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Elastase 2, neutrophil (Predicted) (Elastase, neutrophil-expressed)

 D4A488_RAT              Unreviewed;       271 AA.
D4A488;
20-APR-2010, integrated into UniProtKB/TrEMBL.
20-APR-2010, sequence version 1.
23-MAY-2018, entry version 76.
SubName: Full=Elastase 2, neutrophil (Predicted) {ECO:0000313|EMBL:EDL89378.1};
SubName: Full=Elastase, neutrophil-expressed {ECO:0000313|Ensembl:ENSRNOP00000014981};
Name=Elane {ECO:0000313|Ensembl:ENSRNOP00000014981,
ECO:0000313|RGD:1307968};
Synonyms=Ela2_predicted {ECO:0000313|EMBL:EDL89378.1};
ORFNames=rCG_29176 {ECO:0000313|EMBL:EDL89378.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000014981, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000014981, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014981,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDL89378.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL89378.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDL89378.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL89378.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000014981}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014981};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000256|SAAS:SAAS00559343}.
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EMBL; AABR07055844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474029; EDL89378.1; -; Genomic_DNA.
RefSeq; NP_001100237.1; NM_001106767.1.
UniGene; Rn.90573; -.
STRING; 10116.ENSRNOP00000014981; -.
MEROPS; S01.131; -.
PeptideAtlas; D4A488; -.
PRIDE; D4A488; -.
Ensembl; ENSRNOT00000014981; ENSRNOP00000014981; ENSRNOG00000033685.
GeneID; 299606; -.
KEGG; rno:299606; -.
UCSC; RGD:1307968; rat.
CTD; 1991; -.
RGD; 1307968; Elane.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00910000144219; -.
KO; K01327; -.
OMA; NWINSII; -.
OrthoDB; EOG091G0DF7; -.
TreeFam; TF335284; -.
Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6803157; Antimicrobial peptides.
Reactome; R-RNO-977606; Regulation of Complement cascade.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000033685; -.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0019955; F:cytokine binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IBA:GO_Central.
GO; GO:0002812; P:biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IEA:Ensembl.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
GO; GO:0045079; P:negative regulation of chemokine biosynthetic process; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; IEA:Ensembl.
GO; GO:0070947; P:neutrophil mediated killing of fungus; IEA:Ensembl.
GO; GO:0070945; P:neutrophil mediated killing of gram-negative bacterium; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
GO; GO:0050778; P:positive regulation of immune response; IEA:Ensembl.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IEA:Ensembl.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IEA:Ensembl.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
Hydrolase {ECO:0000256|RuleBase:RU363034};
Protease {ECO:0000256|RuleBase:RU363034};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Serine protease {ECO:0000256|RuleBase:RU363034};
Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 30 {ECO:0000256|SAM:SignalP}.
CHAIN 31 271 {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5014087825.
DOMAIN 33 251 Peptidase S1.
{ECO:0000259|PROSITE:PS50240}.
SEQUENCE 271 AA; 29557 MW; F560D40D7118F1E3 CRC64;
MQPTMALHRP SNQTLASMLL ALLLVCPALA SEIVGGRPAQ PHAWPFMVSL QRRGGHFCGA
TLIARNFVMS AAHCVNGRNF QSVQVVLGAH DLRRREPTRQ IFSVQRIFEN GFDPSRLLND
IVIIQLNGSA TINANVQVAE LPAQGQGVGN RTPCVAMGWG RLGTNRPLPS VLQELNVTVV
TNLCRRRVNV CTLVPRRQAG ICFGDSGGPL VCNNLVQGID SFIRGGCGSG FYPDAFAPVA
EFADWINSII RSHDDRPLTN PKDREREGRT N


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