CAMP_MOUSE
ID CAMP_MOUSE Reviewed; 172 AA.
AC P51437; Q0VB78;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cathelicidin antimicrobial peptide {ECO:0000312|MGI:MGI:108443};
DE AltName: Full=Cathelin-like protein {ECO:0000303|PubMed:8706928};
DE Short=CLP {ECO:0000303|PubMed:8706928};
DE Contains:
DE RecName: Full=Cathelin-related antimicrobial peptide {ECO:0000303|PubMed:9148921};
DE Short=Cramp {ECO:0000303|PubMed:9148921};
DE Flags: Precursor;
GN Name=Camp {ECO:0000312|MGI:MGI:108443};
GN Synonyms=Cnlp, Cramp {ECO:0000303|PubMed:9148921};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=9148921; DOI=10.1074/jbc.272.20.13088;
RA Gallo R.L., Kim K.J., Bernfield M., Kozak C.A., Zanetti M., Merluzzi L.,
RA Gennaro R.;
RT "Identification of CRAMP, a cathelin-related antimicrobial peptide
RT expressed in the embryonic and adult mouse.";
RL J. Biol. Chem. 272:13088-13093(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX PubMed=8706928; DOI=10.1016/0014-5793(96)00692-8;
RA Popsueva A.E., Zinovjeva M.V., Visser Y.W.M., Fibbe W.E., Belyavsky A.V.;
RT "A novel murine cathelin-like protein expressed in bone marrow.";
RL FEBS Lett. 391:5-8(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Huttner K.M., Piraino J., Gallo R.L.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS) and has
CC antibacterial activity. Acts via neutrophil N-formyl peptide receptors
CC to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P49913}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in testis, spleen, stomach, and
CC intestine. Very low expression found in heart, lung and skeletal
CC muscle. No expression in brain, kidney or liver.
CC -!- PTM: Proteolytically cleaved by cathepsin CTSG.
CC {ECO:0000250|UniProtKB:P49913}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; U43409; AAA85898.1; -; mRNA.
DR EMBL; X94353; CAA64078.1; -; mRNA.
DR EMBL; AF035680; AAB88303.1; -; Genomic_DNA.
DR EMBL; BC120752; AAI20753.1; -; mRNA.
DR EMBL; BC120754; AAI20755.1; -; mRNA.
DR CCDS; CCDS52934.1; -.
DR PIR; S70521; S70521.
DR RefSeq; NP_034051.2; NM_009921.2.
DR AlphaFoldDB; P51437; -.
DR SMR; P51437; -.
DR STRING; 10090.ENSMUSP00000107653; -.
DR PhosphoSitePlus; P51437; -.
DR PaxDb; P51437; -.
DR PeptideAtlas; P51437; -.
DR PRIDE; P51437; -.
DR ProteomicsDB; 265328; -.
DR Antibodypedia; 13077; 428 antibodies from 35 providers.
DR DNASU; 12796; -.
DR Ensembl; ENSMUST00000112022; ENSMUSP00000107653; ENSMUSG00000038357.
DR GeneID; 12796; -.
DR KEGG; mmu:12796; -.
DR UCSC; uc009rsv.2; mouse.
DR CTD; 820; -.
DR MGI; MGI:108443; Camp.
DR VEuPathDB; HostDB:ENSMUSG00000038357; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR InParanoid; P51437; -.
DR OMA; MERGWIM; -.
DR OrthoDB; 1534863at2759; -.
DR PhylomeDB; P51437; -.
DR TreeFam; TF338457; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 12796; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Camp; mouse.
DR PRO; PR:P51437; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P51437; protein.
DR Bgee; ENSMUSG00000038357; Expressed in granulocyte and 66 other tissues.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042581; C:specific granule; IDA:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0002544; P:chronic inflammatory response; ISO:MGI.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:MGI.
DR GO; GO:0051873; P:killing by host of symbiont cells; IMP:MGI.
DR GO; GO:0035821; P:modulation of process of another organism; ISO:MGI.
DR GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0001878; P:response to yeast; ISO:MGI.
DR InterPro; IPR001894; Cathelicidin-like.
DR InterPro; IPR018216; Cathelicidin_CS.
DR InterPro; IPR022746; Cathlecidin_C.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR10206; PTHR10206; 1.
DR Pfam; PF12153; CAP18_C; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00946; CATHELICIDINS_1; 1.
DR PROSITE; PS00947; CATHELICIDINS_2; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..134
FT /evidence="ECO:0000250|UniProtKB:P49913"
FT /id="PRO_0000435275"
FT PEPTIDE 135..172
FT /note="Cathelin-related antimicrobial peptide"
FT /evidence="ECO:0000305|PubMed:9148921"
FT /id="PRO_0000435276"
FT DISULFID 83..94
FT /evidence="ECO:0000250"
FT DISULFID 105..122
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="L -> M (in Ref. 2; CAA64078)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="E -> EQ (in Ref. 2; CAA64078, 3; AAB88303 and 4;
FT AAI20753/AAI20755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19453 MW; 6F0E784762F77E4A CRC64;
MQFQRDVPSL WLWRSLSLLL LLGLGFSQTP SYRDAVLRAV DDFNQQSLDT NLYRLLDLDP
EPQGDEDPDT PKSVRFRVKE TVCGKAERQL PEQCAFKEQG VVKQCMGAVT LNPAADSFDI
SCNEPGAQPF RFKKISRLAG LLRKGGEKIG EKLKKIGQKI KNFFQKLVPQ PE
