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P03973

- SLPI_HUMAN

UniProt

P03973 - SLPI_HUMAN

Protein

Antileukoproteinase

Gene

SLPI

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

    Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei45 – 462Reactive bond for trypsinCurated
    Sitei97 – 982Reactive bond for chymotrypsin and elastaseCurated

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: ProtInc
    2. enzyme binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: GOC
    2. negative regulation of protein binding Source: UniProtKB
    3. negative regulation of viral genome replication Source: UniProtKB

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI17.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antileukoproteinase
    Short name:
    ALP
    Alternative name(s):
    BLPI
    HUSI-1
    Mucus proteinase inhibitor
    Short name:
    MPI
    Protease inhibitor WAP4
    Secretory leukocyte protease inhibitor
    Seminal proteinase inhibitor
    WAP four-disulfide core domain protein 4
    Gene namesi
    Name:SLPI
    Synonyms:WAP4, WFDC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11092. SLPI.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35944.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25253 PublicationsAdd
    BLAST
    Chaini26 – 132107AntileukoproteinasePRO_0000041355Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 64
    Disulfide bondi43 ↔ 68
    Disulfide bondi51 ↔ 63
    Disulfide bondi57 ↔ 72
    Disulfide bondi89 ↔ 118
    Disulfide bondi96 ↔ 122
    Disulfide bondi105 ↔ 117
    Disulfide bondi111 ↔ 126

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP03973.
    PaxDbiP03973.
    PeptideAtlasiP03973.
    PRIDEiP03973.

    Miscellaneous databases

    PMAP-CutDBP03973.

    Expressioni

    Tissue specificityi

    Mucous fluids.

    Gene expression databases

    ArrayExpressiP03973.
    BgeeiP03973.
    CleanExiHS_SLPI.
    GenevestigatoriP03973.

    Organism-specific databases

    HPAiCAB002303.
    HPA027774.

    Interactioni

    Protein-protein interaction databases

    BioGridi112475. 2 interactions.
    STRINGi9606.ENSP00000342082.

    Structurei

    Secondary structure

    1
    132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi86 – 883
    Beta strandi95 – 973
    Helixi108 – 1103
    Beta strandi116 – 1205
    Beta strandi123 – 1275

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z7FX-ray1.70I83-132[»]
    4DOQX-ray2.00B/D85-131[»]
    ProteinModelPortaliP03973.
    SMRiP03973. Positions 83-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03973.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 7649WAP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini82 – 13049WAP 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 8358Trypsin inhibitory domainAdd
    BLAST
    Regioni84 – 13249Elastase inhibitory domainAdd
    BLAST

    Sequence similaritiesi

    Contains 2 WAP domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG45457.
    HOGENOMiHOG000115819.
    HOVERGENiHBG018073.
    InParanoidiP03973.
    OMAiPWAVEGS.
    OrthoDBiEOG7S7SG9.
    PhylomeDBiP03973.
    TreeFamiTF338375.

    Family and domain databases

    Gene3Di4.10.75.10. 2 hits.
    InterProiIPR008197. WAP.
    [Graphical view]
    PfamiPF00095. WAP. 2 hits.
    [Graphical view]
    PRINTSiPR00003. 4DISULPHCORE.
    SMARTiSM00217. WAP. 2 hits.
    [Graphical view]
    SUPFAMiSSF57256. SSF57256. 2 hits.
    PROSITEiPS51390. WAP. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P03973-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSSGLFPFL VLLALGTLAP WAVEGSGKSF KAGVCPPKKS AQCLRYKKPE    50
    CQSDWQCPGK KRCCPDTCGI KCLDPVDTPN PTRRKPGKCP VTYGQCLMLN 100
    PPNFCEMDGQ CKRDLKCCMG MCGKSCVSPV KA 132
    Length:132
    Mass (Da):14,326
    Last modified:October 1, 1989 - v2
    Checksum:iB62F3221E0903D90
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04470 mRNA. Translation: CAA28158.1.
    X04502 Genomic DNA. Translation: CAA28187.1.
    X04503 mRNA. Translation: CAA28188.1.
    AF114471 mRNA. Translation: AAD19661.1.
    AK312192 mRNA. Translation: BAG35125.1.
    AL035660 Genomic DNA. Translation: CAB64235.1.
    CH471077 Genomic DNA. Translation: EAW75869.1.
    BC020708 mRNA. Translation: AAH20708.1.
    CCDSiCCDS13347.1.
    PIRiA25541. TIHUSP.
    RefSeqiNP_003055.1. NM_003064.3.
    UniGeneiHs.517070.

    Genome annotation databases

    EnsembliENST00000338380; ENSP00000342082; ENSG00000124107.
    GeneIDi6590.
    KEGGihsa:6590.
    UCSCiuc002xnm.1. human.

