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Reviewed, UniProtKB/Swiss-Prot P09093 (ELA3A_HUMAN)

Last modified March 3, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-3A
    EC=3.4.21.70
Alternative name(s):
    Elastase IIIA
    Protease E
Gene names
Name: ELA3A
Synonyms: ELA3
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 length270 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

Efficient protease with alanine specificity but only little elastolytic activity.

Catalytic activity

Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

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Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcholesterol metabolic process Ref.1

Traceable author statement. Source: ProtInc

digestion Ref.1

Traceable author statement. Source: ProtInc

proteolysis Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionserine-type endopeptidase activity Ref.2

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 – 1515Or 16 Potential
Propeptide16 – 2813Activation peptide Potential
PRO_0000027697
Chain29 – 270242Elastase-3A Ref.1
PRO_0000027698

Regions

Domain29 – 268240Peptidase S1

Sites

Active site731Charge relay system By similarity
Active site1231Charge relay system By similarity
Active site2171Charge relay system By similarity

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 74 By similarity
Disulfide bond117 ↔ 120 Probable
Disulfide bond157 ↔ 223 By similarity
Disulfide bond188 ↔ 204 By similarity
Disulfide bond213 ↔ 244 By similarity

Natural variations

Natural variant2411G → A: dbSNP rs3820285. Ref.3
VAR_051838

Experimental info

Sequence conflict631I → T in AAH05918. Ref.4
Sequence conflict1061Missing in AAA66350. Ref.1
Sequence conflict1741K → E in AAH05918. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P09093-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 576DDB255A4A118C

FASTA27029,475
        10         20         30         40         50         60 
MMLRLLSSLL LVAVASGYGP PSSHSSSRVV HGEDAVPYSW PWQVSLQYEK SGSFYHTCGG 

        70         80         90        100        110        120 
SLIAPDWVVT AGHCISRDLT YQVVLGEYNL AVKEGPEQVI PINSEELFVH PLWNRSCVAC 

       130        140        150        160        170        180 
GNDIALIKLS RSAQLGDAVQ LASLPPAGDI LPNKTPCYIT GWGRLYTNGP LPDKLQQARL 

       190        200        210        220        230        240 
PVVDYKHCSR WNWWGSTVKK TMVCAGGYIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS 

       250        260        270 
GFGCNFIWKP TVFTRVSAFI DWIEETIASH

« Hide

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References

« Hide 'large scale' references
[1]"Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning."
Tani T., Ohsumi J., Mita K., Takiguchi Y.
J. Biol. Chem. 263:1231-1239(1988) [PubMed: 2826474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Pancreas.
[2]"Molecular cloning of complementary DNA encoding one of the human pancreatic protease E isozymes."
Shirasu Y., Takemura K., Yoshida H., Sato Y., Iijima H., Shimada Y., Mikayama T., Ozawa T., Ikeda N., Ishida A., Tamai Y., Matsuki S., Tanaka J., Ikenaga H., Ogawa M.
J. Biochem. 104:259-264(1988) [PubMed: 2460440] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Pancreas.
[3]"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], VARIANT ALA-241.
[4]"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 and Prostate.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M18700 expand/collapse EMBL AC list , M18693, M18694, M18695, M18696, M18697, M18698, M18699 Genomic DNA. Translation: AAA66350.1.
D00306 mRNA. Translation: BAA00212.1.
AL590556 Genomic DNA. Translation: CAH71875.1.
BC005918 mRNA. Translation: AAH05918.1.
BC007028 mRNA. Translation: AAH07028.1.
BC015103 mRNA. Translation: AAH15103.1.
IPIIPI00295663.
PIRA29934.
RefSeqNP_005738.3.
UniGeneHs.654349

3D structure databases

HSSPHSSP built from PDB template 1FON based on UniProtKB P05805.
SMRP09093. Positions 23-270.
ModBaseSearch...

Protein family/group databases

MEROPSS01.154.

Genome annotation databases

EnsemblENSG00000142789. Homo sapiens. [Contig view]
GeneID10136.
KEGGhsa:10136.

Organism-specific databases

GeneCardsGC01P022200.
H-InvDBHIX0000228.
HGNCHGNC:15944. ELA3A.
PharmGKBPA27736.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP09093.

Enzyme and pathway databases

BRENDA3.4.21.70. 247.

Gene expression databases

ArrayExpressP09093.
BgeeP09093.
CleanExHS_ELA3A.
GermOnlineENSG00000142789. 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

NextBio38345.

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Entry information

Entry nameELA3A_HUMAN
AccessionPrimary (citable) accession number: P09093
Secondary accession number(s): B1AQ53, Q9BRW4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: March 3, 2009
This is version 94 of the entry and version 2 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

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