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Q9NQ38

- ISK5_HUMAN

UniProt

Q9NQ38 - ISK5_HUMAN

Protein

Serine protease inhibitor Kazal-type 5

Gene

SPINK5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Serine protease inhibitor, probably important for the anti-inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense-activating and desquamation-involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei46 – 472Reactive bondPROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. anagen Source: UniProtKB
    2. epidermal cell differentiation Source: UniProtKB
    3. epithelial cell differentiation Source: UniProtKB
    4. extracellular matrix organization Source: UniProtKB
    5. hair cell differentiation Source: UniProtKB
    6. negative regulation of angiogenesis Source: UniProtKB
    7. negative regulation of endopeptidase activity Source: GOC
    8. negative regulation of immune response Source: UniProtKB
    9. negative regulation of proteolysis Source: Ensembl
    10. regulation of cell adhesion Source: Ensembl
    11. regulation of T cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Enzyme and pathway databases

    SABIO-RKQ9NQ38.

    Protein family/group databases

    MEROPSiI01.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine protease inhibitor Kazal-type 5
    Alternative name(s):
    Lympho-epithelial Kazal-type-related inhibitor
    Short name:
    LEKTI
    Cleaved into the following 2 chains:
    Gene namesi
    Name:SPINK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:15464. SPINK5.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. endoplasmic reticulum Source: UniProtKB
    5. endoplasmic reticulum membrane Source: UniProtKB
    6. epidermal lamellar body Source: UniProtKB
    7. extracellular region Source: UniProtKB
    8. extracellular vesicular exosome Source: UniProt
    9. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Netherton syndrome (NETH) [MIM:256500]: An autosomal recessive congenital ichthyosis associated with hair shaft abnormalities and anomalies of the immune system. Typical features are ichthyosis linearis circumflexa, ichthyosiform erythroderma, trichorrhexis invaginata (bamboo hair), atopic dermatitis, and hayfever. High postnatal mortality is due to failure to thrive, infections and hypernatremic dehydration.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Hypotrichosis, Ichthyosis

    Organism-specific databases

    MIMi256500. phenotype.
    Orphaneti634. Netherton syndrome.
    PharmGKBiPA37962.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 10641042Serine protease inhibitor Kazal-type 5PRO_0000016572Add
    BLAST
    Peptidei23 – 7755Hemofiltrate peptide HF6478PRO_0000016573Add
    BLAST
    Peptidei356 – 42368Hemofiltrate peptide HF7665PRO_0000016574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 66
    Disulfide bondi44 ↔ 63
    Disulfide bondi97 ↔ 133PROSITE-ProRule annotation
    Disulfide bondi111 ↔ 130PROSITE-ProRule annotation
    Disulfide bondi119 ↔ 151PROSITE-ProRule annotation
    Disulfide bondi161 ↔ 197PROSITE-ProRule annotation
    Disulfide bondi175 ↔ 194PROSITE-ProRule annotation
    Disulfide bondi225 ↔ 261PROSITE-ProRule annotation
    Disulfide bondi239 ↔ 258PROSITE-ProRule annotation
    Disulfide bondi297 ↔ 333PROSITE-ProRule annotation
    Disulfide bondi311 ↔ 330PROSITE-ProRule annotation
    Disulfide bondi367 ↔ 403
    Disulfide bondi381 ↔ 400
    Disulfide bondi437 ↔ 473PROSITE-ProRule annotation
    Disulfide bondi451 ↔ 470PROSITE-ProRule annotation
    Disulfide bondi496 ↔ 532PROSITE-ProRule annotation
    Disulfide bondi510 ↔ 529PROSITE-ProRule annotation
    Disulfide bondi567 ↔ 603PROSITE-ProRule annotation
    Disulfide bondi581 ↔ 600PROSITE-ProRule annotation
    Disulfide bondi632 ↔ 668PROSITE-ProRule annotation
    Disulfide bondi646 ↔ 665PROSITE-ProRule annotation
    Disulfide bondi707 ↔ 743PROSITE-ProRule annotation
    Disulfide bondi721 ↔ 740PROSITE-ProRule annotation
    Disulfide bondi774 ↔ 810PROSITE-ProRule annotation
    Disulfide bondi788 ↔ 807PROSITE-ProRule annotation
    Disulfide bondi849 ↔ 885PROSITE-ProRule annotation
    Disulfide bondi863 ↔ 882PROSITE-ProRule annotation
    Disulfide bondi916 ↔ 952PROSITE-ProRule annotation
    Disulfide bondi930 ↔ 949PROSITE-ProRule annotation
    Disulfide bondi993 ↔ 1028
    Disulfide bondi1006 ↔ 1025
    Disulfide bondi1014 ↔ 1046

    Post-translational modificationi

    Proteolytically processed by furin in individual domains (D1, D5, D6, D8 through D11, and D9 through D15) exhibiting various inhibitory potentials for multiple proteases.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiQ9NQ38.
    PRIDEiQ9NQ38.

