P49913 (CAMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial
PTM	Cleavage on pair of basic residues Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	killing by host of symbiont cells Inferred from direct assay. Source: MGI negative regulation of growth of symbiont on or near host surface Inferred from direct assay. Source: MGI
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Propeptide

31 – 131

101

PRO_0000004722

Chain

132 – 170

39

Antibacterial protein FALL-39

PRO_0000004723

Chain

134 – 170

37

Antibacterial protein LL-37

PRO_0000004724

Amino acid modifications

Modified residue

31

1

Pyrrolidone carboxylic acid By similarity

Disulfide bond

86 ↔ 97

By similarity

Disulfide bond

108 ↔ 125

By similarity

Experimental info

Sequence conflict

6

1

D → N Ref.1

Sequence conflict

6

1

D → N Ref.6

Sequence conflict

6

1

D → N Ref.7

Sequence conflict

6

1

D → N in CAG46759. Ref.9

Secondary structure

1

.

.

.

.

.

170

Helix Strand Turn

Details...

Helix

136 – 140

5

Helix

151 – 161

11

Sequences

	Sequence		Length	Mass (Da)
	P49913 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 055B07DCA95A7D16	FASTA	170	19,301
	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

References

	« Hide 'large scale' referencesShow '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: 7529412] [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: 7615076] [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: 7890387] [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: 8946956] [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: 8681941] [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: 11238224] [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: 15489334] [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: 16637646] [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: 18818205] [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.

IPI

IPI00292532.

PIR

I38932.
S74248.

RefSeq

NP_004336.3. NM_004345.4.

UniGene

Hs.51120.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P49913.

SMR

P49913. Positions 31-127, 134-170.

DisProt

DP00004.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49913. 1 interaction.

STRING

P49913.

Protein family/group databases

TCDB

1.C.33.1.10. cathelicidin family.

Polymorphism databases

DMDM

1706745.

Proteomic databases

PRIDE

P49913.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296435; ENSP00000296435; ENSG00000164047.

GeneID

820.

KEGG

hsa:820.

UCSC

uc003csj.1. human.

Organism-specific databases

CTD

820.

GeneCards

GC03P048240.

H-InvDB

HIX0024318.

HGNC

HGNC:1472. CAMP.

HPA

CAB015949.
CAB016522.
HPA029874.

MIM

600474. gene.

neXtProt

NX_P49913.

PharmGKB

PA26054.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07162.

GeneTree

ENSGT00390000000410.

HOGENOM

HBG127142.

HOVERGEN

HBG006116.

InParanoid

P49913.

OMA

QRSSDAN.

OrthoDB

EOG4PK29B.

Gene expression databases

ArrayExpress

P49913.

Bgee

P49913.

CleanEx

HS_CAMP.

Genevestigator

P49913.

GermOnline

ENSG00000164047. Homo sapiens.

Family and domain databases

InterPro

IPR001894. Cathelicidin.
IPR018216. Cathelicidin_CS.
IPR022746. Cathlecidin_C.
[Graphical view]

KO

K13916.

PANTHER

PTHR10206. Cathelicidin. 1 hit.

Pfam

PF12153. CAP18_C. 1 hit.
PF00666. Cathelicidins. 1 hit.
[Graphical view]

ProDom

PD001838. Cathelicidin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00946. CATHELICIDINS_1. 1 hit.
PS00947. CATHELICIDINS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

3356.

PMAP-CutDB

P49913.

SOURCE

Search...

Entry information

Entry name

CAMP_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.