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P08218 (CEL2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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 2B

EC=3.4.21.71
Alternative name(s):
Elastase-2B
Gene names
Name:CELA2B
Synonyms:ELA2B
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 transcript level

General annotation (Comments)

Function

Acts upon elastin.

Catalytic activity

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

Subcellular location

Secreted.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionserine-type endopeptidase activity

Traceable author statement PubMed 3427074. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 2812Activation peptide
PRO_0000027695
Chain29 – 269241Chymotrypsin-like elastase family member 2B
PRO_0000027696

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 variant791G → R. Ref.1 Ref.4
Corresponds to variant rs3820071 [ dbSNP | Ensembl ].
VAR_044534
Natural variant1141D → N. Ref.1 Ref.4
Corresponds to variant rs3766160 [ dbSNP | Ensembl ].
VAR_044535
Natural variant1771Q → R. Ref.1 Ref.4
Corresponds to variant rs6429745 [ dbSNP | Ensembl ].
VAR_044536
Natural variant2351G → S.
Corresponds to variant rs3737703 [ dbSNP | Ensembl ].
VAR_044537

Sequences

Sequence LengthMass (Da)Tools
P08218 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: CC81C1D18B918B5F

FASTA26928,810
        10         20         30         40         50         60 
MIRTLLLSTL VAGALSCGVS TYAPDMSRML GGEEARPNSW PWQVSLQYSS NGQWYHTCGG 

        70         80         90        100        110        120 
SLIANSWVLT AAHCISSSGI YRVMLGQHNL YVAESGSLAV SVSKIVVHKD WNSDQVSKGN 

       130        140        150        160        170        180 
DIALLKLANP VSLTDKIQLA CLPPAGTILP NNYPCYVTGW GRLQTNGALP DDLKQGQLLV 

       190        200        210        220        230        240 
VDYATCSSSG WWGSTVKTNM ICAGGDGVIC TCNGDSGGPL NCQASDGRWE VHGIGSLTSV 

       250        260 
LGCNYYYKPS IFTRVSNYND WINSVIANN 

« Hide

References

« Hide 'large scale' references
[1]"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], VARIANTS ARG-79; ASN-114 AND ARG-177.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.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].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-79; ASN-114 AND ARG-177.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16653 mRNA. Translation: AAA52381.1.
AL512883 Genomic DNA. Translation: CAC42422.1.
CH471167 Genomic DNA. Translation: EAW51728.1.
BC069455 mRNA. Translation: AAH69455.1.
BC113540 mRNA. Translation: AAI13541.1.
BC113542 mRNA. Translation: AAI13543.1.
CCDSCCDS30605.1.
PIRC26823.
RefSeqNP_056933.2. NM_015849.2.
UniGeneHs.631871.

3D structure databases

ProteinModelPortalP08218.
SMRP08218. Positions 29-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000365075.

Chemistry

BindingDBP08218.

Protein family/group databases

MEROPSS01.206.

Polymorphism databases

DMDM212288098.

Proteomic databases

PaxDbP08218.
PRIDEP08218.

Protocols and materials databases

DNASU51032.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375910; ENSP00000365075; ENSG00000215704.
GeneID51032.
KEGGhsa:51032.
UCSCuc001awl.3. human.

Organism-specific databases

CTD51032.
GeneCardsGC01P015792.
HGNCHGNC:29995. CELA2B.
HPAHPA047270.
MIM609444. gene.
neXtProtNX_P08218.
PharmGKBPA165750841.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
KOK01346.
OMAHIWETVE.
OrthoDBEOG75B84T.
PhylomeDBP08218.
TreeFamTF330455.

Gene expression databases

ArrayExpressP08218.
BgeeP08218.
GenevestigatorP08218.

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

GeneWikiCELA2B.
GenomeRNAi51032.
NextBio53589.
PMAP-CutDBP08218.
PROP08218.
SOURCESearch...

Entry information

Entry nameCEL2B_HUMAN
AccessionPrimary (citable) accession number: P08218
Secondary accession number(s): Q14D16, Q6ISM5, Q96QV5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 129 of the entry and version 2 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