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P08217 (CEL2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsin-like elastase family member 2A

EC=3.4.21.71
Alternative name(s):
Elastase-2A
Gene names
Name:CELA2A
Synonyms:ELA2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts upon elastin.

Catalytic activity

Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.

Subunit structure

Interacts with CPA1. Ref.8

Subcellular location

Secreted.

Tissue specificity

Pancreas. Not detected in keratinocytes. Ref.9

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 2812Activation peptide
PRO_0000027693
Chain29 – 269241Chymotrypsin-like elastase family member 2A
PRO_0000027694

Regions

Domain29 – 267239Peptidase S1

Sites

Active site731Charge relay system By similarity
Active site1211Charge relay system By similarity
Active site2161Charge relay system By similarity

Amino acid modifications

Disulfide bond58 ↔ 74 By similarity
Disulfide bond155 ↔ 222 By similarity
Disulfide bond186 ↔ 202 By similarity
Disulfide bond212 ↔ 243 By similarity

Natural variations

Natural variant2571N → S.
Corresponds to variant rs2303193 [ dbSNP | Ensembl ].
VAR_051837

Experimental info

Sequence conflict2021C → V in BAA00165. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08217 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A2E05143EFF4987C

FASTA26928,888
        10         20         30         40         50         60 
MIRTLLLSTL VAGALSCGDP TYPPYVTRVV GGEEARPNSW PWQVSLQYSS NGKWYHTCGG 

        70         80         90        100        110        120 
SLIANSWVLT AAHCISSSRT YRVGLGRHNL YVAESGSLAV SVSKIVVHKD WNSNQISKGN 

       130        140        150        160        170        180 
DIALLKLANP VSLTDKIQLA CLPPAGTILP NNYPCYVTGW GRLQTNGAVP DVLQQGRLLV 

       190        200        210        220        230        240 
VDYATCSSSA WWGSSVKTSM ICAGGDGVIS SCNGDSGGPL NCQASDGRWQ VHGIVSFGSR 

       250        260 
LGCNYYHKPS VFTRVSNYID WINSVIANN 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human pancreatic elastase 2 determined by sequence analysis of the cloned mRNA."
Fletcher T.S., Shen W.F., Largman C.
Biochemistry 26:7256-7261(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas."
Kawashima I., Tani T., Shimoda K., Takiguchi Y.
DNA 6:163-172(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning and expression in Escherichia coli of a cDNA encoding human pancreatic elastase 2."
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.
J. Biochem. 102:1555-1563(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas and Prostate.
[5]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[8]"Further studies on the human pancreatic binary complexes involving procarboxypeptidase A."
Moulard M., Michon T., Kerfelec B., Chapus C.
FEBS Lett. 261:179-183(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-50, INTERACTION WITH CPA1.
[9]"Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism."
Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.
J. Invest. Dermatol. 114:165-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16631 mRNA. Translation: AAA52374.1.
M16652 mRNA. Translation: AAA52380.1.
D00236 mRNA. Translation: BAA00165.1.
AK312198 mRNA. Translation: BAG35131.1.
AK056678 mRNA. Translation: BAG51782.1.
AL512883 Genomic DNA. Translation: CAC42421.1.
CH471167 Genomic DNA. Translation: EAW51727.1.
BC007031 mRNA. Translation: AAH07031.1.
CCDSCCDS157.1.
PIRB26823.
RefSeqNP_254275.1. NM_033440.2.
UniGeneHs.631866.

3D structure databases

ProteinModelPortalP08217.
SMRP08217. Positions 29-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000352639.

Chemistry

BindingDBP08217.

Protein family/group databases

MEROPSS01.155.

PTM databases

PhosphoSiteP08217.

Polymorphism databases

DMDM119255.

Proteomic databases

PaxDbP08217.
PRIDEP08217.

Protocols and materials databases

DNASU63036.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359621; ENSP00000352639; ENSG00000142615.
GeneID63036.
KEGGhsa:63036.
UCSCuc001awk.3. human.

Organism-specific databases

CTD63036.
GeneCardsGC01P015783.
HGNCHGNC:24609. CELA2A.
MIM609443. gene.
neXtProtNX_P08217.
PharmGKBPA165750794.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
KOK01346.
OMAAWWGSSV.
OrthoDBEOG75B84T.
PhylomeDBP08217.
TreeFamTF330455.

Gene expression databases

BgeeP08217.
GenevestigatorP08217.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCELA2A.
GenomeRNAi63036.
NextBio65535.
PMAP-CutDBP08217.
PROP08217.
SOURCESearch...

Entry information

Entry nameCEL2A_HUMAN
AccessionPrimary (citable) accession number: P08217
Secondary accession number(s): B2R5I4, Q14243
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM