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Protein

Kallikrein-8

Gene

Klk8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury.8 Publications

Catalytic activityi

Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.

Enzyme regulationi

Strongly inhibited by diisopropyl fluorophosphate, leupeptin and (4-amidinophenyl)methanesulfonyl 1-fluoride.1 Publication

Kineticsi

  1. KM=300 µM for Boc-Val-Pro-Arg-MCA1 Publication
  2. KM=540 µM for Boc-Phe-Ser-Arg-MCA1 Publication
  3. KM=280 µM for D-Val-Leu-Arg-MCA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731Charge relay systemBy similarity
    Active sitei120 – 1201Charge relay systemBy similarity
    Active sitei212 – 2121Charge relay systemBy similarity

    GO - Molecular functioni

    • serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • cell death Source: UniProtKB
    • keratinocyte proliferation Source: UniProtKB
    • memory Source: UniProtKB
    • negative regulation of axon regeneration Source: UniProtKB
    • negative regulation of myelination Source: UniProtKB
    • neuron projection morphogenesis Source: UniProtKB
    • regulation of synapse organization Source: UniProtKB
    • response to wounding Source: UniProtKB
    • synapse organization Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.118. 3474.

    Protein family/group databases

    MEROPSiS01.244.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kallikrein-8 (EC:3.4.21.118)
    Short name:
    mK8
    Alternative name(s):
    Neuropsin
    Short name:
    NP
    Serine protease 19
    Gene namesi
    Name:Klk8
    Synonyms:Nrpn, Prss19
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 7

    Organism-specific databases

    MGIiMGI:1343327. Klk8.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • extracellular space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mice display marked abnormalities of synapses and neurons in the CA1 subfield of the hippocampus with enlarged and elongated pyramidal cell soma and reduced asymmetrical synapse numbers. Mutants also display impaired spatial memory acquisition, increased hippocampal susceptibility to hyperexcitability in response to repetitive afferent stimulation and prolonged recovery of UV-irradiated skin. Following spinal cord injury, mutants display reduced demyelination, oligodendrocyte death and axonal degeneration, and inproved hind limb recovery, suggesting that attenuation of neuropsin activity may be beneficial in the treatment of spinal cord injury. Blocking of Klk8 activity by intraventricular injection with monoclonal antibodies reduces or eliminates epileptic seizures in kindled mice.7 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 3241 PublicationPRO_0000027948
    Chaini33 – 260228Kallikrein-8PRO_0000027949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 173
    Disulfide bondi58 ↔ 74
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi145 ↔ 246
    Disulfide bondi152 ↔ 218
    Disulfide bondi184 ↔ 198
    Disulfide bondi208 ↔ 233

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ61955.
    PRIDEiQ61955.

    PTM databases

    PhosphoSiteiQ61955.

    Expressioni

    Tissue specificityi

    Expressed in the limbic system of mouse brain and is localized at highest concentration in pyramidal neurons of the hippocampal CA1-3 subfields. Also detected in spinal cord gray matter and in keratinized stratified epithelia of epidermis, hair, tongue, palate, nasal cavity, pharynges, esophagus and forestomach. In skin and mucus membranes, expressed in stratum spinosum and stratum granulosum. Expressed during estrus in vaginal epithelial cells but not stromal cells. Within the vaginal epithelium, expressed in prickle cells, granular cells and parakeratotic cells but not in basal cells. Not expressed in uterus. Expressed in the keratinocytes.7 Publications

    Developmental stagei

    Expression is detected in the brain from embryonic day 12 and continues into adulthood.1 Publication

    Inductioni

    By chemical/incision-induced brain injury which leads to increased expression in axon fiber bundles of the peri-lesioned region, by electrically-induced seizure (kindling) in brain, by UV irradiation in skin and by incisional and chemically-induced skin wounding which causes epidermal proliferation and hyperkeratosis. Induced by chemically-induced oxidative stress which leads to increased expression in the hippocampal pyramidal neurons 2 hours after treatment. Levels then decrease, drop to 60% of pretreated control levels at day 7 when avoidance learning is impaired and return to control levels at day 30. Also induced by spinal crush injury which leads to increased expression in spinal cord white matter adjacent to the lesion. Expression increases between days 1-14 post-injury with a peak at day 4.8 Publications

    Gene expression databases

    BgeeiQ61955.
    CleanExiMM_KLK8.
    GenevisibleiQ61955. MM.

