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Protein

Cathelicidin-1

Gene

CATHL1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds bacterial lipopolysaccharide (LPS). Has potent antimicrobial activity against Gram-positive and Gram-negative bacteria (in vitro). Has hemolytic activity (in vitro). May play a role in the innate immune response.2 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: AgBase

GO - Biological processi

  • cell death Source: AgBase
  • cytolysis Source: AgBase
  • defense response to Gram-negative bacterium Source: AgBase
  • defense response to Gram-positive bacterium Source: AgBase
  • immunoglobulin production involved in immunoglobulin mediated immune response Source: AgBase
  • innate immune response Source: UniProtKB-KW
  • macrophage activation Source: AgBase
  • membrane disruption in other organism Source: AgBase
  • negative regulation of gene expression Source: AgBase
  • neutrophil chemotaxis Source: AgBase
  • positive regulation of gene expression Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Cathelicidin-1
Short name:
CATH-1
Alternative name(s):
Fowlicidin-1
Gene namesi
Name:CATHL1
Synonyms:CATH
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 122105Sequence analysisPRO_0000333220Add
BLAST
Peptidei123 – 14826Cathelicidin-1PRO_0000333221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 86By similarity
Disulfide bondi97 ↔ 114By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ6QLQ5.

Expressioni

Tissue specificityi

Detected in gizzard, liver, small intestine, large intestine, cloaca, bursa of Fabricius, gall bladder, lung, trachea, kidney, testis and bone marrow.2 Publications

Gene expression databases

ExpressionAtlasiQ6QLQ5. differential.

Structurei

Secondary structure

1
148
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi131 – 1399Combined sources
Beta strandi140 – 1423Combined sources
Helixi143 – 1464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AMNNMR-A123-148[»]
ProteinModelPortaliQ6QLQ5.
SMRiQ6QLQ5. Positions 123-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6QLQ5.

Family & Domainsi

Sequence similaritiesi

Belongs to the cathelicidin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000000410.
HOVERGENiHBG099601.
InParanoidiQ6QLQ5.
OMAiGRKLENI.
PhylomeDBiQ6QLQ5.

Family and domain databases

InterProiIPR001894. Cathelicidin.
[Graphical view]
PANTHERiPTHR10206. PTHR10206. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6QLQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSCWVLLLA LLGGACALPA PLGYSQALAQ AVDSYNQRPE VQNAFRLLSA
60 70 80 90 100
DPEPGPNVQL SSLHNLNFTI METRCQARSG AQLDSCEFKE DGLVKDCAAP
110 120 130 140
VVLQGGRAVL DVTCVDSMAD PVRVKRVWPL VIRTVIAGYN LYRAIKKK
Length:148
Mass (Da):16,072
Last modified:July 5, 2004 - v1
Checksum:i26B5418625FFA2B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → G in AAZ65841 (PubMed:16326712).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY534900 mRNA. Translation: AAS99323.1.
DQ092351 mRNA. Translation: AAZ42399.1.
DQ092350 Genomic DNA. Translation: AAZ65841.1.
AB308318 Genomic DNA. Translation: BAF75952.1.
RefSeqiNP_001001605.1. NM_001001605.3.
UniGeneiGga.51464.

Genome annotation databases

EnsembliENSGALT00000045759; ENSGALP00000042184; ENSGALG00000027973.
GeneIDi414337.
KEGGigga:414337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY534900 mRNA. Translation: AAS99323.1.
DQ092351 mRNA. Translation: AAZ42399.1.
DQ092350 Genomic DNA. Translation: AAZ65841.1.
AB308318 Genomic DNA. Translation: BAF75952.1.
RefSeqiNP_001001605.1. NM_001001605.3.
UniGeneiGga.51464.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AMNNMR-A123-148[»]
ProteinModelPortaliQ6QLQ5.
SMRiQ6QLQ5. Positions 123-148.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6QLQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000045759; ENSGALP00000042184; ENSGALG00000027973.
GeneIDi414337.
KEGGigga:414337.

Organism-specific databases

CTDi414337.

Phylogenomic databases

GeneTreeiENSGT00390000000410.
HOVERGENiHBG099601.
InParanoidiQ6QLQ5.
OMAiGRKLENI.
PhylomeDBiQ6QLQ5.

Miscellaneous databases

EvolutionaryTraceiQ6QLQ5.
NextBioi20818692.
PROiQ6QLQ5.

Gene expression databases

ExpressionAtlasiQ6QLQ5. differential.

Family and domain databases

InterProiIPR001894. Cathelicidin.
[Graphical view]
PANTHERiPTHR10206. PTHR10206. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken."
    Lynn D.J., Higgs R., Gaines S., Tierney J., James T., Lloyd A.T., Fares M.A., Mulcahy G., O'Farrelly C.
    Immunogenetics 56:170-177(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity."
    Xiao Y., Cai Y., Bommineni Y.R., Fernando S.C., Prakash O., Gilliland S.E., Zhang G.
    J. Biol. Chem. 281:2858-2867(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
  3. "Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway."
    Goitsuka R., Chen C.-I.H., Benyon L., Asano Y., Kitamura D., Cooper M.D.
    Proc. Natl. Acad. Sci. U.S.A. 104:15063-15068(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Tissue: Bursa of Fabricius.
  4. "Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken."
    Xiao Y., Dai H., Bommineni Y.R., Soulages J.L., Gong Y.X., Prakash O., Zhang G.
    FEBS J. 273:2581-2593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 123-148, FUNCTION.

Entry informationi

Entry nameiCTHL1_CHICK
AccessioniPrimary (citable) accession number: Q6QLQ5
Secondary accession number(s): Q2IAM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.