P08861 (CEL3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Traceable author statement Ref.1. Source: ProtInc proteolysis Non-traceable author statement. Source: UniProtKB
Cellular_component	extracellular region Non-traceable author statement. Source: UniProtKB
Molecular_function	serine-type endopeptidase activity Non-traceable author statement Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Or 16 Potential
	Propeptide	16 – 28	13	Activation peptide Potential		PRO_0000027699
	Chain	29 – 270	242	Chymotrypsin-like elastase family member 3B		PRO_0000027700
Regions
	Domain	29 – 268	240	Peptidase S1
Sites
	Active site	73	1	Charge relay system By similarity
	Active site	123	1	Charge relay system By similarity
	Active site	217	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	114	1	N-linked (GlcNAc...) Ref.10		CAR_000212
	Disulfide bond	58 ↔ 74		By similarity
	Disulfide bond	117 ↔ 120		Probable
	Disulfide bond	157 ↔ 223		By similarity
	Disulfide bond	188 ↔ 204		By similarity
	Disulfide bond	213 ↔ 244		By similarity
Natural variations
	Natural variant	79	1	R → W. Ref.2 Ref.3 Ref.5 Corresponds to variant rs7528405 [ dbSNP | Ensembl ].		VAR_025446
Experimental info
	Sequence conflict	4	1	R → G in AAA36482. Ref.5
	Sequence conflict	64	1	A → G in AAA36482. Ref.5
	Sequence conflict	129 – 131	3	Missing AA sequence Ref.10
	Sequence conflict	164	1	R → P in AAA36482. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P08861 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: F738C5F8F5195D8C	FASTA	270	29,263
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00307485.
PIR	B29934.
RefSeq	NP_031378.1. NM_007352.2.
UniGene	Hs.728752.
3D structure databases
ProteinModelPortal	P08861.
SMR	P08861. Positions 23-270.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000338369.
Protein family/group databases
MEROPS	S01.205.
PTM databases
GlycoSuiteDB	P08861.
PhosphoSite	P08861.
Polymorphism databases
DMDM	14195655.
2D gel databases
SWISS-2DPAGE	P08861.
Proteomic databases
PaxDb	P08861.
PRIDE	P08861.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000337107; ENSP00000338369; ENSG00000219073. ENST00000374666; ENSP00000363798; ENSG00000219073. ENST00000400277; ENSP00000383135; ENSG00000219073.
GeneID	23436.
KEGG	hsa:23436.
UCSC	uc001bfk.3. human.
Organism-specific databases
CTD	23436.
GeneCards	GC01P022303.
HGNC	HGNC:15945. CELA3B.
HPA	HPA045650.
neXtProt	NX_P08861.
PharmGKB	PA27737.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000251820.
InParanoid	P08861.
KO	K01345.
OMA	GCNTIKK.
OrthoDB	EOG4XPQGN.
PhylomeDB	P08861.
Gene expression databases
Bgee	P08861.
CleanEx	HS_ELA3B.
Genevestigator	P08861.
GermOnline	ENSG00000142789. Homo sapiens.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P08861.
ChEMBL	CHEMBL4995.
GenomeRNAi	23436.
NextBio	45699.

Entry information

Entry name

CEL3B_HUMAN

Accession

Primary (citable) accession number: P08861
Secondary accession number(s): B2RE44 , P11423, Q5VU28, Q5VU29, Q5VU30

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.