CELA1_HUMAN
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 03-AUG-2022, entry version 165.
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: Acts upon elastin.
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.
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";
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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 GlyGen; Q9UNI1; 2 sites.
DR PhosphoSitePlus; Q9UNI1; -.
DR BioMuta; CELA1; -.
DR DMDM; 62298049; -.
DR MassIVE; Q9UNI1; -.
DR PaxDb; Q9UNI1; -.
DR PeptideAtlas; Q9UNI1; -.
DR PRIDE; Q9UNI1; -.
DR ProteomicsDB; 85297; -.
DR Antibodypedia; 14377; 158 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 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; 1314811at2759; -.
DR PhylomeDB; Q9UNI1; -.
DR TreeFam; TF330455; -.
DR BRENDA; 3.4.21.36; 2681.
DR PathwayCommons; Q9UNI1; -.
DR SignaLink; Q9UNI1; -.
DR BioGRID-ORCS; 1990; 18 hits in 1072 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 left adrenal gland and 27 other tissues.
DR Genevisible; Q9UNI1; HS.
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: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; -; 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..8
FT /evidence="ECO:0000250"
FT PROPEP 9..18
FT /note="Activation peptide"
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"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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
