CELA1_MOUSE
ID CELA1_MOUSE Reviewed; 266 AA.
AC Q91X79; Q9D936; Q9Z1H1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chymotrypsin-like elastase family member 1;
DE EC=3.4.21.36;
DE AltName: Full=Elastase-1;
DE Flags: Precursor;
GN Name=Cela1; Synonyms=Ela1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3493908; DOI=10.1002/eji.1830170215;
RA Yamasaki N., Sugimura K., Hiida M., Naito T., Watanabe T.;
RT "Sequence analysis of a cDNA clone of a gene encoding a component of a
RT putative phosphorylcholine-specific T suppressor factor and functional
RT property of its gene product.";
RL Eur. J. Immunol. 17:247-253(1987).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts upon elastin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including elastin. Preferential
CC cleavage: Ala-|-Xaa.; EC=3.4.21.36;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AK007392; BAB25008.1; -; mRNA.
DR EMBL; AC123724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04074.1; -; Genomic_DNA.
DR EMBL; BC011218; AAH11218.1; -; mRNA.
DR EMBL; M27347; AAA39901.1; -; mRNA.
DR CCDS; CCDS37213.1; -.
DR RefSeq; NP_291090.2; NM_033612.2.
DR AlphaFoldDB; Q91X79; -.
DR SMR; Q91X79; -.
DR BioGRID; 225137; 1.
DR STRING; 10090.ENSMUSP00000023775; -.
DR MEROPS; S01.153; -.
DR GlyGen; Q91X79; 1 site.
DR PhosphoSitePlus; Q91X79; -.
DR MaxQB; Q91X79; -.
DR PaxDb; Q91X79; -.
DR PeptideAtlas; Q91X79; -.
DR PRIDE; Q91X79; -.
DR ProteomicsDB; 279998; -.
DR Antibodypedia; 14377; 158 antibodies from 22 providers.
DR DNASU; 109901; -.
DR Ensembl; ENSMUST00000023775; ENSMUSP00000023775; ENSMUSG00000023031.
DR GeneID; 109901; -.
DR KEGG; mmu:109901; -.
DR UCSC; uc007xrx.2; mouse.
DR CTD; 1990; -.
DR MGI; MGI:95314; Cela1.
DR VEuPathDB; HostDB:ENSMUSG00000023031; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q91X79; -.
DR OMA; KQGCNVS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q91X79; -.
DR TreeFam; TF330455; -.
DR BioGRID-ORCS; 109901; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cela1; mouse.
DR PRO; PR:Q91X79; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91X79; protein.
DR Bgee; ENSMUSG00000023031; Expressed in pyloric antrum and 137 other tissues.
DR ExpressionAtlas; Q91X79; baseline and differential.
DR Genevisible; Q91X79; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0055123; P:digestive system development; IMP:MGI.
DR GO; GO:0060309; P:elastin catabolic process; IMP:MGI.
DR GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0061113; P:pancreas morphogenesis; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048771; P:tissue remodeling; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..26
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416103"
FT CHAIN 27..266
FT /note="Chymotrypsin-like elastase family member 1"
FT /id="PRO_0000416104"
FT DOMAIN 27..264
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 153..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 210..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 12
FT /note="L -> P (in Ref. 1; BAB25008)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> M (in Ref. 1; BAB25008)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..33
FT /note="AEA -> EFP (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="L -> V (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> L (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="G -> C (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="H -> D (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="V -> L (in Ref. 5; AAA39901)"
FT /evidence="ECO:0000305"
SQ 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
