVKL 100
    GAHQLDSYSE DAKVSTLKDI IPHPSYLQEG SQGDIALLQL SRPITFSRYI 150
    RPICLPAANA SFPNGLHCTV TGWGHVAPSV SLLTPKPLQQ LEVPLISRET 200
    CNCLYNIDAK PEEPHFVQED MVCAGYVEGG KDACQGDSGG PLSCPVEGLW 250
    YLTGIVSWGD ACGARNRPGV YTLASSYASW IQSKVTELQP RVVPQTQESQ 300
    PDSNLCGSHL AFSSAPAQGL LRPILFLPLG LALGLLSPWL SEH 343
    Length:343
    Mass (Da):36,431
    Last modified:November 1, 1996 - v1
    Checksum:i98DD6447F5A8C1B2
    GO
    Isoform 2 (identifier: Q16651-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-113: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:289
    Mass (Da):30,519
    Checksum:i4A85CFA9DE10BCDD
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei60 – 11354Missing in isoform 2. 1 PublicationVSP_056632Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41351 mRNA. Translation: AAC41759.1.
    U33446 Genomic DNA. Translation: AAB19071.1.
    AK301619 mRNA. Translation: BAG63104.1.
    AC009088 Genomic DNA. No translation available.
    BC001462 mRNA. Translation: AAH01462.1.
    CCDSiCCDS45469.1.
    PIRiA57014.
    RefSeqiNP_002764.1. NM_002773.3.
    UniGeneiHs.75799.

    Genome annotation databases

    EnsembliENST00000568261; ENSP00000457750; ENSG00000052344.
    GeneIDi5652.
    KEGGihsa:5652.
    UCSCiuc002ebc.4. human.

    Polymorphism databases

    DMDMi2833277.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41351 mRNA. Translation: AAC41759.1 .
    U33446 Genomic DNA. Translation: AAB19071.1 .
    AK301619 mRNA. Translation: BAG63104.1 .
    AC009088 Genomic DNA. No translation available.
    BC001462 mRNA. Translation: AAH01462.1 .
    CCDSi CCDS45469.1.
    PIRi A57014.
    RefSeqi NP_002764.1. NM_002773.3.
    UniGenei Hs.75799.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DFJ X-ray 1.45 A 45-289 [» ]
    3DFL X-ray 2.00 A 45-289 [» ]
    3E0N X-ray 1.70 B 45-305 [» ]
    3E0P X-ray 1.70 B 45-305 [» ]
    3E16 X-ray 1.60 B 45-305 [» ]
    3E1X X-ray 1.70 B 45-305 [» ]
    3FVF X-ray 1.60 B 45-305 [» ]
    3GYL X-ray 1.30 B 45-305 [» ]
    3GYM X-ray 2.80 A/B 45-305 [» ]
    ProteinModelPortali Q16651.
    SMRi Q16651. Positions 45-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q16651. 1 interaction.
    MINTi MINT-5000236.
    STRINGi 9606.ENSP00000319730.

    Chemistry

    BindingDBi Q16651.
    ChEMBLi CHEMBL5610.

    Protein family/group databases

    MEROPSi S01.159.

    Polymorphism databases

    DMDMi 2833277.

    Proteomic databases

    MaxQBi Q16651.
    PaxDbi Q16651.
    PRIDEi Q16651.

    Protocols and materials databases

    DNASUi 5652.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000568261 ; ENSP00000457750 ; ENSG00000052344 .
    GeneIDi 5652.
    KEGGi hsa:5652.
    UCSCi uc002ebc.4. human.

    Organism-specific databases

    CTDi 5652.
    GeneCardsi GC16M031142.
    HGNCi HGNC:9491. PRSS8.
    HPAi HPA030436.
    MIMi 600823. gene.
    neXtProti NX_Q16651.
    PharmGKBi PA33840.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi Q16651.
    KOi K08664.
    OMAi PHFVQED.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q16651.
    TreeFami TF351676.

    Miscellaneous databases

    ChiTaRSi PRSS8. human.
    EvolutionaryTracei Q16651.
    GeneWikii PRSS8.
    GenomeRNAii 5652.
    NextBioi 21962.
    PROi Q16651.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16651.
    Bgeei Q16651.
    CleanExi HS_PRSS8.
    Genevestigatori Q16651.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Prostate.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Placenta.
    5. "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.
    6. "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.
    7. "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.
    8. "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.

    Entry informationi

    Entry nameiPRSS8_HUMAN
    AccessioniPrimary (citable) accession number: Q16651
    Secondary accession number(s): B4DWP2, Q9UCA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3