    Interactioni

    Subunit structurei

    Interacts with SPINK9.By similarity

    Protein-protein interaction databases

    BioGridi234416. 1 interaction.
    STRINGi10090.ENSMUSP00000082588.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi47 – 526Combined sources
    Beta strandi55 – 6410Combined sources
    Beta strandi67 – 704Combined sources
    Helixi72 – 743Combined sources
    Beta strandi80 – 845Combined sources
    Beta strandi96 – 983Combined sources
    Beta strandi100 – 1056Combined sources
    Beta strandi122 – 1287Combined sources
    Beta strandi133 – 1364Combined sources
    Beta strandi151 – 1588Combined sources
    Beta strandi160 – 1645Combined sources
    Beta strandi172 – 1787Combined sources
    Helixi181 – 1877Combined sources
    Turni189 – 1913Combined sources
    Beta strandi196 – 2005Combined sources
    Beta strandi215 – 2184Combined sources
    Beta strandi221 – 2288Combined sources
    Beta strandi231 – 2333Combined sources
    Beta strandi240 – 2445Combined sources
    Helixi245 – 25612Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NPMX-ray2.10A/B33-257[»]
    ProteinModelPortaliQ61955.
    SMRiQ61955. Positions 33-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61955.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 257225Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118862.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ61955.
    KOiK08650.
    OMAiCKKPKYT.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ61955.
    TreeFamiTF331065.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q61955-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGRPPPCAIQ PWILLLLFMG AWAGLTRAQG SKILEGRECI PHSQPWQAAL
    60 70 80 90 100
    FQGERLICGG VLVGDRWVLT AAHCKKQKYS VRLGDHSLQS RDQPEQEIQV
    110 120 130 140 150
    AQSIQHPCYN NSNPEDHSHD IMLIRLQNSA NLGDKVKPVQ LANLCPKVGQ
    160 170 180 190 200
    KCIISGWGTV TSPQENFPNT LNCAEVKIYS QNKCERAYPG KITEGMVCAG
    210 220 230 240 250
    SSNGADTCQG DSGGPLVCDG MLQGITSWGS DPCGKPEKPG VYTKICRYTT
    260
    WIKKTMDNRD
    Length:260
    Mass (Da):28,524
    Last modified:November 1, 1996 - v1
    Checksum:iBE5F6F6BE37CD60E
    GO

    Mass spectrometryi

    Molecular mass is 26613 Da from positions 29 - 260. Determined by MALDI. 1 Publication
    Molecular mass is 26229 Da from positions 33 - 260. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D30785 mRNA. Translation: BAA06451.1.
    AB032202 Genomic DNA. Translation: BAA92435.1.
    BC055895 mRNA. Translation: AAH55895.1.
    AB074296 mRNA. Translation: BAB92021.1.
    CCDSiCCDS21182.1.
    PIRiI56559.
    RefSeqiNP_032966.1. NM_008940.2.
    XP_006540971.1. XM_006540908.1.
    UniGeneiMm.458023.

    Genome annotation databases

    EnsembliENSMUST00000085461; ENSMUSP00000082588; ENSMUSG00000064023.
    GeneIDi259277.
    KEGGimmu:259277.
    UCSCiuc009gns.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D30785 mRNA. Translation: BAA06451.1.
    AB032202 Genomic DNA. Translation: BAA92435.1.
    BC055895 mRNA. Translation: AAH55895.1.
    AB074296 mRNA. Translation: BAB92021.1.
    CCDSiCCDS21182.1.
    PIRiI56559.
    RefSeqiNP_032966.1. NM_008940.2.
    XP_006540971.1. XM_006540908.1.
    UniGeneiMm.458023.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NPMX-ray2.10A/B33-257[»]
    ProteinModelPortaliQ61955.
    SMRiQ61955. Positions 33-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi234416. 1 interaction.
    STRINGi10090.ENSMUSP00000082588.

    Protein family/group databases

    MEROPSiS01.244.

    PTM databases

    PhosphoSiteiQ61955.

    Proteomic databases

    PaxDbiQ61955.
    PRIDEiQ61955.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000085461; ENSMUSP00000082588; ENSMUSG00000064023.
    GeneIDi259277.
    KEGGimmu:259277.
    UCSCiuc009gns.1. mouse.

    Organism-specific databases

    CTDi11202.
    MGIiMGI:1343327. Klk8.

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118862.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ61955.
    KOiK08650.
    OMAiCKKPKYT.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ61955.
    TreeFamiTF331065.

    Enzyme and pathway databases

    BRENDAi3.4.21.118. 3474.

