CTHL1_CHICK
ID CTHL1_CHICK Reviewed; 148 AA.
AC Q6QLQ5; Q2IAM1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cathelicidin-1;
DE Short=CATH-1;
DE AltName: Full=Fowlicidin-1;
DE Flags: Precursor;
GN Name=CATHL1; Synonyms=CATH;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=15148642; DOI=10.1007/s00251-004-0675-0;
RA Lynn D.J., Higgs R., Gaines S., Tierney J., James T., Lloyd A.T.,
RA Fares M.A., Mulcahy G., O'Farrelly C.;
RT "Bioinformatic discovery and initial characterisation of nine novel
RT antimicrobial peptide genes in the chicken.";
RL Immunogenetics 56:170-177(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=16326712; DOI=10.1074/jbc.m507180200;
RA Xiao Y., Cai Y., Bommineni Y.R., Fernando S.C., Prakash O., Gilliland S.E.,
RA Zhang G.;
RT "Identification and functional characterization of three chicken
RT cathelicidins with potent antimicrobial activity.";
RL J. Biol. Chem. 281:2858-2867(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bursa of Fabricius;
RX PubMed=17827276; DOI=10.1073/pnas.0707037104;
RA Goitsuka R., Chen C.-I.H., Benyon L., Asano Y., Kitamura D., Cooper M.D.;
RT "Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell
RT gateway.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15063-15068(2007).
RN [4]
RP STRUCTURE BY NMR OF 123-148, AND FUNCTION.
RX PubMed=16817888; DOI=10.1111/j.1742-4658.2006.05261.x;
RA Xiao Y., Dai H., Bommineni Y.R., Soulages J.L., Gong Y.X., Prakash O.,
RA Zhang G.;
RT "Structure-activity relationships of fowlicidin-1, a cathelicidin
RT antimicrobial peptide in chicken.";
RL FEBS J. 273:2581-2593(2006).
CC -!- FUNCTION: Binds bacterial lipopolysaccharide (LPS). Has potent
CC antimicrobial activity against Gram-positive and Gram-negative bacteria
CC (in vitro). Has hemolytic activity (in vitro). May play a role in the
CC innate immune response. {ECO:0000269|PubMed:16326712,
CC ECO:0000269|PubMed:16817888}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in gizzard, liver, small intestine, large
CC intestine, cloaca, bursa of Fabricius, gall bladder, lung, trachea,
CC kidney, testis and bone marrow. {ECO:0000269|PubMed:15148642,
CC ECO:0000269|PubMed:17827276}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; AY534900; AAS99323.1; -; mRNA.
DR EMBL; DQ092351; AAZ42399.1; -; mRNA.
DR EMBL; DQ092350; AAZ65841.1; -; Genomic_DNA.
DR EMBL; AB308318; BAF75952.1; -; Genomic_DNA.
DR RefSeq; NP_001001605.1; NM_001001605.3.
DR PDB; 2AMN; NMR; -; A=123-148.
DR PDBsum; 2AMN; -.
DR AlphaFoldDB; Q6QLQ5; -.
DR BMRB; Q6QLQ5; -.
DR SMR; Q6QLQ5; -.
DR STRING; 9031.ENSGALP00000042184; -.
DR Ensembl; ENSGALT00000045759; ENSGALP00000042184; ENSGALG00000027973.
DR GeneID; 414337; -.
DR KEGG; gga:414337; -.
DR CTD; 414337; -.
DR VEuPathDB; HostDB:geneid_414337; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR HOGENOM; CLU_121724_1_1_1; -.
DR InParanoid; Q6QLQ5; -.
DR OMA; HFNIDIC; -.
DR OrthoDB; 1534863at2759; -.
DR PhylomeDB; Q6QLQ5; -.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-6803157; Antimicrobial peptides.
DR EvolutionaryTrace; Q6QLQ5; -.
DR PRO; PR:Q6QLQ5; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000027973; Expressed in granulocyte and 4 other tissues.
DR ExpressionAtlas; Q6QLQ5; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:AgBase.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IDA:AgBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:AgBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:AgBase.
DR GO; GO:0045087; P:innate immune response; IDA:AgBase.
DR GO; GO:0042116; P:macrophage activation; IDA:AgBase.
DR GO; GO:0051673; P:membrane disruption in another organism; IMP:AgBase.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:AgBase.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:AgBase.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; IDA:AgBase.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:AgBase.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:AgBase.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IDA:AgBase.
DR InterPro; IPR001894; Cathelicidin-like.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR10206; PTHR10206; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Disulfide bond; Immunity;
KW Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..122
FT /evidence="ECO:0000255"
FT /id="PRO_0000333220"
FT PEPTIDE 123..148
FT /note="Cathelicidin-1"
FT /id="PRO_0000333221"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT DISULFID 97..114
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="A -> G (in Ref. 2; AAZ65841)"
FT /evidence="ECO:0000305"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2AMN"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2AMN"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2AMN"
SQ SEQUENCE 148 AA; 16072 MW; 26B5418625FFA2B9 CRC64;
MLSCWVLLLA LLGGACALPA PLGYSQALAQ AVDSYNQRPE VQNAFRLLSA DPEPGPNVQL
SSLHNLNFTI METRCQARSG AQLDSCEFKE DGLVKDCAAP VVLQGGRAVL DVTCVDSMAD
PVRVKRVWPL VIRTVIAGYN LYRAIKKK