    PTM databases

    PhosphoSiteiQ9NQ38.

    Miscellaneous databases

    PMAP-CutDBQ9NQ38.

    Expressioni

    Tissue specificityi

    Highly expressed in the thymus and stratum corneum. Also found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate.1 Publication

    Gene expression databases

    ArrayExpressiQ9NQ38.
    BgeeiQ9NQ38.
    CleanExiHS_SPINK5.
    GenevestigatoriQ9NQ38.

    Organism-specific databases

    HPAiCAB015347.
    HPA009067.
    HPA011351.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000352936.

    Structurei

    Secondary structure

    1
    1064
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni25 – 273
    Helixi33 – 364
    Beta strandi37 – 404
    Helixi48 – 525
    Helixi54 – 7623
    Helixi363 – 3664
    Helixi367 – 3704
    Turni371 – 3733
    Beta strandi375 – 3773
    Helixi399 – 41315
    Helixi990 – 9934
    Turni1000 – 10023
    Beta strandi1013 – 10153
    Turni1016 – 10183
    Beta strandi1019 – 10246
    Helixi1025 – 103410
    Beta strandi1040 – 10456
    Helixi1047 – 10493
    Helixi1055 – 10584

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H0ZNMR-A356-423[»]
    1HDLNMR-A23-77[»]
    1UUCNMR-A23-77[»]
    1UVFNMR-A989-1047[»]
    1UVGNMR-A989-1064[»]
    ProteinModelPortaliQ9NQ38.
    SMRiQ9NQ38. Positions 23-77, 105-154, 159-201, 223-266, 295-353, 356-423, 426-478, 487-537, 556-608, 624-673, 707-744, 768-811, 841-889, 916-956, 989-1064.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQ38.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6639Kazal-like 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini91 – 15363Kazal-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini155 – 21662Kazal-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini219 – 28567Kazal-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini291 – 35262Kazal-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini361 – 42363Kazal-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini431 – 48959Kazal-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini490 – 55162Kazal-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 62262Kazal-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini626 – 68863Kazal-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini701 – 75757Kazal-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini768 – 83063Kazal-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini843 – 90563Kazal-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini910 – 97162Kazal-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini987 – 104862Kazal-like 15PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Contains at least one active inhibitory domain for trypsin (domain 6).

    Sequence similaritiesi

    Contains 15 Kazal-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG253835.
    HOVERGENiHBG006183.
    OMAiCHENLIR.
    OrthoDBiEOG7BW0M2.
    PhylomeDBiQ9NQ38.
    TreeFamiTF336724.

    Family and domain databases

    InterProiIPR002350. Kazal_dom.
    [Graphical view]
    PfamiPF00050. Kazal_1. 1 hit.
    PF07648. Kazal_2. 13 hits.
    [Graphical view]
    SMARTiSM00280. KAZAL. 14 hits.
    [Graphical view]
    PROSITEiPS00282. KAZAL_1. 2 hits.
    PS51465. KAZAL_2. 14 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform f-l (identifier: Q9NQ38-1) [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

    MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF     50
    FQSLDGIMFI NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF 100
    KKGERDGDFI CPDYYEAVCG TDGKTYDNRC ALCAENAKTG SQIGVKSEGE 150
    CKSSNPEQDV CSAFRPFVRD GRLGCTREND PVLGPDGKTH GNKCAMCAEL 200
    FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT RESDPVRGPD 250
    GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY 300
    QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR 350
    ARNKRESGKA TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC 400
    SMCEVFFQAE EEEKKKKEGK SRNKRQSKST ASFEELCSEY RKSRKNGRLF 450
    CTRENDPIQG PDGKMHGNTC SMCEAFFQQE ERARAKAKRE AAKEICSEFR 500
    DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE EEKKNDKEEK 550
    GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC 600
    SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN 650
    DPVRGPDGKT HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG 700
    GNTQDECAEY REQMKNGRLS CTRESDPVRD ADGKSYNNQC TMCKAKLERE 750
    AERKNEYSRS RSNGTGSESG KDTCDEFRSQ MKNGKLICTR ESDPVRGPDG 800
    KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE RSNDKEDLCR 850
    EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD 900
    EEKSSSKPSN NAKDECSEFR NYIRNNELIC PRENDPVHGA DGKFYTNKCY 950
    MCRAVFLTEA LERAKLQEKP SHVRASQEED SPDSFSSLDS EMCKDYRVLP 1000
    RIGYLCPKDL KPVCGDDGQT YNNPCMLCHE NLIRQTNTHI RSTGKCEESS 1050
    TPGTTAASMP PSDE 1064
    Length:1,064
    Mass (Da):120,714
    Last modified:November 4, 2008 - v2
    Checksum:i6CBEF39BB9E6D75D
    GO
    Isoform short (identifier: Q9NQ38-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         914-916: DEC → VIY
         917-1064: Missing.

    Show »
    Length:916
    Mass (Da):104,017
    Checksum:i82A029D102BD8C26
    GO
    Isoform long (identifier: Q9NQ38-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         914-914: D → DQCRQVQNEAEDAKFRQPGRSLASVARMSTD

    Show »
    Length:1,094
    Mass (Da):124,076
    Checksum:i8EF0D8DE3A62227A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 279DAASKNEDQ → GQCEKDSLS in CAB96877. (PubMed:10835624)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti267 – 2671Q → R.3 Publications
    Corresponds to variant rs6892205 [ dbSNP | Ensembl ].
    VAR_047115
    Natural varianti335 – 3351A → V.2 Publications
    Corresponds to variant rs34482796 [ dbSNP | Ensembl ].
    VAR_061337
    Natural varianti368 – 3681S → N.3 Publications
    Corresponds to variant rs2303063 [ dbSNP | Ensembl ].
    VAR_047116
    Natural varianti386 – 3861D → N.
    Corresponds to variant rs2303064 [ dbSNP | Ensembl ].
    VAR_047117
    Natural varianti395 – 3951V → M.
    Corresponds to variant rs17775319 [ dbSNP | Ensembl ].
    VAR_047118
    Natural varianti420 – 4201K → E.3 Publications
    Corresponds to variant rs2303067 [ dbSNP | Ensembl ].
    VAR_015537
    Natural varianti441 – 4411R → H.
    Corresponds to variant rs34393923 [ dbSNP | Ensembl ].
    VAR_047119
    Natural varianti588 – 5881I → M.
    Corresponds to variant rs35877540 [ dbSNP | Ensembl ].
    VAR_047120
    Natural varianti711 – 7111R → Q.2 Publications
    Corresponds to variant rs3777134 [ dbSNP | Ensembl ].
    VAR_047121
    Natural varianti825 – 8251E → D.
    Corresponds to variant rs2303070 [ dbSNP | Ensembl ].
    VAR_047122
    Natural varianti887 – 8871S → R.
    Corresponds to variant rs28408445 [ dbSNP | Ensembl ].
    VAR_047123
    Natural varianti969 – 9691K → E.
    Corresponds to variant rs3188691 [ dbSNP | Ensembl ].
    VAR_047124
    Natural varianti972 – 9721H → R.
    Corresponds to variant rs17705005 [ dbSNP | Ensembl ].
    VAR_047125

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei914 – 9163DEC → VIY in isoform short. 1 PublicationVSP_040019
    Alternative sequencei914 – 9141D → DQCRQVQNEAEDAKFRQPGR SLASVARMSTD in isoform long. 1 PublicationVSP_040020
    Alternative sequencei917 – 1064148Missing in isoform short. 1 PublicationVSP_040021Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ228139 mRNA. Translation: CAB40839.1.
    AJ391230
    , AJ270944, AJ391231, AJ391232, AJ391233, AJ391234, AJ391235, AJ276579, AJ391236, AJ276580, AJ391237, AJ391238, AJ391239, AJ391240, AJ391241, AJ276578, AJ391242, AJ391243, AJ391244, AJ391245, AJ391246, AJ391247, AJ391248, AJ391249, AJ391250, AJ391251, AJ391252, AJ391253, AJ391254, AJ276577 Genomic DNA. Translation: CAB96877.1.
    DQ149927 mRNA. Translation: ABA06534.1.
    DQ149928 mRNA. Translation: ABA06535.1.
    DQ149929 mRNA. Translation: ABA06536.1.
    AC008722 Genomic DNA. No translation available.
    AC116334 Genomic DNA. No translation available.
    AF295784 Genomic DNA. Translation: AAK97139.1.
    AF295783 Genomic DNA. Translation: AAK97140.1.
    CCDSiCCDS43382.1. [Q9NQ38-1]
    CCDS47300.1. [Q9NQ38-3]
    CCDS47301.1. [Q9NQ38-2]
    RefSeqiNP_001121170.1. NM_001127698.1. [Q9NQ38-3]
    NP_001121171.1. NM_001127699.1. [Q9NQ38-2]
    NP_006837.2. NM_006846.3. [Q9NQ38-1]
    UniGeneiHs.331555.

