ID CELA1_HUMAN Reviewed; 258 AA. AC Q9UNI1; Q5MLF0; Q6DJT0; Q6ISM6; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 24-JAN-2024, entry version 171. DE RecName: Full=Chymotrypsin-like elastase family member 1; DE EC=3.4.21.36; DE AltName: Full=Elastase-1; DE AltName: Full=Pancreatic elastase 1; DE Flags: Precursor; GN Name=CELA1; Synonyms=ELA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Keratinocyte; RX PubMed=10620133; DOI=10.1046/j.1523-1747.2000.00825.x; RA Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.; RT "Human elastase 1: evidence for expression in the skin and the RT identification of a frequent frameshift polymorphism."; RL J. Invest. Dermatol. 114:165-170(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-194. RG NIEHS SNPs program; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP VARIANT [LARGE SCALE ANALYSIS] ALA-76. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Serine proteases that hydrolyze many proteins in addition to CC elastin. {ECO:0000250|UniProtKB:Q91X79}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins, including elastin. Preferential CC cleavage: Ala-|-Xaa.; EC=3.4.21.36; CC Evidence={ECO:0000250|UniProtKB:Q91X79}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:P00772}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00772}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00772}. CC -!- TISSUE SPECIFICITY: Basal layers of epidermis (at protein level). Not CC expressed in the pancreas. {ECO:0000269|PubMed:10620133}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: In spite of its original name 'Pancreatic elastase 1', CELA1 CC is not detected in the pancreas. Elastase activity described in the CC pancreas may be in fact due to CELA2A (PubMed:10620133). CC {ECO:0000305|PubMed:10620133}. CC -!- SEQUENCE CAUTION: CC Sequence=AAV88109.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ela1/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Elastase entry; CC URL="https://en.wikipedia.org/wiki/Elastase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF120493; AAD28441.1; -; mRNA. DR EMBL; AC046135; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069454; AAH69454.1; -; mRNA. DR EMBL; BC075091; AAH75091.2; -; mRNA. DR EMBL; AY740424; AAV88109.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS8812.1; -. DR RefSeq; NP_001962.3; NM_001971.5. DR AlphaFoldDB; Q9UNI1; -. DR SMR; Q9UNI1; -. DR BioGRID; 108305; 26. DR IntAct; Q9UNI1; 16. DR STRING; 9606.ENSP00000293636; -. DR BindingDB; Q9UNI1; -. DR ChEMBL; CHEMBL3000; -. DR DrugBank; DB07955; (2-BROMOETHYL)(2-'FORMYL-4'-AMINOPHENYL) ACETATE. DR DrugBank; DB08007; (2R)-3-{[(BENZYLAMINO)CARBONYL]AMINO}-2-HYDROXYPROPANOIC ACID. DR DrugBank; DB08640; (2S,3S)-3-FORMYL-2-({[(4-METHYLPHENYL)SULFONYL]AMINO}METHYL)PENTANOIC ACID. DR DrugBank; DB08641; (2S,3S)-3-FORMYL-2-({[(4-NITROPHENYL)SULFONYL]AMINO}METHYL)PENTANOIC ACID. DR DrugBank; DB06951; (3R)-3-ethyl-N-[(4-methylphenyl)sulfonyl]-L-aspartic acid. DR DrugBank; DB07433; (TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO ETHYL-FORMAMIDE. DR DrugBank; DB03202; 2-[5-Methanesulfonylamino-2-(4-Aminophenyl)-6-Oxo-1,6-Dihydro-1-Pyrimidinyl]-N-(3,3,3-Trifluoro-1-Isopropyl-2-Oxopropyl)Acetamide. DR DrugBank; DB08614; 3-[[(METHYLAMINO)SULFONYL]AMINO]-2-OXO-6-PHENYL-N-[3,3,3-TRIFLUORO-1-(1-METHYLETHYL)-2-OXOPHENYL]-1(2H)-PYRIDINE ACETAMIDE. DR DrugBank; DB07956; [1-(3-CHLORO-2-FORMYL-PHENYLCARBAMOYL)-2-METHYL-PROPYL]-CARBAMIC ACID TERT-BUTYL ESTER. DR DrugBank; DB02114; Cumidine. DR DrugBank; DB03925; Freselestat. DR DrugBank; DB02341; Mdl 101,146. DR DrugBank; DB07957; METHYL(2-ACETOXY-2-(2-CARBOXY-4-AMINO-PHENYL))ACETATE. DR DrugBank; DB01844; N,N-dimethylformamide. DR DrugBank; DB03890; N-[2-(1-Formyl-2-Methyl-Propyl)-1-(4-Piperidin-1-Yl-but-2-Enoyl)-Pyrrolidin-3-Yl]-Methanesulfonamide. DR DrugBank; DB03702; N-{4-[(Carboxymethyl)carbamoyl]benzoyl}-L-valyl-N-[(3S)-1,1,1-trifluoro-4-methyl-2-oxo-3-pentanyl]-L-prolinamide. DR DrugBank; DB03757; N-{[(2-Methyl-2-propanyl)oxy]carbonyl}-L-alanyl-L-alaninamide. DR DrugCentral; Q9UNI1; -. DR GuidetoPHARMACOLOGY; 2338; -. DR MEROPS; S01.153; -. DR