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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
 
 
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