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Reviewed, UniProtKB/Swiss-Prot P08861 (ELA3B_HUMAN)

Last modified March 3, 2009. Version 102. 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-3B
    EC=3.4.21.70
Alternative name(s):
    Elastase IIIB
    Protease E
Gene names
Name: ELA3B
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.

Caution

Was originally (Ref.8) thought to be elastase 1.

Sequence caution

The sequence CAH71872.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH71873.1 differs from that shown. Reason: Erroneous gene model prediction.

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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

proteolysis

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region

Non-traceable author statement. Source: UniProtKB

   Molecular functionserine-type endopeptidase activity Ref.1 Ref.8

Non-traceable author statement. Source: UniProtKB

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_0000027699
Chain29 – 270242Elastase-3B
PRO_0000027700

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...) Ref.8
CAR_000212
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 variant791W → R: dbSNP rs7528405. Ref.1 Ref.2
VAR_025446

Experimental info

Sequence conflict41R → G in AAA36482. Ref.3
Sequence conflict641A → G in AAA36482. Ref.3
Sequence conflict129 – 1313Missing AA sequence Ref.8
Sequence conflict1641R → P in AAA36482. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P08861-1 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: B14BE0AAD3695AFE

FASTA27029,293
        10         20         30         40         50         60 
MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK SGSFYHTCGG 

        70         80         90        100        110        120 
SLIAPDWVVT AGHCISSSWT YQVVLGEYDR AVKEGPEQVI PINSGDLFVH PLWNRSCVAC 

       130        140        150        160        170        180 
GNDIALIKLS RSAQLGDAVQ LASLPPAGDI LPNETPCYIT GWGRLYTNGP LPDKLQEALL 

       190        200        210        220        230        240 
PVVDYEHCSR WNWWGSSVKK TMVCAGGDIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS 

       250        260        270 
AFGCNTRRKP 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 [MRNA], VARIANT ARG-79.
Tissue: Pancreas.
[2]"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 ARG-79.
[3]"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.
[4]"Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA."
Shen W., Fletcher T.S., Largman C.
Biochemistry 26:3447-3452(1987) [PubMed: 3477287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
Tissue: Pancreas.
[5]"Generation of a subunit III-like protein by autolysis of human and porcine proproteinase E in a binary complex with procarboxypeptidase A."
Aviles F.X., Pascual R., Salva M., Bonicel J., Puigserver A.
Biochem. Biophys. Res. Commun. 163:1191-1196(1989) [PubMed: 2675835] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-57.
[6]"Characterization of two glycoproteins of human pancreatic juice: P35, a truncated protease E and P19, precursor of protein X."
Guy-Crotte O., Barthe C., Basso D., Fournet B., Figarella C.
Biochem. Biophys. Res. Commun. 156:318-322(1988) [PubMed: 3178837] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-63.
[7]"Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice."
Moulard M., Kerfelec B., Mallet B., Chapus C.
FEBS Lett. 250:166-170(1989) [PubMed: 2753124] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-50.
Tissue: Pancreas.
[8]"Localization and characterization of the glycosylation site of human pancreatic elastase 1."
Wendorf P., Geyer R., Sziegoleit A., Linder D.
FEBS Lett. 249:275-278(1989) [PubMed: 2737288] [Abstract]
Cited for: PROTEIN SEQUENCE OF 94-164, GLYCOSYLATION AT ASN-114.
Tissue: Pancreas.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M16630 mRNA. Translation: AAA36482.1.
AL590556 Genomic DNA. Translation: CAH71871.1.
AL590556 Genomic DNA. Translation: CAH71872.1. Sequence problems.
AL590556 Genomic DNA. Translation: CAH71873.1. Sequence problems.
BC005216 mRNA. Translation: AAH05216.1.
M18692 mRNA. Translation: AAA58454.1.
IPIIPI00307485.
PIRB29934.
RefSeqNP_031378.1.
UniGeneHs.181289

3D structure databases

HSSPHSSP built from PDB template 1PYT based on UniProtKB P05805.
SMRP08861. Positions 23-270.
ModBaseSearch...

Protein family/group databases

MEROPSS01.205.

PTM databases

GlycoSuiteDBP08861.

2-D gel databases

SWISS-2DPAGEP08861.

Proteomic databases

PRIDEP08861.

Genome annotation databases

EnsemblENSG00000219073. Homo sapiens. [Contig view]
GeneID23436.
KEGGhsa:23436.

Organism-specific databases

GeneCardsGC01P022175.
HGNCHGNC:15945. ELA3B.
PharmGKBPA27737.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP08861.
HOVERGENP08861.

Enzyme and pathway databases

BRENDA3.4.21.70. 247.

Gene expression databases

ArrayExpressP08861.
BgeeP08861.
CleanExHS_ELA3B.
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

NextBio45699.

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Entry information

Entry nameELA3B_HUMAN
AccessionPrimary (citable) accession number: P08861
Secondary accession number(s): P11423 expand/collapse secondary AC list , Q5VU28, Q5VU29, Q5VU30
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: June 1, 2001
Last modified: March 3, 2009
This is version 102 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