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GLL2_CHICK
ID   GLL2_CHICK              Reviewed;          64 AA.
AC   P46158; Q09MT0; Q0PWH3; Q6B9W8; Q6GXJ3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Gallinacin-2;
DE            Short=Gal-2;
DE   AltName: Full=Beta-defensin 2;
DE   Flags: Precursor;
GN   Name=GAL2;
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=Bone marrow;
RX   PubMed=9745666; DOI=10.1046/j.1365-2052.1998.00338.x;
RA   Brockus C.W., Harmon B.G., Jackwood M.W.;
RT   "Characterization of beta-defensin prepropeptide mRNA from chicken and
RT   turkey bone marrow.";
RL   Anim. Genet. 29:283-289(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ALA-17.
RX   PubMed=15310403; DOI=10.1186/1471-2164-5-56;
RA   Xiao Y., Hughes A.L., Ando J., Matsuda Y., Cheng J.-F., Skinner-Noble D.,
RA   Zhang G.;
RT   "A genome-wide screen identifies a single beta-defensin gene cluster in the
RT   chicken: implications for the origin and evolution of mammalian
RT   defensins.";
RL   BMC Genomics 5:56-56(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang H., Bi Y., Cao Y., Chen X.;
RT   "Chicken defensin gene structure.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-17 AND ARG-20.
RC   STRAIN=Guangxi Huang, Huiyang bearded, Qingyuan Ma, Taihe silkies, and
RC   Xinghua;
RA   Chen Y., Cao Y., Xie Q., Bi Y., Chen J.;
RT   "Chicken beta-defensin in China chicken breeds.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 29-64, FUNCTION, AND MASS SPECTROMETRY.
RC   STRAIN=Broiler; 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   [6]
RP   PROTEIN SEQUENCE OF 29-43, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   STRAIN=Broiler; TISSUE=Bone marrow, and Granulocyte;
RX   PubMed=19151352; DOI=10.3382/ps.2008-00366;
RA   Kannan L., Rath N.C., Liyanage R., Lay J.O. Jr.;
RT   "Direct screening identifies mature beta-defensin 2 in avian heterophils.";
RL   Poult. Sci. 88:372-379(2009).
RN   [7]
RP   TISSUE SPECIFICITY.
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   [8]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=16394622; DOI=10.1262/jrd.17070;
RA   Yoshimura Y., Ohashi H., Subedi K., Nishibori M., Isobe N.;
RT   "Effects of age, egg-laying activity, and Salmonella-inoculation on the
RT   expressions of gallinacin mRNA in the vagina of the hen oviduct.";
RL   J. Reprod. Dev. 52:211-218(2006).
RN   [9]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=17244739; DOI=10.1530/rep-06-0083;
RA   Subedi K., Isobe N., Nishibori M., Yoshimura Y.;
RT   "Changes in the expression of gallinacins, antimicrobial peptides, in
RT   ovarian follicles during follicular growth and in response to
RT   lipopolysaccharide in laying hens (Gallus domesticus).";
RL   Reproduction 133:127-133(2007).
RN   [10]
RP   STRUCTURE BY NMR OF 29-64, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-59.
RX   PubMed=22205704; DOI=10.1074/jbc.m111.312108;
RA   Derache C., Meudal H., Aucagne V., Mark K.J., Cadene M., Delmas A.F.,
RA   Lalmanach A.C., Landon C.;
RT   "Initial insights into structure-activity relationships of avian
RT   defensins.";
RL   J. Biol. Chem. 287:7746-7755(2012).
CC   -!- FUNCTION: Potent antibacterial activity against the Gram-negative
CC       bacterium E.coli ML-35, and against the Gram-positive bacterium
CC       L.monocytogenes EGD. Lacks antifungal activity against C.albicans.
CC       {ECO:0000269|PubMed:8150085}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule.
CC   -!- TISSUE SPECIFICITY: Expressed in circulating heterophil granulocytes
CC       and bone marrow (at protein level). Strong expression in the bone
CC       marrow, lung and testis. Moderate expression in the bursa and
CC       intestine. Low expression in the cloaca, gall bladder, brain, pancreas,
CC       trachea, air sacs and spleen. Expressed in the vagina, ovarian stroma
CC       and the theca layer of the ovarian follicle, but not in the granulosa
CC       layer of the ovarian follicle. {ECO:0000269|PubMed:15148642,
CC       ECO:0000269|PubMed:16394622, ECO:0000269|PubMed:17244739,
CC       ECO:0000269|PubMed:19151352}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the theca layer of the ovarian
CC       follicle in the white follicle (WF), F1, F3, F5, and postovulatory
CC       follicle stages. In the vagina expression is higher in laying hens than
CC       in non-laying hens, and is higher in older laying hens than in young
CC       laying hens. {ECO:0000269|PubMed:16394622,
CC       ECO:0000269|PubMed:17244739}.
CC   -!- INDUCTION: Not induced in the ovarian follicle by intravenous injection
CC       of LPS. Expression in cultured vaginal cells is increased by LPS and
CC       S.enteritidis. {ECO:0000269|PubMed:16394622,
CC       ECO:0000269|PubMed:17244739}.
CC   -!- MASS SPECTROMETRY: Mass=3916.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8150085};
CC   -!- MASS SPECTROMETRY: Mass=3916.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19151352};
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; AF033336; AAC36052.1; -; mRNA.
DR   EMBL; AY621317; AAT48926.1; -; Genomic_DNA.
DR   EMBL; AY672652; AAT76973.1; -; Genomic_DNA.
DR   EMBL; DQ677633; ABG73367.1; -; mRNA.
DR   EMBL; DQ858299; ABI48215.1; -; mRNA.
DR   EMBL; DQ858312; ABI48228.1; -; mRNA.
DR   EMBL; DQ858325; ABI48241.1; -; mRNA.
DR   EMBL; DQ858339; ABI48255.1; -; mRNA.
DR   PIR; S43284; S43284.
DR   RefSeq; NP_001188328.1; NM_001201399.1.
DR   RefSeq; NP_990323.2; NM_204992.2.
DR   RefSeq; XP_015140577.1; XM_015285091.1.
DR   PDB; 2LG5; NMR; -; A=29-64.
DR   PDB; 2LG6; NMR; -; A=29-64.
DR   PDBsum; 2LG5; -.
DR   PDBsum; 2LG6; -.
DR   AlphaFoldDB; P46158; -.
DR   BMRB; P46158; -.
DR   SMR; P46158; -.
DR   STRING; 9031.ENSGALP00000030904; -.
DR   PaxDb; P46158; -.
DR   GeneID; 395840; -.
DR   KEGG; gga:395840; -.
DR   CTD; 1673; -.
DR   VEuPathDB; HostDB:geneid_395840; -.
DR   eggNOG; ENOG502TD1D; Eukaryota.
DR   HOGENOM; CLU_189296_5_1_1; -.
DR   InParanoid; P46158; -.
DR   OrthoDB; 1618537at2759; -.
DR   PRO; PR:P46158; -.
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   InterPro; IPR001855; Defensin_beta-typ.
DR   Pfam; PF00711; Defensin_beta; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Defensin;
KW   Direct protein sequencing; Disulfide bond; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..28
FT                   /evidence="ECO:0000269|PubMed:19151352,
FT                   ECO:0000269|PubMed:8150085"
FT                   /id="PRO_0000007012"
FT   PEPTIDE         29..64
FT                   /note="Gallinacin-2"
FT                   /id="PRO_0000007013"
FT   DISULFID        31..57
FT                   /evidence="ECO:0000269|PubMed:22205704"
FT   DISULFID        36..51
FT                   /evidence="ECO:0000269|PubMed:22205704"
FT   DISULFID        41..58
FT                   /evidence="ECO:0000269|PubMed:22205704"
FT   VARIANT         17
FT                   /note="V -> A (in strain: Xinghua)"
FT                   /evidence="ECO:0000269|PubMed:15310403, ECO:0000269|Ref.4"
FT   VARIANT         20
FT                   /note="G -> R (in strain: Xinghua)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   MUTAGEN         59
FT                   /note="K->A: Dramatic decrease in antimicrobial activity."
FT                   /evidence="ECO:0000269|PubMed:22205704"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:2LG5"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:2LG5"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:2LG5"
FT   STRAND          46..50
FT                   /evidence="ECO:0007829|PDB:2LG5"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:2LG5"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:2LG6"
SQ   SEQUENCE   64 AA;  7142 MW;  73E147EE4FCD39E0 CRC64;
     MRILYLLFSL LFLALQVSPG LSSPRRDMLF CKGGSCHFGG CPSHLIKVGS CFGFRSCCKW
     PWNA
 
 
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