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Chymotrypsin-like elastase family member 1 (EC 3.4.21.36) (Elastase-1)

 CELA1_MOUSE             Reviewed;         266 AA.
Q91X79; Q9D936; Q9Z1H1;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 119.
RecName: Full=Chymotrypsin-like elastase family member 1;
EC=3.4.21.36;
AltName: Full=Elastase-1;
Flags: Precursor;
Name=Cela1; Synonyms=Ela1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3493908; DOI=10.1002/eji.1830170215;
Yamasaki N., Sugimura K., Hiida M., Naito T., Watanabe T.;
"Sequence analysis of a cDNA clone of a gene encoding a component of a
putative phosphorylcholine-specific T suppressor factor and functional
property of its gene product.";
Eur. J. Immunol. 17:247-253(1987).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts upon elastin. {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of proteins, including elastin. Preferential
cleavage: Ala-|-Xaa.; EC=3.4.21.36;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; AK007392; BAB25008.1; -; mRNA.
EMBL; AC123724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466550; EDL04074.1; -; Genomic_DNA.
EMBL; BC011218; AAH11218.1; -; mRNA.
EMBL; M27347; AAA39901.1; -; mRNA.
CCDS; CCDS37213.1; -.
RefSeq; NP_291090.2; NM_033612.2.
UniGene; Mm.2131; -.
ProteinModelPortal; Q91X79; -.
SMR; Q91X79; -.
BioGrid; 225137; 1.
STRING; 10090.ENSMUSP00000023775; -.
MEROPS; S01.153; -.
MaxQB; Q91X79; -.
PaxDb; Q91X79; -.
PeptideAtlas; Q91X79; -.
PRIDE; Q91X79; -.
Ensembl; ENSMUST00000023775; ENSMUSP00000023775; ENSMUSG00000023031.
GeneID; 109901; -.
KEGG; mmu:109901; -.
UCSC; uc007xrx.2; mouse.
CTD; 1990; -.
MGI; MGI:95314; Cela1.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00940000155254; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q91X79; -.
KO; K01326; -.
OMA; LYGHSTQ; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q91X79; -.
TreeFam; TF330455; -.
ChiTaRS; Cela1; mouse.
PRO; PR:Q91X79; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023031; Expressed in 162 organ(s), highest expression level in pancreas.
Genevisible; Q91X79; MM.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0055123; P:digestive system development; IMP:MGI.
GO; GO:0060309; P:elastin catabolic process; IMP:MGI.
GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0061113; P:pancreas morphogenesis; IMP:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0048771; P:tissue remodeling; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
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.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Metal-binding; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 26 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000416103.
CHAIN 27 266 Chymotrypsin-like elastase family member
1.
/FTId=PRO_0000416104.
DOMAIN 27 264 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 71 71 Charge relay system. {ECO:0000250}.
ACT_SITE 119 119 Charge relay system. {ECO:0000250}.
ACT_SITE 214 214 Charge relay system. {ECO:0000250}.
METAL 85 85 Calcium. {ECO:0000250}.
METAL 90 90 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 95 95 Calcium. {ECO:0000250}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 72 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 153 220 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 184 200 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 210 240 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 12 12 L -> P (in Ref. 1; BAB25008).
{ECO:0000305}.
CONFLICT 27 27 V -> M (in Ref. 1; BAB25008).
{ECO:0000305}.
CONFLICT 31 33 AEA -> EFP (in Ref. 5; AAA39901).
{ECO:0000305}.
CONFLICT 123 123 L -> V (in Ref. 5; AAA39901).
{ECO:0000305}.
CONFLICT 194 194 V -> L (in Ref. 5; AAA39901).
{ECO:0000305}.
CONFLICT 202 202 G -> C (in Ref. 5; AAA39901).
{ECO:0000305}.
CONFLICT 229 229 H -> D (in Ref. 5; AAA39901).
{ECO:0000305}.
CONFLICT 252 252 V -> L (in Ref. 5; AAA39901).
{ECO:0000305}.
SEQUENCE 266 AA; 28901 MW; 27C50812E8804F5B CRC64;
MLRFLVFASL VLCGHSTEDV PETDARVVGG AEARRNSWPS QISLQYQYGG SWHHTCGGTL
IRSNWVMTAA HCVDSPMTYR VVVGEHNLSQ NDGTEQYVNV QKIVSHPYWN KNNVVAGYDI
ALLRLAKSVT LNNYVQLGVL PREGTILANN SPCYITGWGR TRTNGELAQT LQQAYLPSVS
YSICSSSSYW GSSVKNTMVC AGGDGVRSGC QGDSGGPLHC MVNGQYAVHG VTSFVSSMGC
NVARKPTVFT RVSAYISWMN NVIASN


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