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Chymotrypsin-like elastase family member 2A (EC 3.4.21.71) (Elastase-2A)

 CEL2A_HUMAN             Reviewed;         269 AA.
P08217; B2R5I4; Q14243;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
27-SEP-2017, entry version 160.
RecName: Full=Chymotrypsin-like elastase family member 2A;
EC=3.4.21.71;
AltName: Full=Elastase-2A;
Flags: Precursor;
Name=CELA2A; Synonyms=ELA2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3427074; DOI=10.1021/bi00397a010;
Fletcher T.S., Shen W.F., Largman C.;
"Primary structure of human pancreatic elastase 2 determined by
sequence analysis of the cloned mRNA.";
Biochemistry 26:7256-7261(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3646943; DOI=10.1089/dna.1987.6.163;
Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
"Characterization of pancreatic elastase II cDNAs: two elastase II
mRNAs are expressed in human pancreas.";
DNA 6:163-172(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=2834346;
Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y.,
Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y.,
Tanaka J., Ikenaga H.;
"Molecular cloning and expression in Escherichia coli of a cDNA
encoding human pancreatic elastase 2.";
J. Biochem. 102:1555-1563(1987).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 18-50, AND INTERACTION WITH CPA1.
PubMed=2307232; DOI=10.1016/0014-5793(90)80665-6;
Moulard M., Michon T., Kerfelec B., Chapus C.;
"Further studies on the human pancreatic binary complexes involving
procarboxypeptidase A.";
FEBS Lett. 261:179-183(1990).
[9]
TISSUE SPECIFICITY.
PubMed=10620133; DOI=10.1046/j.1523-1747.2000.00825.x;
Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.;
"Human elastase 1: evidence for expression in the skin and the
identification of a frequent frameshift polymorphism.";
J. Invest. Dermatol. 114:165-170(2000).
-!- FUNCTION: Acts upon elastin.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
and Phe-|-Xaa. Hydrolyzes elastin.
-!- SUBUNIT: Interacts with CPA1. {ECO:0000269|PubMed:2307232}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Pancreas. Not detected in keratinocytes.
{ECO:0000269|PubMed:10620133}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; M16631; AAA52374.1; -; mRNA.
EMBL; M16652; AAA52380.1; -; mRNA.
EMBL; D00236; BAA00165.1; -; mRNA.
EMBL; AK312198; BAG35131.1; -; mRNA.
EMBL; AK056678; BAG51782.1; -; mRNA.
EMBL; AL512883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471167; EAW51727.1; -; Genomic_DNA.
EMBL; BC007031; AAH07031.1; -; mRNA.
CCDS; CCDS157.1; -.
PIR; B26823; B26823.
RefSeq; NP_254275.1; NM_033440.2.
UniGene; Hs.631866; -.
ProteinModelPortal; P08217; -.
SMR; P08217; -.
STRING; 9606.ENSP00000352639; -.
DrugBank; DB06901; 2-(2-HYDROXY-CYCLOPENTYL)-PENT-4-ENAL.
MEROPS; S01.155; -.
iPTMnet; P08217; -.
PhosphoSitePlus; P08217; -.
BioMuta; CELA2A; -.
DMDM; 119255; -.
PaxDb; P08217; -.
PeptideAtlas; P08217; -.
PRIDE; P08217; -.
DNASU; 63036; -.
Ensembl; ENST00000359621; ENSP00000352639; ENSG00000142615.
GeneID; 63036; -.
KEGG; hsa:63036; -.
UCSC; uc001awk.4; human.
CTD; 63036; -.
DisGeNET; 63036; -.
EuPathDB; HostDB:ENSG00000142615.7; -.
GeneCards; CELA2A; -.
HGNC; HGNC:24609; CELA2A.
MIM; 609443; gene.
neXtProt; NX_P08217; -.
OpenTargets; ENSG00000142615; -.
PharmGKB; PA165750794; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119027; -.
HOGENOM; HOG000251820; -.
InParanoid; P08217; -.
KO; K01346; -.
OMA; KIQLGCL; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P08217; -.
TreeFam; TF330455; -.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; CELA2A; -.
GenomeRNAi; 63036; -.
PMAP-CutDB; P08217; -.
PRO; PR:P08217; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000142615; -.
Genevisible; P08217; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0036457; C:keratohyalin granule; IDA:MGI.
GO; GO:0004175; F:endopeptidase activity; TAS:Reactome.
GO; GO:0017171; F:serine hydrolase activity; IDA:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0070268; P:cornification; TAS:Reactome.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Hydrolase; Polymorphism; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 16
PROPEP 17 28 Activation peptide.
/FTId=PRO_0000027693.
CHAIN 29 269 Chymotrypsin-like elastase family member
2A.
/FTId=PRO_0000027694.
DOMAIN 29 267 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system. {ECO:0000250}.
ACT_SITE 121 121 Charge relay system. {ECO:0000250}.
ACT_SITE 216 216 Charge relay system. {ECO:0000250}.
DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 155 222 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 186 202 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 212 243 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VARIANT 257 257 N -> S (in dbSNP:rs2303193).
/FTId=VAR_051837.
CONFLICT 202 202 C -> V (in Ref. 3; BAA00165).
{ECO:0000305}.
SEQUENCE 269 AA; 28888 MW; A2E05143EFF4987C CRC64;
MIRTLLLSTL VAGALSCGDP TYPPYVTRVV GGEEARPNSW PWQVSLQYSS NGKWYHTCGG
SLIANSWVLT AAHCISSSRT YRVGLGRHNL YVAESGSLAV SVSKIVVHKD WNSNQISKGN
DIALLKLANP VSLTDKIQLA CLPPAGTILP NNYPCYVTGW GRLQTNGAVP DVLQQGRLLV
VDYATCSSSA WWGSSVKTSM ICAGGDGVIS SCNGDSGGPL NCQASDGRWQ VHGIVSFGSR
LGCNYYHKPS VFTRVSNYID WINSVIANN


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