    Polymorphism databases

    DMDMi113636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04470 mRNA. Translation: CAA28158.1 .
    X04502 Genomic DNA. Translation: CAA28187.1 .
    X04503 mRNA. Translation: CAA28188.1 .
    AF114471 mRNA. Translation: AAD19661.1 .
    AK312192 mRNA. Translation: BAG35125.1 .
    AL035660 Genomic DNA. Translation: CAB64235.1 .
    CH471077 Genomic DNA. Translation: EAW75869.1 .
    BC020708 mRNA. Translation: AAH20708.1 .
    CCDSi CCDS13347.1.
    PIRi A25541. TIHUSP.
    RefSeqi NP_003055.1. NM_003064.3.
    UniGenei Hs.517070.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z7F X-ray 1.70 I 83-132 [» ]
    4DOQ X-ray 2.00 B/D 85-131 [» ]
    ProteinModelPortali P03973.
    SMRi P03973. Positions 83-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112475. 2 interactions.
    STRINGi 9606.ENSP00000342082.

    Protein family/group databases

    MEROPSi I17.001.

    Polymorphism databases

    DMDMi 113636.

    Proteomic databases

    MaxQBi P03973.
    PaxDbi P03973.
    PeptideAtlasi P03973.
    PRIDEi P03973.

    Protocols and materials databases

    DNASUi 6590.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338380 ; ENSP00000342082 ; ENSG00000124107 .
    GeneIDi 6590.
    KEGGi hsa:6590.
    UCSCi uc002xnm.1. human.

    Organism-specific databases

    CTDi 6590.
    GeneCardsi GC20M043880.
    HGNCi HGNC:11092. SLPI.
    HPAi CAB002303.
    HPA027774.
    MIMi 107285. gene.
    neXtProti NX_P03973.
    PharmGKBi PA35944.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45457.
    HOGENOMi HOG000115819.
    HOVERGENi HBG018073.
    InParanoidi P03973.
    OMAi PWAVEGS.
    OrthoDBi EOG7S7SG9.
    PhylomeDBi P03973.
    TreeFami TF338375.

    Miscellaneous databases

    ChiTaRSi SLPI. human.
    EvolutionaryTracei P03973.
    GeneWikii SLPI.
    GenomeRNAii 6590.
    NextBioi 25637.
    PMAP-CutDB P03973.
    PROi P03973.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P03973.
    Bgeei P03973.
    CleanExi HS_SLPI.
    Genevestigatori P03973.

    Family and domain databases

    Gene3Di 4.10.75.10. 2 hits.
    InterProi IPR008197. WAP.
    [Graphical view ]
    Pfami PF00095. WAP. 2 hits.
    [Graphical view ]
    PRINTSi PR00003. 4DISULPHCORE.
    SMARTi SM00217. WAP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57256. SSF57256. 2 hits.
    PROSITEi PS51390. WAP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus."
      Heinzel R., Appelhans H., Gassen G., Seemueller U., Machleidt W., Fritz H., Steffens G.
      Eur. J. Biochem. 160:61-67(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix.
    2. "Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases."
      Stetler G., Brewer M.T., Thompson R.C.
      Nucleic Acids Res. 14:7883-7896(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Parotid gland.
    3. "Cloning and characterization of SLPI from human intestinal epithelium."
      Si-Tahar M., Merlin D., Sitaraman S., Madara J.L.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Intestine.
    4. "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].
      Tissue: Tongue.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Liver.
    8. "The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red sea turtle proteinase inhibitor."
      Seemueller U., Arnhold M., Fritz H., Wiedenmann K., Machleidt W., Heinzel R., Appelhans H., Gassen H.-G., Lottspeich F.
      FEBS Lett. 199:43-48(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-132, NUCLEOTIDE SEQUENCE OF 26-65.
    9. "Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase."
      Thompson R.C., Ohlsson K.
      Proc. Natl. Acad. Sci. U.S.A. 83:6692-6696(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-132.
    10. "Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor."
      Sallenave J.-M., Ryle A.P.
      Biol. Chem. Hoppe-Seyler 372:13-21(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-52.
    11. "The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin."
      Gruetter M.G., Fendrich G., Huber R., Bode W.
      EMBO J. 7:345-351(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiSLPI_HUMAN
    AccessioniPrimary (citable) accession number: P03973
    Secondary accession number(s): B2R5H8, P07757
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 154 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

    Miscellaneous

    The pathologies of several chronic and acute diseases of the respiratory tract involve an imbalance between the proteases of cells involved in inflammatary responses and the inhibitors of these proteases. The inflammation-mediated release of neutrophil elastase in the lungs of patients whose levels of active alpha-1-antiprotease are compromised by genetic background, cigarette smoking, air pollutants, or a combination of all three can result in severe lung damage and a decreased lifespan. The relatively small size of this protein, its lack of glycosylation and its stability make this protein a candidate for use as a therapeutic agent in diseases mediated by leukocyte elastase-antielastase imbalances.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3