GLL1A_CHICK
ID GLL1A_CHICK Reviewed; 65 AA.
AC P46157; P80390; Q09MR8; Q9DG59;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Gallinacin-1 alpha;
DE Short=Gal-1 alpha;
DE AltName: Full=Antimicrobial peptide CHP2;
DE AltName: Full=Chicken heterophil peptide 2;
DE Flags: Precursor;
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].
RC TISSUE=Trachea;
RX PubMed=11254635; DOI=10.1128/iai.69.4.2684-2691.2001;
RA Zhao C., Nguyen T., Liu L., Sacco R.E., Brogden K.A., Lehrer R.I.;
RT "Gallinacin-3, an inducible epithelial beta-defensin in the chicken.";
RL Infect. Immun. 69:2684-2691(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Guangxi Huang, and Qingyuan Ma;
RA Cao Y., Chen Y., Bi Y., Xie Q., Chen J.;
RT "Chicken beta-defensin in China chicken breeds.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 26-64.
RC STRAIN=Cross Broiler-6; TISSUE=Leukocyte;
RX PubMed=8150085; DOI=10.1016/0014-5793(94)80517-2;
RA Harwig S.S.L., Swiderek K.M., Kokryakov V.N., Tan L., Lee T.D.,
RA Panyutich E.A., Aleshina G.M., Shamova O.V., Lehrer R.I.;
RT "Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes.";
RL FEBS Lett. 342:281-285(1994).
RN [4]
RP PROTEIN SEQUENCE OF 26-59.
RX PubMed=7964174; DOI=10.1002/jlb.56.5.661;
RA Evans E.W., Beach G.G., Wunderlich J., Harmon B.G.;
RT "Isolation of antimicrobial peptides from avian heterophils.";
RL J. Leukoc. Biol. 56:661-665(1994).
CC -!- FUNCTION: Has bactericidal activity. Potent activity against E.coli ML-
CC 35, L.monocytogenes EGD and C.albicans.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AF181951; AAG09211.1; -; mRNA.
DR EMBL; DQ858337; ABI48253.1; -; mRNA.
DR EMBL; DQ858297; ABI48213.1; -; mRNA.
DR PIR; S43282; S43282.
DR AlphaFoldDB; P46157; -.
DR SMR; P46157; -.
DR TCDB; 1.C.85.3.1; the pore-forming Beta-defensin (Beta-defensin) family.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; TAS:AgBase.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; TAS:AgBase.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR001855; Defensin_beta-typ.
DR Pfam; PF00711; Defensin_beta; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW Disulfide bond; Fungicide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..25
FT /evidence="ECO:0000269|PubMed:7964174,
FT ECO:0000269|PubMed:8150085"
FT /id="PRO_0000007010"
FT PEPTIDE 26..65
FT /note="Gallinacin-1 alpha"
FT /id="PRO_0000007011"
FT DISULFID 31..59
FT /evidence="ECO:0000250"
FT DISULFID 38..53
FT /evidence="ECO:0000250"
FT DISULFID 43..60
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="K -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 65 AA; 7286 MW; BC835B79574F2ECE CRC64;
MRIVYLLLPF ILLLAQGAAG SSQALGRKSD CFRKNGFCAF LKCPYLTLIS GKCSRFHLCC
KRIWG