    Genome annotation databases

    EnsembliENST00000256084; ENSP00000256084; ENSG00000133710. [Q9NQ38-1]
    ENST00000359874; ENSP00000352936; ENSG00000133710. [Q9NQ38-3]
    ENST00000398454; ENSP00000381472; ENSG00000133710. [Q9NQ38-2]
    GeneIDi11005.
    KEGGihsa:11005.
    UCSCiuc003low.2. human. [Q9NQ38-2]
    uc003lox.2. human. [Q9NQ38-1]
    uc003loy.2. human. [Q9NQ38-3]

    Polymorphism databases

    DMDMi212276440.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SPINK5base

    SPINK5 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ228139 mRNA. Translation: CAB40839.1 .
    AJ391230
    , AJ270944 , AJ391231 , AJ391232 , AJ391233 , AJ391234 , AJ391235 , AJ276579 , AJ391236 , AJ276580 , AJ391237 , AJ391238 , AJ391239 , AJ391240 , AJ391241 , AJ276578 , AJ391242 , AJ391243 , AJ391244 , AJ391245 , AJ391246 , AJ391247 , AJ391248 , AJ391249 , AJ391250 , AJ391251 , AJ391252 , AJ391253 , AJ391254 , AJ276577 Genomic DNA. Translation: CAB96877.1 .
    DQ149927 mRNA. Translation: ABA06534.1 .
    DQ149928 mRNA. Translation: ABA06535.1 .
    DQ149929 mRNA. Translation: ABA06536.1 .
    AC008722 Genomic DNA. No translation available.
    AC116334 Genomic DNA. No translation available.
    AF295784 Genomic DNA. Translation: AAK97139.1 .
    AF295783 Genomic DNA. Translation: AAK97140.1 .
    CCDSi CCDS43382.1. [Q9NQ38-1 ]
    CCDS47300.1. [Q9NQ38-3 ]
    CCDS47301.1. [Q9NQ38-2 ]
    RefSeqi NP_001121170.1. NM_001127698.1. [Q9NQ38-3 ]
    NP_001121171.1. NM_001127699.1. [Q9NQ38-2 ]
    NP_006837.2. NM_006846.3. [Q9NQ38-1 ]
    UniGenei Hs.331555.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H0Z NMR - A 356-423 [» ]
    1HDL NMR - A 23-77 [» ]
    1UUC NMR - A 23-77 [» ]
    1UVF NMR - A 989-1047 [» ]
    1UVG NMR - A 989-1064 [» ]
    ProteinModelPortali Q9NQ38.
    SMRi Q9NQ38. Positions 23-77, 105-154, 159-201, 223-266, 295-353, 356-423, 426-478, 487-537, 556-608, 624-673, 707-744, 768-811, 841-889, 916-956, 989-1064.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000352936.

    Protein family/group databases

    MEROPSi I01.950.

    PTM databases

    PhosphoSitei Q9NQ38.

    Polymorphism databases

    DMDMi 212276440.

    Proteomic databases

    PaxDbi Q9NQ38.
    PRIDEi Q9NQ38.

    Protocols and materials databases

    DNASUi 11005.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256084 ; ENSP00000256084 ; ENSG00000133710 . [Q9NQ38-1 ]
    ENST00000359874 ; ENSP00000352936 ; ENSG00000133710 . [Q9NQ38-3 ]
    ENST00000398454 ; ENSP00000381472 ; ENSG00000133710 . [Q9NQ38-2 ]
    GeneIDi 11005.
    KEGGi hsa:11005.
    UCSCi uc003low.2. human. [Q9NQ38-2 ]
    uc003lox.2. human. [Q9NQ38-1 ]
    uc003loy.2. human. [Q9NQ38-3 ]

    Organism-specific databases

    CTDi 11005.
    GeneCardsi GC05P147423.
    H-InvDB HIX0005288.
    HGNCi HGNC:15464. SPINK5.
    HPAi CAB015347.
    HPA009067.
    HPA011351.
    MIMi 256500. phenotype.
    605010. gene.
    neXtProti NX_Q9NQ38.
    Orphaneti 634. Netherton syndrome.
    PharmGKBi PA37962.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253835.
    HOVERGENi HBG006183.
    OMAi CHENLIR.
    OrthoDBi EOG7BW0M2.
    PhylomeDBi Q9NQ38.
    TreeFami TF336724.

