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P49913

- CAMP_HUMAN

UniProt

P49913 - CAMP_HUMAN

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Protein
Cathelicidin antimicrobial peptide
Gene
CAMP, CAP18, FALL39, HSD26
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. antibacterial humoral response Source: UniProt
  2. defense response to Gram-positive bacterium Source: UniProt
  3. defense response to bacterium Source: ProtInc
  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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26054.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP49913.

Family & Domainsi

Sequence similaritiesi

Belongs to the cathelicidin family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61D → N1 Publication
Sequence conflicti6 – 61D → N1 Publication
Sequence conflicti6 – 61D → N1 Publication
Sequence conflicti6 – 61D → N in CAG46759. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
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
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

1 Publication sequence was incorrectly assigned to originate from M.mulatta.

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

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