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Protein

Chymotrypsin-like elastase family member 3B

Gene

CELA3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Efficient protease with alanine specificity but only little elastolytic activity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Charge relay systemBy similarity
Active sitei123 – 1231Charge relay systemBy similarity
Active sitei217 – 2171Charge relay systemBy similarity

GO - Molecular functioni

  1. peptidase activity Source: ProtInc
  2. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. cholesterol metabolic process Source: ProtInc
  2. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.205.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-like elastase family member 3B (EC:3.4.21.70)
Alternative name(s):
Elastase IIIB
Elastase-3B
Protease E
Gene namesi
Name:CELA3B
Synonyms:ELA3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:15945. CELA3B.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Or 16Sequence AnalysisAdd
BLAST
Propeptidei16 – 2813Activation peptideSequence AnalysisPRO_0000027699Add
BLAST
Chaini29 – 270242Chymotrypsin-like elastase family member 3BPRO_0000027700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Glycosylationi114 – 1141N-linked (GlcNAc...)1 PublicationCAR_000212
Disulfide bondi117 ↔ 120Curated
Disulfide bondi157 ↔ 223PROSITE-ProRule annotation
Disulfide bondi188 ↔ 204PROSITE-ProRule annotation
Disulfide bondi213 ↔ 244PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP08861.
PRIDEiP08861.

2D gel databases

SWISS-2DPAGEP08861.

PTM databases

PhosphoSiteiP08861.
UniCarbKBiP08861.

Expressioni

Tissue specificityi

Pancreas. Not detectable in keratinocytes.1 Publication

Gene expression databases

BgeeiP08861.
CleanExiHS_ELA3B.
GenevestigatoriP08861.

Organism-specific databases

HPAiHPA045650.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000338369.

Structurei

3D structure databases

ProteinModelPortaliP08861.
SMRiP08861. Positions 23-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 268240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
InParanoidiP08861.
KOiK01345.
OMAiCGRPSYQ.
OrthoDBiEOG75B84T.
PhylomeDBiP08861.
TreeFamiTF330455.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08861-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK
60 70 80 90 100
SGSFYHTCGG SLIAPDWVVT AGHCISSSRT YQVVLGEYDR AVKEGPEQVI
110 120 130 140 150
PINSGDLFVH PLWNRSCVAC GNDIALIKLS RSAQLGDAVQ LASLPPAGDI
160 170 180 190 200
LPNETPCYIT GWGRLYTNGP LPDKLQEALL PVVDYEHCSR WNWWGSSVKK
210 220 230 240 250
TMVCAGGDIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS AFGCNTRRKP
260 270
TVFTRVSAFI DWIEETIASH
Length:270
Mass (Da):29,263
Last modified:January 11, 2011 - v3
Checksum:iF738C5F8F5195D8C
GO

Sequence cautioni

The sequence CAH71872.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH71873.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41R → G in AAA36482. (PubMed:15489334)Curated
Sequence conflicti64 – 641A → G in AAA36482. (PubMed:15489334)Curated
Sequence conflicti129 – 1313Missing AA sequence (PubMed:2737288)Curated
Sequence conflicti164 – 1641R → P in AAA36482. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791R → W.3 Publications
Corresponds to variant rs7528405 [ dbSNP | Ensembl ].
VAR_025446

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS219.1.
PIRiB29934.
RefSeqiNP_031378.1. NM_007352.2.
UniGeneiHs.728752.

Genome annotation databases

EnsembliENST00000337107; ENSP00000338369; ENSG00000219073.
GeneIDi23436.
KEGGihsa:23436.
UCSCiuc001bfk.3. human.

Polymorphism databases

DMDMi317373457.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS219.1.
PIRiB29934.
RefSeqiNP_031378.1. NM_007352.2.
UniGeneiHs.728752.

3D structure databases

ProteinModelPortaliP08861.
SMRiP08861. Positions 23-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000338369.

Protein family/group databases

MEROPSiS01.205.

PTM databases

PhosphoSiteiP08861.
UniCarbKBiP08861.

Polymorphism databases

DMDMi317373457.

2D gel databases

SWISS-2DPAGEP08861.

Proteomic databases

PaxDbiP08861.
PRIDEiP08861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337107; ENSP00000338369; ENSG00000219073.
GeneIDi23436.
KEGGihsa:23436.
UCSCiuc001bfk.3. human.

Organism-specific databases

CTDi23436.
GeneCardsiGC01P022303.
HGNCiHGNC:15945. CELA3B.
HPAiHPA045650.
neXtProtiNX_P08861.
PharmGKBiPA27737.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
InParanoidiP08861.
KOiK01345.
OMAiCGRPSYQ.
OrthoDBiEOG75B84T.
PhylomeDBiP08861.
TreeFamiTF330455.

Miscellaneous databases

GeneWikiiCELA3B.
GenomeRNAii23436.
NextBioi45699.
PROiP08861.

Gene expression databases

BgeeiP08861.
CleanExiHS_ELA3B.
GenevestigatoriP08861.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCEL3B_HUMAN
AccessioniPrimary (citable) accession number: P08861
Secondary accession number(s): B2RE44
, P11423, Q5VU28, Q5VU29, Q5VU30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 11, 2011
Last modified: January 7, 2015
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was originally thought to be elastase 1.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.