    Enzyme and pathway databases

    SABIO-RK Q9NQ38.

    Miscellaneous databases

    EvolutionaryTracei Q9NQ38.
    GeneWikii LEKTI.
    GenomeRNAii 11005.
    NextBioi 41803.
    PMAP-CutDB Q9NQ38.
    PROi Q9NQ38.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQ38.
    Bgeei Q9NQ38.
    CleanExi HS_SPINK5.
    Genevestigatori Q9NQ38.

    Family and domain databases

    InterProi IPR002350. Kazal_dom.
    [Graphical view ]
    Pfami PF00050. Kazal_1. 1 hit.
    PF07648. Kazal_2. 13 hits.
    [Graphical view ]
    SMARTi SM00280. KAZAL. 14 hits.
    [Graphical view ]
    PROSITEi PS00282. KAZAL_1. 2 hits.
    PS51465. KAZAL_2. 14 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS F-L), PARTIAL PROTEIN SEQUENCE, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Epithelium.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NETHERTON SYNDROME, VARIANTS ARG-267 AND ASN-368.
    3. "SPINK5, the defective gene in netherton syndrome, encodes multiple LEKTI isoforms derived from alternative pre-mRNA processing."
      Tartaglia-Polcini A., Bonnart C., Micheloni A., Cianfarani F., Andre A., Zambruno G., Hovnanian A., D'Alessio M.
      J. Invest. Dermatol. 126:315-324(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT; F-L AND LONG), ALTERNATIVE SPLICING, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711.
      Tissue: Keratinocyte.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The spectrum of pathogenic mutations in SPINK5 in 19 families with Netherton syndrome: implications for mutation detection and first case of prenatal diagnosis."
      Sprecher E., Chavanas S., DiGiovanna J.J., Amin S., Nielsen K., Prendiville J.S., Silverman R., Esterly N.B., Spraker M.K., Guelig E., de Luna M.L., Williams M.L., Buehler B., Siegfried E.C., Van Maldergem L., Pfendner E., Bale S.J., Uitto J., Hovnanian A., Richard G.
      J. Invest. Dermatol. 117:179-187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-222 AND 266-294.
    6. "Purification and partial amino acid sequence of proteins from human epidermal keratinocyte conditioned medium."
      Ahmed A., Kandola P., Ziada G., Parenteau N.
      J. Protein Chem. 20:273-278(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 490-507.
      Tissue: Foreskin keratinocyte.
    7. "LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction."
      Deraison C., Bonnart C., Lopez F., Besson C., Robinson R., Jayakumar A., Wagberg F., Brattsand M., Hachem J.P., Leonardsson G., Hovnanian A.
      Mol. Biol. Cell 18:3607-3619(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CLEAVAGE BY FURIN, INHIBITION OF KLK5; KLK7 AND KLK14.
    8. "New role for LEKTI in skin barrier formation: label-free quantitative proteomic identification of caspase 14 as a novel target for the protease inhibitor LEKTI."
      Bennett K., Callard R., Heywood W., Harper J., Jayakumar A., Clayman G.L., Di W.L., Mills K.
      J. Proteome Res. 9:4289-4294(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INHIBITION OF CASP14.
    9. "Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI."
      Lauber T., Schulz A., Schweimer K., Adermann K., Marx U.C.
      J. Mol. Biol. 328:205-219(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 23-77 AND 356-423.
    10. "The solution structure of a chimeric LEKTI domain reveals a chameleon sequence."
      Tidow H., Lauber T., Vitzithum K., Sommerhoff C.P., Rosch P., Marx U.C.
      Biochemistry 43:11238-11247(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 989-1064.
    11. Cited for: VARIANT GLU-420.

    Entry informationi

    Entry nameiISK5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQ38
    Secondary accession number(s): A8MYE8
    , B7WPB7, D6REN5, O75770, Q3LX95, Q3LX96, Q3LX97, Q96PP2, Q96PP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 142 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3