DFAL1_RAT
ID DFAL1_RAT Reviewed; 87 AA.
AC Q4JEI2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Defensin alpha-like protein 1 {ECO:0000312|RGD:1561398};
DE AltName: Full=Defensin alpha-related sequence 1 {ECO:0000303|PubMed:15494476};
DE AltName: Full=Rattusin {ECO:0000303|PubMed:23380721};
DE Flags: Precursor;
GN Name=Defal1 {ECO:0000312|RGD:1561398};
GN Synonyms=Defa-rs1 {ECO:0000303|PubMed:15494476};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:AAT68755.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15494476; DOI=10.1152/physiolgenomics.00150.2004;
RA Patil A., Hughes A.L., Zhang G.;
RT "Rapid evolution and diversification of mammalian alpha-defensins as
RT revealed by comparative analysis of rodent and primate genes.";
RL Physiol. Genomics 20:1-11(2004).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000312|EMBL:EDM08974.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP SYNTHESIS OF 57-87, FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=23380721; DOI=10.1128/aac.02237-12;
RA Patil A.A., Ouellette A.J., Lu W., Zhang G.;
RT "Rattusin, an intestinal alpha-defensin-related peptide in rats with a
RT unique cysteine spacing pattern and salt-insensitive antibacterial
RT activities.";
RL Antimicrob. Agents Chemother. 57:1823-1831(2013).
RN [5] {ECO:0007744|PDB:5GWG}
RP STRUCTURE BY NMR OF 57-87, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND
RP MUTAGENESIS OF CYS-71.
RX PubMed=28345637; DOI=10.1038/srep45282;
RA Min H.J., Yun H., Ji S., Rajasekaran G., Kim J.I., Kim J.S., Shin S.Y.,
RA Lee C.W.;
RT "Rattusin structure reveals a novel defensin scaffold formed by
RT intermolecular disulfide exchanges.";
RL Sci. Rep. 7:45282-45282(2017).
CC -!- FUNCTION: Intestinal defense peptide (PubMed:23380721,
CC PubMed:28345637). Has potent antibacterial activity against Gram-
CC negative bacteria E.coli O157:H7, S.typhimurium DT104, and
CC K.pneumoniae; and against Gram-positive bacteria S.aureus, methicillin-
CC resistant S.aureus and L.monocytogenes (PubMed:23380721,
CC PubMed:28345637). Remains active in the presence of NaCl and Mg(2+)
CC (PubMed:23380721). Probably functions by disrupting bacterial membrane
CC integrity (PubMed:28345637). However, does not show cytotoxic activity
CC towards human intestinal cells (PubMed:23380721).
CC {ECO:0000269|PubMed:23380721, ECO:0000269|PubMed:28345637}.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked.
CC {ECO:0000269|PubMed:23380721, ECO:0000269|PubMed:28345637}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23380721,
CC ECO:0000305|PubMed:28345637}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in small intestine (jejunum
CC and ileum) (PubMed:15494476, PubMed:23380721). Probably expressed by
CC Paneth cells at the base of intestinal crypts (PubMed:23380721).
CC Coexpressed with MMP7 in small intestine (PubMed:23380721).
CC {ECO:0000269|PubMed:15494476, ECO:0000269|PubMed:23380721}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; AY623756; AAT68755.1; -; mRNA.
DR EMBL; AY623767; AAT68763.1; -; Genomic_DNA.
DR EMBL; AC128185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473970; EDM08974.1; -; Genomic_DNA.
DR RefSeq; NP_001028245.1; NM_001033073.1.
DR PDB; 5GWG; NMR; -; A/B=57-87.
DR PDBsum; 5GWG; -.
DR AlphaFoldDB; Q4JEI2; -.
DR BMRB; Q4JEI2; -.
DR SMR; Q4JEI2; -.
DR STRING; 10116.ENSRNOP00000047361; -.
DR PaxDb; Q4JEI2; -.
DR PRIDE; Q4JEI2; -.
DR Ensembl; ENSRNOT00000049394; ENSRNOP00000047361; ENSRNOG00000029462.
DR GeneID; 613220; -.
DR KEGG; rno:613220; -.
DR UCSC; RGD:1561398; rat.
DR CTD; 613220; -.
DR RGD; 1561398; Defal1.
DR eggNOG; ENOG502TF4X; Eukaryota.
DR GeneTree; ENSGT00940000153268; -.
DR HOGENOM; CLU_160803_1_0_1; -.
DR InParanoid; Q4JEI2; -.
DR OMA; QARIVCH; -.
DR OrthoDB; 1610714at2759; -.
DR PhylomeDB; Q4JEI2; -.
DR TreeFam; TF338414; -.
DR Reactome; R-RNO-1461973; Defensins.
DR Reactome; R-RNO-1462054; Alpha-defensins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q4JEI2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Proteomes; UP000234681; Chromosome 16.
DR Bgee; ENSRNOG00000029462; Expressed in jejunum and 12 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..56
FT /evidence="ECO:0000305|PubMed:23380721"
FT /id="PRO_0000442242"
FT PEPTIDE 57..87
FT /note="Defensin alpha-like protein 1"
FT /evidence="ECO:0000305|PubMed:23380721"
FT /id="PRO_0000442243"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 65
FT /note="Interchain (with C-77)"
FT /evidence="ECO:0000269|PubMed:28345637,
FT ECO:0007744|PDB:5GWG"
FT DISULFID 67
FT /note="Interchain (with C-75)"
FT /evidence="ECO:0000269|PubMed:28345637,
FT ECO:0007744|PDB:5GWG"
FT DISULFID 71
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:28345637,
FT ECO:0007744|PDB:5GWG"
FT DISULFID 75
FT /note="Interchain (with C-67)"
FT /evidence="ECO:0000269|PubMed:28345637,
FT ECO:0007744|PDB:5GWG"
FT DISULFID 77
FT /note="Interchain (with C-65)"
FT /evidence="ECO:0000269|PubMed:28345637,
FT ECO:0007744|PDB:5GWG"
FT MUTAGEN 71
FT /note="C->S: Aberrant protein folding and disordered
FT structure."
FT /evidence="ECO:0000269|PubMed:28345637"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5GWG"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5GWG"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5GWG"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5GWG"
SQ SEQUENCE 87 AA; 9702 MW; 60A7A9A61C1233FA CRC64;
MKTLILLSAL VLLALQVQAD PIQEAEEETK TEEQPADEDQ DVSVSFEGPE ASAVQDLRVR
RTLQCSCRRV CRNTCSCIRL SRSTYAS