GlyCosmos; Q9UNI1; 2 sites, No reported glycans. DR GlyGen; Q9UNI1; 2 sites. DR PhosphoSitePlus; Q9UNI1; -. DR BioMuta; CELA1; -. DR DMDM; 62298049; -. DR MassIVE; Q9UNI1; -. DR PaxDb; 9606-ENSP00000293636; -. DR PeptideAtlas; Q9UNI1; -. DR ProteomicsDB; 85297; -. DR Antibodypedia; 14377; 168 antibodies from 22 providers. DR DNASU; 1990; -. DR Ensembl; ENST00000293636.2; ENSP00000293636.1; ENSG00000139610.2. DR GeneID; 1990; -. DR KEGG; hsa:1990; -. DR MANE-Select; ENST00000293636.2; ENSP00000293636.1; NM_001971.6; NP_001962.3. DR UCSC; uc001ryi.1; human. DR AGR; HGNC:3308; -. DR CTD; 1990; -. DR DisGeNET; 1990; -. DR GeneCards; CELA1; -. DR HGNC; HGNC:3308; CELA1. DR HPA; ENSG00000139610; Group enriched (adrenal gland, pancreas). DR MIM; 130120; gene. DR neXtProt; NX_Q9UNI1; -. DR OpenTargets; ENSG00000139610; -. DR PharmGKB; PA27734; -. DR VEuPathDB; HostDB:ENSG00000139610; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01030000234528; -. DR HOGENOM; CLU_006842_0_4_1; -. DR InParanoid; Q9UNI1; -. DR OMA; KQGCNVS; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q9UNI1; -. DR TreeFam; TF330455; -. DR BRENDA; 3.4.21.36; 2681. DR PathwayCommons; Q9UNI1; -. DR SignaLink; Q9UNI1; -. DR BioGRID-ORCS; 1990; 35 hits in 1150 CRISPR screens. DR ChiTaRS; CELA1; human. DR GeneWiki; CELA1; -. DR GenomeRNAi; 1990; -. DR Pharos; Q9UNI1; Tchem. DR PRO; PR:Q9UNI1; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9UNI1; Protein. DR Bgee; ENSG00000139610; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 28 other cell types or tissues. 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; ISS:UniProtKB. DR GO; GO:0060309; P:elastin catabolic process; IEA:Ensembl. DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0061113; P:pancreas morphogenesis; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0045595; P:regulation of cell differentiation; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0048771; P:tissue remodeling; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24257; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER; 1. DR PANTHER; PTHR24257:SF0; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; Q9UNI1; HS. 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..8 FT /evidence="ECO:0000250|UniProtKB:P00772" FT PROPEP 9..18 FT /note="Activation peptide" FT /evidence="ECO:0000250|UniProtKB:P00772" FT /id="PRO_0000027677" FT CHAIN 19..258 FT /note="Chymotrypsin-like elastase family member 1" FT /id="PRO_0000027678" FT DOMAIN 19..256 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 63 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00772" FT ACT_SITE 111 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00772" FT ACT_SITE 206 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00772" FT BINDING 77 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00772" FT BINDING 79 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00772" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00772" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00772" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 48..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 145..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 176..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 202..232 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT VARIANT 10 FT /note="Q -> H (in dbSNP:rs17860287)" FT /id="VAR_033645" FT VARIANT 44 FT /note="R -> W (in dbSNP:rs17860299)" FT /id="VAR_033646" FT VARIANT 59 FT /note="M -> V (in dbSNP:rs17860300)" FT /id="VAR_033647" FT VARIANT 76 FT /note="G -> A (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036295" FT VARIANT 243 FT /note="Q -> R (in dbSNP:rs17860364)" FT /id="VAR_033648" FT CONFLICT 220 FT /note="V -> L (in Ref. 1; AAD28441)" FT /evidence="ECO:0000305" SQ SEQUENCE 258 AA; 27798 MW; 684EDE8F1F011F8D CRC64; MLVLYGHSTQ DLPETNARVV GGTEAGRNSW PSQISLQYRS GGSRYHTCGG TLIRQNWVMT AAHCVDYQKT FRVVAGDHNL SQNDGTEQYV SVQKIVVHPY WNSDNVAAGY DIALLRLAQS VTLNSYVQLG VLPQEGAILA NNSPCYITGW GKTKTNGQLA QTLQQAYLPS VDYAICSSSS YWGSTVKNTM VCAGGDGVRS GCQGDSGGPL HCLVNGKYSV HGVTSFVSSR GCNVSRKPTV FTQVSAYISW INNVIASN //