Reviewed, UniProtKB/Swiss-Prot P08218 (ELA2B_HUMAN)

Names and origin

Protein names

Recommended name:
    Elastase-2B
    EC=3.4.21.71

Gene names

Name:

ELA2B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.1 Traceable author statement. Source: ProtInc
Molecular function	serine-type endopeptidase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16
	Propeptide	17 – 28	12	Activation peptide		PRO_0000027695
	Chain	29 – 269	241	Elastase-2B		PRO_0000027696
Regions
	Domain	29 – 267	239	Peptidase S1
Sites
	Active site	73	1	Charge relay system By similarity
	Active site	121	1	Charge relay system By similarity
	Active site	216	1	Charge relay system By similarity
Amino acid modifications
	Disulfide bond	58 ↔ 74		By similarity
	Disulfide bond	155 ↔ 222		By similarity
	Disulfide bond	186 ↔ 202		By similarity
	Disulfide bond	212 ↔ 243		By similarity
Natural variations
	Natural variant	79	1	G → R: dbSNP rs3820071. Ref.1 Ref.4		VAR_044534
	Natural variant	114	1	D → N: dbSNP rs3766160. Ref.1 Ref.4		VAR_044535
	Natural variant	177	1	Q → R: dbSNP rs6429745. Ref.1 Ref.4		VAR_044536
	Natural variant	235	1	G → S: dbSNP rs3737703.		VAR_044537

Sequences

	Sequence		Length	Mass (Da)
	P08218-1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: CC81C1D18B918B5F	FASTA	269	28,810
	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

References

	« Hide 'large scale' referencesShow '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: 3646943] [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. , 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].
[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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-79; ASN-114 AND ARG-177.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00027723.
PIR	C26823.
UniGene	Hs.631871
3D structure databases
HSSP	HSSP built from PDB template 1BRU based on UniProtKB P08419.
SMR	P08218. Positions 29-269.
ModBase	Search...
Protein family/group databases
MEROPS	S01.206.
Genome annotation databases
Ensembl	ENSG00000215704. Homo sapiens. [Contig view]
Organism-specific databases
GeneCards	GC01P015675.
MIM	609444. gene.
Phylogenomic databases
HOVERGEN	P08218.
Enzyme and pathway databases
BRENDA	3.4.21.71. 247.
Gene expression databases
ArrayExpress	P08218.
Bgee	P08218.
GermOnline	ENSG00000142615. Homo sapiens.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
PMAP-CutDB	P08218.
SOURCE	Search...

Entry information

Entry name

ELA2B_HUMAN

Accession

Primary (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:	May 26, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)