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Reviewed, UniProtKB/Swiss-Prot P08217 (ELA2A_HUMAN)

Last modified June 16, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Elastase-2A
    EC=3.4.21.71
Gene names
Name: ELA2A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.6

Subcellular location

Secreted.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

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Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity Ref.3

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 2812Activation peptide
PRO_0000027693
Chain29 – 269241Elastase-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: dbSNP rs2303193.
VAR_051837

Experimental info

Sequence conflict2021C → V in BAA00165. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P08217-1 [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

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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: 3427074] [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: 3646943] [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: 2834346] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[4]"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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[6]"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: 2307232] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-50, INTERACTION WITH CPA1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M16631 mRNA. Translation: AAA52374.1.
M16652 mRNA. Translation: AAA52380.1.
D00236 mRNA. Translation: BAA00165.1.
AL512883 Genomic DNA. Translation: CAC42421.1.
BC007031 mRNA. Translation: AAH07031.1.
IPIIPI00027722.
PIRB26823.
RefSeqNP_254275.1.
UniGeneHs.631866

3D structure databases

HSSPHSSP built from PDB template 1BRU based on UniProtKB P08419.
SMRP08217. Positions 29-269.
ModBaseSearch...

Protein family/group databases

MEROPSS01.155.

Proteomic databases

PRIDEP08217.

Genome annotation databases

EnsemblENSG00000142615. Homo sapiens. [Contig view]
GeneID63036.
KEGGhsa:63036.

Organism-specific databases

GeneCardsGC01P015655.
H-InvDBHIX0000152.
MIM609443. gene.

Phylogenomic databases

HOVERGENP08217.

Enzyme and pathway databases

BRENDA3.4.21.71. 247.

Gene expression databases

ArrayExpressP08217.
BgeeP08217.
GermOnlineENSG00000142615. Homo sapiens.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio65535.
PMAP-CutDBP08217.
SOURCESearch...

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Entry information

Entry nameELA2A_HUMAN
AccessionPrimary (citable) accession number: P08217
Secondary accession number(s): Q14243
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents