DEFB4_MOUSE
ID DEFB4_MOUSE Reviewed; 63 AA.
AC P82019;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Beta-defensin 4;
DE Short=BD-4;
DE Short=mBD-4;
DE AltName: Full=Defensin, beta 4;
DE Flags: Precursor;
GN Name=Defb4; Synonyms=Bdef4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT PRO-12.
RC STRAIN=129/SvJ, C57BL/6J, and FVB/NJ; TISSUE=Lung;
RX PubMed=10922379; DOI=10.1074/jbc.m006603200;
RA Jia H.P., Wowk S.A., Schutte B.C., Lee S.K., Vivado A., Tack B.F.,
RA Bevins C.L., McCray P.B. Jr.;
RT "A novel murine beta-defensin expressed in tongue, esophagus, and
RT trachea.";
RL J. Biol. Chem. 275:33314-33320(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, AND BINDING TO CCR6.
RX PubMed=20068036; DOI=10.1074/jbc.m109.091090;
RA Roehrl J., Yang D., Oppenheim J.J., Hehlgans T.;
RT "Specific binding and chemotactic activity of mBD4 and its functional
RT orthologue hBD2 to CCR6-expressing cells.";
RL J. Biol. Chem. 285:7028-7034(2010).
CC -!- FUNCTION: Exhibits antimicrobial activity against Gram-negative
CC bacteria and Gram-positive bacteria. May act as a ligand for C-C
CC chemokine receptor CCR6. Can bind to mouse (but not human) CCR6 and
CC induce chemotactic activity of CCR6-expressing cells (PubMed:20068036).
CC {ECO:0000269|PubMed:20068036}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Tongue, esophagus and trachea.
CC {ECO:0000269|PubMed:10922379}.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AF155882; AAD38852.1; -; mRNA.
DR EMBL; AF287475; AAG02197.1; -; Genomic_DNA.
DR EMBL; AF288371; AAG10514.1; -; Genomic_DNA.
DR EMBL; AK009306; BAB26207.1; -; mRNA.
DR EMBL; AK009061; BAB26051.1; -; mRNA.
DR CCDS; CCDS40254.1; -.
DR RefSeq; NP_062702.1; NM_019728.4.
DR PDB; 6M56; NMR; -; A=34-63.
DR PDBsum; 6M56; -.
DR AlphaFoldDB; P82019; -.
DR BMRB; P82019; -.
DR SMR; P82019; -.
DR STRING; 10090.ENSMUSP00000079808; -.
DR PaxDb; P82019; -.
DR PRIDE; P82019; -.
DR DNASU; 56519; -.
DR Ensembl; ENSMUST00000081017; ENSMUSP00000079808; ENSMUSG00000059230.
DR GeneID; 56519; -.
DR KEGG; mmu:56519; -.
DR UCSC; uc009laj.2; mouse.
DR CTD; 56519; -.
DR MGI; MGI:1927667; Defb4.
DR VEuPathDB; HostDB:ENSMUSG00000059230; -.
DR eggNOG; ENOG502SYUI; Eukaryota.
DR GeneTree; ENSGT00940000160995; -.
DR HOGENOM; CLU_189296_4_1_1; -.
DR InParanoid; P82019; -.
DR OMA; HRSCHRI; -.
DR OrthoDB; 1630369at2759; -.
DR PhylomeDB; P82019; -.
DR Reactome; R-MMU-1461957; Beta defensins.
DR Reactome; R-MMU-1461973; Defensins.
DR BioGRID-ORCS; 56519; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Defb4; mouse.
DR PRO; PR:P82019; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P82019; protein.
DR Bgee; ENSMUSG00000059230; Expressed in esophagus and 18 other tissues.
DR ExpressionAtlas; P82019; baseline and differential.
DR Genevisible; P82019; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; IDA:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR InterPro; IPR001855; Defensin_beta-typ.
DR Pfam; PF00711; Defensin_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..63
FT /note="Beta-defensin 4"
FT /id="PRO_0000006930"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P46162"
FT DISULFID 31..59
FT /evidence="ECO:0000250"
FT DISULFID 38..52
FT /evidence="ECO:0000250"
FT DISULFID 42..60
FT /evidence="ECO:0000250"
FT VARIANT 12
FT /note="L -> P (in strain: FVB)"
FT /evidence="ECO:0000269|PubMed:10922379"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:6M56"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6M56"
SQ SEQUENCE 63 AA; 7129 MW; 4C7692ED589EE289 CRC64;
MRIHYLLFTF LLVLLSPLAA FTQIINNPIT CMTNGAICWG PCPTAFRQIG NCGHFKVRCC
KIR