    Miscellaneous databases

    EvolutionaryTraceiQ61955.
    NextBioi392031.
    PROiQ61955.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ61955.
    CleanExiMM_KLK8.
    GenevisibleiQ61955. MM.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus."
      Chen Z.-L., Yoshida S., Kato K., Momota Y., Suzuki J., Tanaka T., Ito J., Nishino H., Aimoto S., Kiyama H., Shiosaka S.
      J. Neurosci. 15:5088-5097(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Hippocampus.
    2. "Assignment of the neuropsin gene (Prss19) to mouse chromosome band 7B4 by in situ hybridization."
      Yoshida S., Hirata A., Inoue N., Shiosaka S.
      Cytogenet. Cell Genet. 88:97-98(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "Characterization of recombinant and brain neuropsin, a plasticity-related serine protease."
      Shimizu C., Yoshida S., Shibata M., Kato K., Momota Y., Matsumoto K., Shiosaka T., Midorikawa R., Kamachi T., Kawabe A., Shiosaka S.
      J. Biol. Chem. 273:11189-11196(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
      Strain: BALB/c.
      Tissue: Brain.
    5. "Estrogen-independent expression of neuropsin, a serine protease in the vagina of mice exposed neonatally to diethylstilbestrol."
      Katsu Y., Takasu E., Iguchi T.
      Mol. Cell. Endocrinol. 195:99-107(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-260, TISSUE SPECIFICITY.
      Strain: C57BL/6.
    6. "Ontogeny of neuropsin mRNA expression in the mouse brain."
      Suzuki J., Yoshida S., Chen Z.-L., Momota Y., Kato K., Hirata A., Shiosaka S.
      Neurosci. Res. 23:345-351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. Cited for: INDUCTION.
    8. "Effects of oxidative stress on the expression of limbic-specific protease neuropsin and avoidance learning in mice."
      Akita H., Matsuyama T., Iso H., Sugita M., Yoshida S.
      Brain Res. 769:86-96(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy."
      Momota Y., Yoshida S., Ito J., Shibata M., Kato K., Sakurai K., Matsumoto K., Shiosaka S.
      Eur. J. Neurosci. 10:760-764(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    10. "Expression of neuropsin in the keratinizing epithelial tissue - immunohistochemical analysis of wild-type and nude mice."
      Inoue N., Kuwae K., Ishida-Yamamoto A., Iizuka H., Shibata M., Yoshida S., Kato K., Shiosaka S.
      J. Invest. Dermatol. 110:923-931(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Effect of 12-O-tetradecanoyl-phorbol ester and incisional wounding on neuropsin mRNA and its protein expression in murine skin."
      Kitayoshi H., Inoue N., Kuwae K., Chen Z.-L., Sato H., Ohta T., Hosokawa K., Itami S., Yoshikawa K., Yoshida S., Shiosaka S.
      Arch. Dermatol. Res. 291:333-338(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. "Injury induces neuropsin mRNA in the central nervous system."
      Tomizawa K., He X.-P., Yamanaka H., Shiosaka S., Yoshida S.
      Brain Res. 824:308-311(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "Neuropsin regulates an early phase of Schaffer-collateral long-term potentiation in the murine hippocampus."
      Komai S., Matsuyama T., Matsumoto K., Kato K., Kobayashi M., Imamura K., Yoshida S., Ugawa S., Shiosaka S.
      Eur. J. Neurosci. 12:1479-1486(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Loss of hippocampal serine protease BSP1/neuropsin predisposes to global seizure activity."
      Davies B., Kearns I.R., Ure J., Davies C.H., Lathe R.
      J. Neurosci. 21:6993-7000(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    15. Cited for: DISRUPTION PHENOTYPE.
    16. "Expression of neuropsin in oligodendrocytes after injury to the CNS."
      He X.-P., Shiosaka S., Yoshida S.
      Neurosci. Res. 39:455-462(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    17. "Extracellular serine protease neuropsin (KLK8) modulates neurite outgrowth and fasciculation of mouse hippocampal neurons in culture."
      Oka T., Akisada M., Okabe A., Sakurai K., Shiosaka S., Kato K.
      Neurosci. Lett. 321:141-144(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Prolonged recovery of ultraviolet B-irradiated skin in neuropsin (KLK8)-deficient mice."
      Kirihara T., Matsumoto-Miyai K., Nakamura Y., Sadayama T., Yoshida S., Shiosaka S.
      Br. J. Dermatol. 149:700-706(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, DISRUPTION PHENOTYPE.
    19. "NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the hippocampus by neuropsin."
      Matsumoto-Miyai K., Ninomiya A., Yamasaki H., Tamura H., Nakamura Y., Shiosaka S.
      J. Neurosci. 23:7727-7736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons."
      Nakamura Y., Tamura H., Horinouchi K., Shiosaka S.
      J. Cell Sci. 119:1341-1349(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    21. "Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo."
      Tamura H., Ishikawa Y., Hino N., Maeda M., Yoshida S., Kaku S., Shiosaka S.
      J. Physiol. (Lond.) 570:541-551(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    22. "SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes."
      Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.
      J. Biochem. 142:435-442(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    23. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    24. "Neuropsin promotes oligodendrocyte death, demyelination and axonal degeneration after spinal cord injury."
      Terayama R., Bando Y., Murakami K., Kato K., Kishibe M., Yoshida S.
      Neuroscience 148:175-187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
    25. "Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis."
      Kishi T., Kato M., Shimizu T., Kato K., Matsumoto K., Yoshida S., Shiosaka S., Hakoshima T.
      J. Biol. Chem. 274:4220-4224(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-257.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiKLK8_MOUSE
    AccessioniPrimary (citable) accession number: Q61955
    Secondary accession number(s): Q8K5D7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: June 24, 2015
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.