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P49913 (CAMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Antibacterial protein FALL-39
    Alternative name(s):
    FALL-39 peptide antibiotic
  2. Antibacterial protein LL-37
Gene names
Name:CAMP
Synonyms:CAP18, FALL39
ORF Names:HSD26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. Ref.11 Ref.12

Subcellular location

Secreted.

Tissue specificity

Expressed in bone marrow and testis and neutrophils.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the cathelicidin family.

Caution

Ref.8 sequence was incorrectly assigned to originate from M.mulatta.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IGF1RP080693EBI-6378485,EBI-475981

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Propeptide31 – 131101
PRO_0000004722
Chain132 – 17039Antibacterial protein FALL-39
PRO_0000004723
Chain134 – 17037Antibacterial protein LL-37
PRO_0000004724

Amino acid modifications

Disulfide bond86 ↔ 97 By similarity
Disulfide bond108 ↔ 125 By similarity

Experimental info

Sequence conflict61D → N Ref.1
Sequence conflict61D → N Ref.6
Sequence conflict61D → N Ref.7
Sequence conflict61D → N in CAG46759. Ref.9

Secondary structure

................. 170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49913 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 055B07DCA95A7D16

FASTA17019,301
        10         20         30         40         50         60 
MKTQRDGHSL GRWSLVLLLL GLVMPLAIIA QVLSYKEAVL RAIDGINQRS SDANLYRLLD 

        70         80         90        100        110        120 
LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QQSPEDCDFK KDGLVKRCMG TVTLNQARGS 

       130        140        150        160        170 
FDISCDKDNK RFALLGDFFR KSKEKIGKEF KRIVQRIKDF LRNLVPRTES 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI38932.
S74248.
RefSeqNP_004336.3. NM_004345.4.
UniGeneHs.51120.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FBSNMR-N150-162[»]
2FBUNMR-H134-145[»]
2FCGNMR-F146-170[»]
2K6ONMR-A134-170[»]
2LMFNMR-A134-156[»]
4EYCX-ray1.90A/B31-133[»]
DisProtDP00004.
ProteinModelPortalP49913.
SMRP49913. Positions 31-130, 134-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49913. 2 interactions.
STRING9606.ENSP00000296435.

Protein family/group databases

TCDB1.C.33.1.10. the cathelicidin (cathelicidin) family.

Polymorphism databases

DMDM1706745.

Proteomic databases

PaxDbP49913.
PRIDEP49913.

Protocols and materials databases

DNASU820.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000576243; ENSP00000458149; ENSG00000164047.
GeneID820.
KEGGhsa:820.

Organism-specific databases

CTD820.
GeneCardsGC03P048264.
HGNCHGNC:1472. CAMP.
HPACAB015949.
CAB016522.
HPA029874.
MIM600474. gene.
neXtProtNX_P49913.
PharmGKBPA26054.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40811.
HOGENOMHOG000093184.
HOVERGENHBG006116.
InParanoidP49913.
KOK13916.
PhylomeDBP49913.
TreeFamTF338457.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP49913.
BgeeP49913.
CleanExHS_CAMP.
GenevestigatorP49913.

Family and domain databases

InterProIPR001894. Cathelicidin.
IPR018216. Cathelicidin_CS.
IPR022746. Cathlecidin_C.
[Graphical view]
PANTHERPTHR10206. PTHR10206. 1 hit.
PfamPF12153. CAP18_C. 1 hit.
PF00666. Cathelicidins. 1 hit.
[Graphical view]
ProDomPD001838. Cathelicidin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00946. CATHELICIDINS_1. 1 hit.
PS00947. CATHELICIDINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49913.
GeneWikiCathelicidin.
GenomeRNAi820.
NextBio3356.
PMAP-CutDBP49913.
PROP49913.
SOURCESearch...

Entry information

Entry nameCAMP_HUMAN
AccessionPrimary (citable) accession number: P49913
Secondary accession number(s): Q71SN9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM