Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P49913

- CAMP_HUMAN

UniProt

P49913 - CAMP_HUMAN

Protein

Cathelicidin antimicrobial peptide

Gene

CAMP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. defense response to bacterium Source: ProtInc
    3. defense response to Gram-positive bacterium Source: UniProt
    4. innate immune response in mucosa Source: UniProt
    5. interaction with host Source: Reactome
    6. killing by host of symbiont cells Source: MGI
    7. negative regulation of growth of symbiont on or near host surface Source: MGI
    8. phagosome maturation Source: Reactome

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial

    Enzyme and pathway databases

    ReactomeiREACT_121256. Phagosomal maturation (early endosomal stage).

    Protein family/group databases

    TCDBi1.C.33.1.10. the cathelicidin (cathelicidin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathelicidin antimicrobial peptide
    Alternative name(s):
    18 kDa cationic antimicrobial protein
    Short name:
    CAP-18
    Short name:
    hCAP-18
    Cleaved into the following 2 chains:
    Alternative name(s):
    FALL-39 peptide antibiotic
    Gene namesi
    Name:CAMP
    Synonyms:CAP18, FALL39
    ORF Names:HSD26
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1472. CAMP.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: Reactome
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26054.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Propeptidei31 – 131101PRO_0000004722Add
    BLAST
    Chaini132 – 17039Antibacterial protein FALL-39PRO_0000004723Add
    BLAST
    Chaini134 – 17037Antibacterial protein LL-37PRO_0000004724Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi86 ↔ 97By similarity
    Disulfide bondi108 ↔ 125By similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP49913.
    PRIDEiP49913.

    Miscellaneous databases

    PMAP-CutDBP49913.

    Expressioni

    Tissue specificityi

    Expressed in bone marrow and testis and neutrophils.

    Gene expression databases

    ArrayExpressiP49913.
    BgeeiP49913.
    CleanExiHS_CAMP.
    GenevestigatoriP49913.

    Organism-specific databases

    HPAiCAB015949.
    CAB016522.
    HPA029874.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IGF1RP080693EBI-6378485,EBI-475981

    Protein-protein interaction databases

    IntActiP49913. 2 interactions.
    STRINGi9606.ENSP00000296435.

    Structurei

    Secondary structure

    1
    170
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 4915
    Beta strandi53 – 619
    Beta strandi75 – 8713
    Helixi94 – 963
    Beta strandi105 – 1128
    Beta strandi122 – 1265
    Helixi136 – 1405
    Helixi151 – 16111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FBSNMR-N150-162[»]
    2FBUNMR-H134-145[»]
    2FCGNMR-F146-170[»]
    2K6ONMR-A134-170[»]
    2LMFNMR-A134-156[»]
    4EYCX-ray1.90A/B31-133[»]
    DisProtiDP00004.
    ProteinModelPortaliP49913.
    SMRiP49913. Positions 31-130, 134-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49913.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cathelicidin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40811.
    HOGENOMiHOG000093184.
    HOVERGENiHBG006116.
    InParanoidiP49913.
    KOiK13916.
    PhylomeDBiP49913.
    TreeFamiTF338457.

    Family and domain databases

    InterProiIPR001894. Cathelicidin.
    IPR018216. Cathelicidin_CS.
    IPR022746. Cathlecidin_C.
    [Graphical view]
    PANTHERiPTHR10206. PTHR10206. 1 hit.
    PfamiPF12153. CAP18_C. 1 hit.
    PF00666. Cathelicidins. 1 hit.
    [Graphical view]
    ProDomiPD001838. Cathelicidin. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    PROSITEiPS00946. CATHELICIDINS_1. 1 hit.
    PS00947. CATHELICIDINS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49913-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTQRDGHSL GRWSLVLLLL GLVMPLAIIA QVLSYKEAVL RAIDGINQRS    50
    SDANLYRLLD LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QQSPEDCDFK 100
    KDGLVKRCMG TVTLNQARGS FDISCDKDNK RFALLGDFFR KSKEKIGKEF 150
    KRIVQRIKDF LRNLVPRTES 170
    Length:170
    Mass (Da):19,301
    Last modified:October 1, 1996 - v1
    Checksum:i055B07DCA95A7D16
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61D → N(PubMed:7529412)Curated
    Sequence conflicti6 – 61D → N1 PublicationCurated
    Sequence conflicti6 – 61D → N1 PublicationCurated
    Sequence conflicti6 – 61D → N in CAG46759. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38026 mRNA. Translation: CAA86115.1.
    X89658 mRNA. Translation: CAA61805.1.
    U19970 mRNA. Translation: AAA74084.1.
    U48795 Genomic DNA. Translation: AAC02634.1.
    X96735 Genomic DNA. No translation available.
    AY162210 mRNA. Translation: AAN78318.1.
    AY251531 mRNA. Translation: AAP20054.1.
    AF288284 mRNA. Translation: AAG40802.1.
    CR457083 mRNA. Translation: CAG33364.1.
    CR541961 mRNA. Translation: CAG46759.1.
    BC055089 mRNA. Translation: AAH55089.1.
    PIRiI38932.
    S74248.
    RefSeqiNP_004336.3. NM_004345.4.
    UniGeneiHs.51120.

