DFB22_MOUSE
ID DFB22_MOUSE Reviewed; 179 AA.
AC Q8BVC1;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Beta-defensin 22 {ECO:0000303|PubMed:16033865, ECO:0000312|MGI:MGI:3045368};
DE Short=Defb22 {ECO:0000303|PubMed:16033865, ECO:0000312|MGI:MGI:3045368};
DE Flags: Precursor;
GN Name=Defb22 {ECO:0000312|MGI:MGI:3045368};
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 {ECO:0000312|EMBL:AAY59769.1};
RN [1] {ECO:0000312|EMBL:AAY59769.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16033865; DOI=10.1152/physiolgenomics.00104.2005;
RA Patil A.A., Cai Y., Sang Y., Blecha F., Zhang G.;
RT "Cross-species analysis of the mammalian beta-defensin gene family:
RT presence of syntenic gene clusters and preferential expression in the male
RT reproductive tract.";
RL Physiol. Genomics 23:5-17(2005).
RN [2] {ECO:0000312|EMBL:BAC37493.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37493.1};
RC TISSUE=Epididymis {ECO:0000312|EMBL:BAC37493.1};
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:AAI39231.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI39231.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18787081; DOI=10.1530/rep-08-0164;
RA Yudin A.I., Tollner T.L., Treece C.A., Kays R., Cherr G.N.,
RA Overstreet J.W., Bevins C.L.;
RT "Beta-defensin 22 is a major component of the mouse sperm glycocalyx.";
RL Reproduction 136:753-765(2008).
CC -!- FUNCTION: Probable component of sperm glycocalyx. Likely protects and
CC facilitates transport of sperm in the female reproductive tract.
CC Probably released from the sperm surface during capacitation.
CC {ECO:0000269|PubMed:18787081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:18787081}. Secreted, extracellular space
CC {ECO:0000269|PubMed:18787081}. Note=In the corpus epididymis, located
CC in vesicles below the apical surface of the plasma membrane. Secreted
CC by epididymal cells and absorbed to the surface of sperm during transit
CC through the epididymis. Coats the entire surface of ejaculated sperm
CC although presence on the equatorial segment is less intense.
CC {ECO:0000269|PubMed:18787081}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in corpus epididymis and
CC cauda epididymis with expression in corpus being highest (at protein
CC level). Not detected in other tissues tested, including testis,
CC prostate, seminal vesicle and vas deferens (at protein level).
CC {ECO:0000269|PubMed:18787081}.
CC -!- PTM: O-glycosylated; glycans contain alpha(2,3)-linked sialic acids.
CC {ECO:0000250|UniProtKB:Q9BYW3}.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; DQ012033; AAY59769.1; -; mRNA.
DR EMBL; AK078980; BAC37493.1; -; mRNA.
DR EMBL; AL844517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139230; AAI39231.1; -; mRNA.
DR EMBL; BC145928; AAI45929.1; -; mRNA.
DR CCDS; CCDS16887.1; -.
DR RefSeq; NP_001002791.1; NM_001002791.2.
DR AlphaFoldDB; Q8BVC1; -.
DR SMR; Q8BVC1; -.
DR STRING; 10090.ENSMUSP00000028966; -.
DR PaxDb; Q8BVC1; -.
DR PRIDE; Q8BVC1; -.
DR ProteomicsDB; 279379; -.
DR DNASU; 442835; -.
DR Ensembl; ENSMUST00000028966; ENSMUSP00000028966; ENSMUSG00000027468.
DR GeneID; 442835; -.
DR KEGG; mmu:442835; -.
DR UCSC; uc008nfn.1; mouse.
DR CTD; 442835; -.
DR MGI; MGI:3045368; Defb22.
DR VEuPathDB; HostDB:ENSMUSG00000027468; -.
DR eggNOG; ENOG502TDX7; Eukaryota.
DR GeneTree; ENSGT00940000167063; -.
DR HOGENOM; CLU_1503004_0_0_1; -.
DR InParanoid; Q8BVC1; -.
DR OrthoDB; 1608276at2759; -.
DR PhylomeDB; Q8BVC1; -.
DR BioGRID-ORCS; 442835; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8BVC1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BVC1; protein.
DR Bgee; ENSMUSG00000027468; Expressed in morula and 2 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0120238; C:sperm glycocalyx; IDA:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR InterPro; IPR025933; Beta_defensin.
DR Pfam; PF13841; Defensin_beta_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..179
FT /note="Beta-defensin 22"
FT /id="PRO_5007953120"
FT REGION 105..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 27..58
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
FT DISULFID 34..52
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
FT DISULFID 38..59
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
SQ SEQUENCE 179 AA; 17709 MW; 818A7BFA06614259 CRC64;
MKSLLSTLVI IMFLAHLVTG GWYVKKCANT LGNCRKMCRD GEKQTEPATS KCPIGKLCCV
LDFKISGHCG GGGQNSDNLV TAGGDEGSSA KASTAAMVGA AAMAGTPTKT SAPAKTSAPA
KTSTTTKASN AAKASTTTKA SNAAKASAAT MAGNTTKVST AAIASTPAQA STPTKANST
