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   24-JAN-2024, entry version 196.
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}.
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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   GlyCosmos; P09093; 1 site, No reported glycans.
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; 9606-ENSP00000290122; -.
DR   PeptideAtlas; P09093; -.
DR   ProteomicsDB; 52197; -.
DR   Antibodypedia; 30054; 192 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   AGR; HGNC:15944; -.
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; QWISDTM; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P09093; -.
DR   TreeFam; TF330455; -.
DR   PathwayCommons; P09093; -.
DR   SignaLink; P09093; -.
DR   BioGRID-ORCS; 10136; 11 hits in 1136 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 cell types or tissues.
DR   ExpressionAtlas; P09093; baseline and differential.
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; 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:SF11; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 3A; 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; P09093; HS.
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
//