Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08861 (CEL3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 3B

EC=3.4.21.70
Alternative name(s):
Elastase IIIB
Elastase-3B
Protease E
Gene names
Name:CELA3B
Synonyms:ELA3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Efficient protease with alanine specificity but only little elastolytic activity.

Catalytic activity

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

Tissue specificity

Pancreas. Not detectable in keratinocytes. Ref.11

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Caution

Was originally (Ref.10) 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515Or 16 Potential
Propeptide16 – 2813Activation peptide Potential
PRO_0000027699
Chain29 – 270242Chymotrypsin-like elastase family member 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.10
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 variant791R → W. Ref.2 Ref.3 Ref.5
Corresponds to variant rs7528405 [ dbSNP | Ensembl ].
VAR_025446

Experimental info

Sequence conflict41R → G in AAA36482. Ref.5
Sequence conflict641A → G in AAA36482. Ref.5
Sequence conflict129 – 1313Missing AA sequence Ref.10
Sequence conflict1641R → P in AAA36482. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P08861 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: F738C5F8F5195D8C

FASTA27029,263
        10         20         30         40         50         60 
MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK SGSFYHTCGG 

        70         80         90        100        110        120 
SLIAPDWVVT AGHCISSSRT 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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-79.
Tissue: Urinary bladder.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-79.
[4]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].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-79.
Tissue: Pancreas.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
Tissue: Pancreas.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-57.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-63.
[9]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-50.
Tissue: Pancreas.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 94-164, GLYCOSYLATION AT ASN-114.
Tissue: Pancreas.
[11]"Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism."
Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.
J. Invest. Dermatol. 114:165-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16630 mRNA. Translation: AAA36482.1.
AK315798 mRNA. Translation: BAG38141.1.
AL590556 Genomic DNA. Translation: CAH71871.1.
AL590556 Genomic DNA. Translation: CAH71872.1. Sequence problems.
AL590556 Genomic DNA. Translation: CAH71873.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW94999.1.
BC005216 mRNA. Translation: AAH05216.1.
M18692 mRNA. Translation: AAA58454.1.
CCDSCCDS219.1.
PIRB29934.
RefSeqNP_031378.1. NM_007352.2.
UniGeneHs.728752.

3D structure databases

ProteinModelPortalP08861.
SMRP08861. Positions 23-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000338369.

Chemistry

BindingDBP08861.

Protein family/group databases

MEROPSS01.205.

PTM databases

PhosphoSiteP08861.
UniCarbKBP08861.

Polymorphism databases

DMDM317373457.

2D gel databases

SWISS-2DPAGEP08861.

Proteomic databases

PaxDbP08861.
PRIDEP08861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337107; ENSP00000338369; ENSG00000219073.
GeneID23436.
KEGGhsa:23436.
UCSCuc001bfk.3. human.

Organism-specific databases

CTD23436.
GeneCardsGC01P022303.
HGNCHGNC:15945. CELA3B.
HPAHPA045650.
neXtProtNX_P08861.
PharmGKBPA27737.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidP08861.
KOK01345.
OMAGCNTIKK.
OrthoDBEOG75B84T.
PhylomeDBP08861.
TreeFamTF330455.

Gene expression databases

BgeeP08861.
CleanExHS_ELA3B.
GenevestigatorP08861.

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

GeneWikiCELA3B.
GenomeRNAi23436.
NextBio45699.
PROP08861.

Entry information

Entry nameCEL3B_HUMAN
AccessionPrimary (citable) accession number: P08861
Secondary accession number(s): B2RE44 expand/collapse secondary AC list , P11423, Q5VU28, Q5VU29, Q5VU30
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 144 of the entry and version 3 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

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