    Genome annotation databases

    EnsembliENST00000576243; ENSP00000458149; ENSG00000164047.
    GeneIDi820.
    KEGGihsa:820.

    Polymorphism databases

    DMDMi1706745.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38026 mRNA. Translation: CAA86115.1 .
    X89658 mRNA. Translation: CAA61805.1 .
    U19970 mRNA. Translation: AAA74084.1 .
    U48795 Genomic DNA. Translation: AAC02634.1 .
    X96735 Genomic DNA. No translation available.
    AY162210 mRNA. Translation: AAN78318.1 .
    AY251531 mRNA. Translation: AAP20054.1 .
    AF288284 mRNA. Translation: AAG40802.1 .
    CR457083 mRNA. Translation: CAG33364.1 .
    CR541961 mRNA. Translation: CAG46759.1 .
    BC055089 mRNA. Translation: AAH55089.1 .
    PIRi I38932.
    S74248.
    RefSeqi NP_004336.3. NM_004345.4.
    UniGenei Hs.51120.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FBS NMR - N 150-162 [» ]
    2FBU NMR - H 134-145 [» ]
    2FCG NMR - F 146-170 [» ]
    2K6O NMR - A 134-170 [» ]
    2LMF NMR - A 134-156 [» ]
    4EYC X-ray 1.90 A/B 31-133 [» ]
    DisProti DP00004.
    ProteinModelPortali P49913.
    SMRi P49913. Positions 31-130, 134-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49913. 2 interactions.
    STRINGi 9606.ENSP00000296435.

    Protein family/group databases

    TCDBi 1.C.33.1.10. the cathelicidin (cathelicidin) family.

    Polymorphism databases

    DMDMi 1706745.

    Proteomic databases

    PaxDbi P49913.
    PRIDEi P49913.

    Protocols and materials databases

    DNASUi 820.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000576243 ; ENSP00000458149 ; ENSG00000164047 .
    GeneIDi 820.
    KEGGi hsa:820.

    Organism-specific databases

    CTDi 820.
    GeneCardsi GC03P048264.
    HGNCi HGNC:1472. CAMP.
    HPAi CAB015949.
    CAB016522.
    HPA029874.
    MIMi 600474. gene.
    neXtProti NX_P49913.
    PharmGKBi PA26054.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40811.
    HOGENOMi HOG000093184.
    HOVERGENi HBG006116.
    InParanoidi P49913.
    KOi K13916.
    PhylomeDBi P49913.
    TreeFami TF338457.

    Enzyme and pathway databases

    Reactomei REACT_121256. Phagosomal maturation (early endosomal stage).

    Miscellaneous databases

    EvolutionaryTracei P49913.
    GeneWikii Cathelicidin.
    GenomeRNAii 820.
    NextBioi 3356.
    PMAP-CutDB P49913.
    PROi P49913.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49913.
    Bgeei P49913.
    CleanExi HS_CAMP.
    Genevestigatori P49913.

    Family and domain databases

    InterProi IPR001894. Cathelicidin.
    IPR018216. Cathelicidin_CS.
    IPR022746. Cathlecidin_C.
    [Graphical view ]
    PANTHERi PTHR10206. PTHR10206. 1 hit.
    Pfami PF12153. CAP18_C. 1 hit.
    PF00666. Cathelicidins. 1 hit.
    [Graphical view ]
    ProDomi PD001838. Cathelicidin. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS00946. CATHELICIDINS_1. 1 hit.
    PS00947. CATHELICIDINS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis."
      Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G., Gudmundsson G.H.
      Proc. Natl. Acad. Sci. U.S.A. 92:195-199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 132-170.
      Tissue: Bone marrow.
    2. "hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules."
      Cowland J.B., Johnsen A.H., Borregaard N.
      FEBS Lett. 368:173-176(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-68 AND 83-100.
      Tissue: Bone marrow.
    3. "Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein."
      Larrick J.W., Hirata M., Balint R.F., Lee J., Zhong J., Wright S.C.
      Infect. Immun. 63:1291-1297(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    4. "Structural, functional analysis and localization of the human CAP18 gene."
      Larrick J.W., Lee J., Ma S., Li X., Francke U., Wright S.C., Balint R.F.
      FEBS Lett. 398:74-80(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes."
      Gudmundsson G.H., Agerberth B., Odeberg J., Bergman T., Olsson B., Salcedo R.
      Eur. J. Biochem. 238:325-332(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Gao Y., Huang Y.F., Xia X.Y.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Epididymis.
    7. "A new spermatogenesis-related gene."
      Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    8. "Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules."
      Bals R., Lang C., Weiner D.J., Vogelmeier C., Welsch U., Wilson J.M.
      Clin. Diagn. Lab. Immunol. 8:370-375(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    10. "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].
    11. "Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region."
      Li X., Li Y., Han H., Miller D.W., Wang G.
      J. Am. Chem. Soc. 128:5776-5785(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 146-170, FUNCTION.
    12. "Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles."
      Wang G.
      J. Biol. Chem. 283:32637-32643(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 134-170, FUNCTION.

    Entry informationi

    Entry nameiCAMP_HUMAN
    AccessioniPrimary (citable) accession number: P49913
    Secondary accession number(s): Q71SN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 128 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

    Caution

    PubMed:11238224 sequence was incorrectly assigned to originate from M.mulatta.Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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