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CTHL2_CHICK
ID   CTHL2_CHICK             Reviewed;         154 AA.
AC   Q2IAL7; Q56QZ4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cathelicidin-2;
DE            Short=CATH-2;
DE   AltName: Full=Fowlicidin-2;
DE   AltName: Full=Myeloid antimicrobial peptide 27;
DE   Flags: Precursor;
GN   Name=CATHL2; Synonyms=CMAP27;
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=Bone marrow;
RX   PubMed=15963828; DOI=10.1016/j.vetimm.2005.03.003;
RA   van Dijk A., Veldhuizen E.J.A., van Asten A.J.A.M., Haagsman H.P.;
RT   "CMAP27, a novel chicken cathelicidin-like antimicrobial protein.";
RL   Vet. Immunol. Immunopathol. 106:321-327(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [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).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in trachea, lung, proventriculus,
CC       duodenum, jejunum, ileum, caeca, colon, caecal tonsil, bursa of
CC       Fabricius, kidney, ovary, testis, thymus, liver, spleen, bone marrow,
CC       skin, uropygial gland, muscle and brain. {ECO:0000269|PubMed:15963828}.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; AY817057; AAX20012.1; -; mRNA.
DR   EMBL; DQ092352; AAZ42400.1; -; mRNA.
DR   EMBL; DQ092350; AAZ65842.1; -; Genomic_DNA.
DR   RefSeq; NP_001020001.2; NM_001024830.2.
DR   AlphaFoldDB; Q2IAL7; -.
DR   SMR; Q2IAL7; -.
DR   STRING; 9031.ENSGALP00000030658; -.
DR   PaxDb; Q2IAL7; -.
DR   Ensembl; ENSGALT00000031294; ENSGALP00000030658; ENSGALG00000019696.
DR   GeneID; 420407; -.
DR   KEGG; gga:420407; -.
DR   CTD; 420407; -.
DR   VEuPathDB; HostDB:geneid_420407; -.
DR   eggNOG; ENOG502SAES; Eukaryota.
DR   GeneTree; ENSGT00390000000410; -.
DR   HOGENOM; CLU_121724_1_1_1; -.
DR   InParanoid; Q2IAL7; -.
DR   OMA; EQCPFKD; -.
DR   OrthoDB; 1534863at2759; -.
DR   PhylomeDB; Q2IAL7; -.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   Reactome; R-GGA-6803157; Antimicrobial peptides.
DR   PRO; PR:Q2IAL7; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000019696; Expressed in granulocyte and 4 other tissues.
DR   ExpressionAtlas; Q2IAL7; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IMP:AgBase.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:AgBase.
DR   GO; GO:0019835; P:cytolysis; IMP:AgBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:AgBase.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:AgBase.
DR   GO; GO:0045087; P:innate immune response; IDA:AgBase.
DR   GO; GO:0042116; P:macrophage activation; IDA:AgBase.
DR   GO; GO:0001818; P:negative 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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Immunity; Innate immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..122
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000333222"
FT   PEPTIDE         123..154
FT                   /note="Cathelicidin-2"
FT                   /id="PRO_0000333223"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15
FT                   /note="V -> L (in Ref. 1; AAX20012)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  16975 MW;  0C1D87D1F54C7226 CRC64;
     MLSCWVLLLA LLGGVCALPA PLSYPQALIQ AVDSYNQRPE VQNAFRLLSA DPEPGPGVDL
     STLRALNFTI METECTPSAR LPVDDCDFKE NGVIRDCSGP VSVLQDTPEI NLRCRDASSD
     PVLVQRGRFG RFLRKIRRFR PKVTITIQGS ARFG
 
 
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