CEL2A_MOUSE
ID CEL2A_MOUSE Reviewed; 271 AA.
AC P05208;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Chymotrypsin-like elastase family member 2A {ECO:0000305};
DE EC=3.4.21.71;
DE AltName: Full=Elastase-2;
DE AltName: Full=Elastase-2A;
DE Flags: Precursor;
GN Name=Cela2a {ECO:0000312|MGI:MGI:95316}; Synonyms=Ela-2, Ela2, Ela2a;
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 [GENOMIC DNA / MRNA].
RX PubMed=3641189; DOI=10.1093/nar/14.21.8307;
RA Stevenson B.J., Hagenbuechle O., Wellauer P.K.;
RT "Sequence organisation and transcriptional regulation of the mouse elastase
RT II and trypsin genes.";
RL Nucleic Acids Res. 14:8307-8330(1986).
RN [2]
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 [3]
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).
RN [4]
RP TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=31358993; DOI=10.1038/s41588-019-0470-3;
RA Esteghamat F., Broughton J.S., Smith E., Cardone R., Tyagi T., Guerra M.,
RA Szabo A., Ugwu N., Mani M.V., Azari B., Kayingo G., Chung S., Fathzadeh M.,
RA Weiss E., Bender J., Mane S., Lifton R.P., Adeniran A., Nathanson M.H.,
RA Gorelick F.S., Hwa J., Sahin-Toth M., Belfort-DeAguiar R., Kibbey R.G.,
RA Mani A.;
RT "CELA2A mutations predispose to early-onset atherosclerosis and metabolic
RT syndrome and affect plasma insulin and platelet activation.";
RL Nat. Genet. 51:1233-1243(2019).
CC -!- FUNCTION: Elastase that enhances insulin signaling and might have a
CC physiologic role in cellular glucose metabolism. Circulates in plasma
CC and reduces platelet hyperactivation, triggers both insulin secretion
CC and degradation, and increases insulin sensitivity.
CC {ECO:0000269|PubMed:31358993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa.
CC Hydrolyzes elastin.; EC=3.4.21.71;
CC Evidence={ECO:0000305|PubMed:31358993};
CC -!- SUBUNIT: Interacts with CPA1. Interacts with SERPINA1.
CC {ECO:0000250|UniProtKB:P08217}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31358993}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas (at mRNA and protein
CC levels). Also expressed in adrenal gland and small intestine.
CC {ECO:0000269|PubMed:31358993}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; X04573; CAA28242.1; -; mRNA.
DR EMBL; X04576; CAA28244.1; -; Genomic_DNA.
DR EMBL; BC026552; AAH26552.1; -; mRNA.
DR CCDS; CCDS18884.1; -.
DR PIR; A25528; A25528.
DR RefSeq; NP_031945.1; NM_007919.3.
DR AlphaFoldDB; P05208; -.
DR SMR; P05208; -.
DR STRING; 10090.ENSMUSP00000099539; -.
DR MEROPS; S01.155; -.
DR PhosphoSitePlus; P05208; -.
DR jPOST; P05208; -.
DR MaxQB; P05208; -.
DR PaxDb; P05208; -.
DR PeptideAtlas; P05208; -.
DR PRIDE; P05208; -.
DR ProteomicsDB; 281571; -.
DR DNASU; 13706; -.
DR Ensembl; ENSMUST00000102481; ENSMUSP00000099539; ENSMUSG00000058579.
DR GeneID; 13706; -.
DR KEGG; mmu:13706; -.
DR UCSC; uc008vpj.1; mouse.
DR CTD; 63036; -.
DR MGI; MGI:95316; Cela2a.
DR VEuPathDB; HostDB:ENSMUSG00000058579; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P05208; -.
DR OMA; NRWFLTA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P05208; -.
DR TreeFam; TF330455; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 13706; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cela2a; mouse.
DR PRO; PR:P05208; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P05208; protein.
DR Bgee; ENSMUSG00000058579; Expressed in pyloric antrum and 43 other tissues.
DR Genevisible; P05208; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0036457; C:keratohyalin granule; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0017171; F:serine hydrolase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:1901143; P:insulin catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
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 Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT PROPEP 17..30
FT /note="Activation peptide"
FT /id="PRO_0000027687"
FT CHAIN 31..271
FT /note="Chymotrypsin-like elastase family member 2A"
FT /id="PRO_0000027688"
FT DOMAIN 31..269
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 60..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 157..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 271 AA; 28914 MW; FA542AE38FED3B4B CRC64;
MIRTLLLSAL VAGALSCGYP TYEVEDDVSR VVGGQEATPN TWPWQVSLQV LSSGRWRHNC
GGSLVANNWV LTAAHCLSNY QTYRVLLGAH SLSNPGAGSA AVQVSKLVVH QRWNSQNVGN
GYDIALIKLA SPVTLSKNIQ TACLPPAGTI LPRNYVCYVT GWGLLQTNGN SPDTLRQGRL
LVVDYATCSS ASWWGSSVKS SMVCAGGDGV TSSCNGDSGG PLNCRASNGQ WQVHGIVSFG
SSLGCNYPRK PSVFTRVSNY IDWINSVMAR N
