CTHL3_CHICK
ID CTHL3_CHICK Reviewed; 151 AA.
AC Q2IAL6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cathelicidin-3;
DE Short=CATH-3;
DE AltName: Full=Fowlicidin-3;
DE Flags: Precursor;
GN Name=CATHL3;
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 [GENOMIC DNA / MRNA].
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 [2]
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).
CC -!- FUNCTION: May bind bacterial lipopolysaccharide (LPS). May have
CC antimicrobial activity and play a role in the innate immune response
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in bone marrow, liver and lung.
CC {ECO:0000269|PubMed:17827276}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ092353; AAZ42401.1; -; mRNA.
DR EMBL; DQ092350; AAZ65843.1; -; Genomic_DNA.
DR EMBL; AB308318; BAF75955.1; -; Genomic_DNA.
DR RefSeq; NP_001298106.1; NM_001311177.1.
DR PDB; 2HFR; NMR; -; A=125-151.
DR PDBsum; 2HFR; -.
DR AlphaFoldDB; Q2IAL6; -.
DR BMRB; Q2IAL6; -.
DR SMR; Q2IAL6; -.
DR STRING; 9031.ENSGALP00000030659; -.
DR Ensembl; ENSGALT00000061585; ENSGALP00000056590; ENSGALG00000034150.
DR GeneID; 100858343; -.
DR KEGG; gga:100858343; -.
DR CTD; 100858343; -.
DR VEuPathDB; HostDB:geneid_100858343; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR InParanoid; Q2IAL6; -.
DR OMA; ICCRETS; -.
DR PhylomeDB; Q2IAL6; -.
DR EvolutionaryTrace; Q2IAL6; -.
DR PRO; PR:Q2IAL6; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000034150; Expressed in granulocyte and 7 other tissues.
DR ExpressionAtlas; Q2IAL6; baseline.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0042116; P:macrophage activation; IDA:AgBase.
DR GO; GO:0051673; P:membrane disruption in another organism; IMP:AgBase.
DR GO; GO:0001819; P:positive regulation of cytokine production; 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; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..122
FT /evidence="ECO:0000255"
FT /id="PRO_0000333224"
FT PEPTIDE 123..151
FT /note="Cathelicidin-3"
FT /id="PRO_0000333225"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT DISULFID 97..114
FT /evidence="ECO:0000250"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2HFR"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:2HFR"
FT TURN 145..149
FT /evidence="ECO:0007829|PDB:2HFR"
SQ SEQUENCE 151 AA; 16281 MW; D6071251413C9828 CRC64;
MLSCWVLLLA LLGGACALPA PLGYSQALAQ AVDSYNQRPE VQNAFRLLSA DPEPGPNVQL
SSLHNLNFTI METRCQARSG AQLDSCEFKE DGLVKDCAAP VVLQGGRAVL DVTCVDSMAD
PVRVKRFWPL VPVAINTVAA GINLYKAIRR K
