CEL3A_HUMAN
ID CEL3A_HUMAN Reviewed; 270 AA.
AC P09093; B1AQ53; Q9BRW4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Chymotrypsin-like elastase family member 3A;
DE EC=3.4.21.70;
DE AltName: Full=Elastase IIIA;
DE AltName: Full=Elastase-3A;
DE AltName: Full=Protease E;
DE Flags: Precursor;
GN Name=CELA3A; Synonyms=ELA3, ELA3A;
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 [GENOMIC DNA], AND VARIANT GLY-241.
RC TISSUE=Pancreas;
RX PubMed=2826474; DOI=10.1016/s0021-9258(19)57291-x;
RA Tani T., Ohsumi J., Mita K., Takiguchi Y.;
RT "Identification of a novel class of elastase isozyme, human pancreatic
RT elastase III, by cDNA and genomic gene cloning.";
RL J. Biol. Chem. 263:1231-1239(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT GLY-241.
RC TISSUE=Pancreas;
RX PubMed=2460440; DOI=10.1093/oxfordjournals.jbchem.a122454;
RA Shirasu Y., Takemura K., Yoshida H., Sato Y., Iijima H., Shimada Y.,
RA Mikayama T., Ozawa T., Ikeda N., Ishida A., Tamai Y., Matsuki S.,
RA Tanaka J., Ikenaga H., Ogawa M.;
RT "Molecular cloning of complementary DNA encoding one of the human
RT pancreatic protease E isozymes.";
RL J. Biochem. 104:259-264(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-241.
RC TISSUE=Pancreas, and Prostate;
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).
CC -!- FUNCTION: Efficient protease with alanine specificity but only little
CC elastolytic activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.;
CC EC=3.4.21.70;
CC -!- INTERACTION:
CC P09093; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-8646391, EBI-11522760;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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; M18700; AAA66350.1; -; Genomic_DNA.
DR EMBL; M18693; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18694; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18695; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18696; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18697; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18698; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; M18699; AAA66350.1; JOINED; Genomic_DNA.
DR EMBL; D00306; BAA00212.1; -; mRNA.
DR EMBL; AL590556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005918; AAH05918.1; -; mRNA.
DR EMBL; BC007028; AAH07028.1; -; mRNA.
DR EMBL; BC015103; AAH15103.1; -; mRNA.
DR CCDS; CCDS220.1; -.
DR PIR; A29934; A29934.
DR RefSeq; NP_005738.4; NM_005747.4.
DR AlphaFoldDB; P09093; -.
DR SMR; P09093; -.
DR BioGRID; 115439; 47.
DR IntAct; P09093; 13.
DR MINT; P09093; -.
DR STRING; 9606.ENSP00000290122; -.
DR MEROPS; S01.154; -.
DR GlyGen; P09093; 2 sites, 1 O-linked glycan (1 site).
DR BioMuta; CELA3A; -.
DR DMDM; 288558842; -.
DR jPOST; P09093; -.
DR MassIVE; P09093; -.
DR PaxDb; P09093; -.
DR PeptideAtlas; P09093; -.
DR PRIDE; P09093; -.
DR ProteomicsDB; 52197; -.
DR Antibodypedia; 30054; 171 antibodies from 21 providers.
DR DNASU; 10136; -.
DR Ensembl; ENST00000290122.8; ENSP00000290122.3; ENSG00000142789.20.
DR GeneID; 10136; -.
DR KEGG; hsa:10136; -.
DR MANE-Select; ENST00000290122.8; ENSP00000290122.3; NM_005747.5; NP_005738.4.
DR UCSC; uc001bfl.4; human.
DR CTD; 10136; -.
DR DisGeNET; 10136; -.
DR GeneCards; CELA3A; -.
DR HGNC; HGNC:15944; CELA3A.
DR HPA; ENSG00000142789; Tissue enriched (pancreas).
DR MIM; 618693; gene.
DR neXtProt; NX_P09093; -.
DR OpenTargets; ENSG00000142789; -.
DR PharmGKB; PA27736; -.
DR VEuPathDB; HostDB:ENSG00000142789; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P09093; -.
DR OMA; GHCIGSR; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P09093; -.
DR TreeFam; TF330455; -.
DR PathwayCommons; P09093; -.
DR SignaLink; P09093; -.
DR BioGRID-ORCS; 10136; 11 hits in 1058 CRISPR screens.
DR GeneWiki; CELA3A; -.
DR GenomeRNAi; 10136; -.
DR Pharos; P09093; Tbio.
DR PRO; PR:P09093; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P09093; protein.
DR Bgee; ENSG00000142789; Expressed in body of pancreas and 81 other tissues.
DR ExpressionAtlas; P09093; baseline and differential.
DR Genevisible; P09093; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /note="Or 16"
FT /evidence="ECO:0000255"
FT PROPEP 16..28
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027697"
FT CHAIN 29..270
FT /note="Chymotrypsin-like elastase family member 3A"
FT /id="PRO_0000027698"
FT DOMAIN 29..268
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
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 217
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..120
FT /evidence="ECO:0000305"
FT DISULFID 157..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 213..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 24
FT /note="H -> R (in dbSNP:rs7531336)"
FT /id="VAR_059783"
FT VARIANT 25
FT /note="S -> P (in dbSNP:rs7533776)"
FT /id="VAR_059784"
FT VARIANT 31
FT /note="H -> N (in dbSNP:rs7519660)"
FT /id="VAR_059785"
FT VARIANT 241
FT /note="A -> G (in dbSNP:rs3820285)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2460440, ECO:0000269|PubMed:2826474"
FT /id="VAR_051838"
FT CONFLICT 63
FT /note="I -> T (in Ref. 4; AAH05918)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Missing (in Ref. 1; AAA66350)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="K -> E (in Ref. 4; AAH05918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29489 MW; 576DDB255A4C71EA CRC64;
MMLRLLSSLL LVAVASGYGP PSSHSSSRVV HGEDAVPYSW PWQVSLQYEK SGSFYHTCGG
SLIAPDWVVT AGHCISRDLT YQVVLGEYNL AVKEGPEQVI PINSEELFVH PLWNRSCVAC
GNDIALIKLS RSAQLGDAVQ LASLPPAGDI LPNKTPCYIT GWGRLYTNGP LPDKLQQARL
PVVDYKHCSR WNWWGSTVKK TMVCAGGYIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS
AFGCNFIWKP TVFTRVSAFI DWIEETIASH
