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P08861

- CEL3B_HUMAN

UniProt

P08861 - CEL3B_HUMAN

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Protein

Chymotrypsin-like elastase family member 3B

Gene
CELA3B, ELA3B
Organism
Homo sapiens (Human)
Status
Reviewed - 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 system By similarity
Active sitei123 – 1231Charge relay system By similarity
Active sitei217 – 2171Charge relay system By 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 16 Reviewed predictionAdd
BLAST
Propeptidei16 – 2813Activation peptide Reviewed predictionPRO_0000027699Add
BLAST
Chaini29 – 270242Chymotrypsin-like elastase family member 3BPRO_0000027700Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 268240Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiP08861.
KOiK01345.
OMAiGCNTIKK.
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

MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK    50
SGSFYHTCGG SLIAPDWVVT AGHCISSSRT YQVVLGEYDR AVKEGPEQVI 100
PINSGDLFVH PLWNRSCVAC GNDIALIKLS RSAQLGDAVQ LASLPPAGDI 150
LPNETPCYIT GWGRLYTNGP LPDKLQEALL PVVDYEHCSR WNWWGSSVKK 200
TMVCAGGDIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS AFGCNTRRKP 250
TVFTRVSAFI DWIEETIASH 270
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.
The sequence CAH71873.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41R → G in AAA36482. 1 Publication
Sequence conflicti64 – 641A → G in AAA36482. 1 Publication
Sequence conflicti129 – 1313Missing AA sequence 1 Publication
Sequence conflicti164 – 1641R → P in AAA36482. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS219.1.
PIRi B29934.
RefSeqi NP_031378.1. NM_007352.2.
UniGenei Hs.728752.

3D structure databases

ProteinModelPortali P08861.
SMRi P08861. Positions 23-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000338369.

Chemistry

BindingDBi P08861.

Protein family/group databases

MEROPSi S01.205.

PTM databases

PhosphoSitei P08861.
UniCarbKBi P08861.

Polymorphism databases

DMDMi 317373457.

2D gel databases

SWISS-2DPAGE P08861.

Proteomic databases

PaxDbi P08861.
PRIDEi P08861.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337107 ; ENSP00000338369 ; ENSG00000219073 .
GeneIDi 23436.
KEGGi hsa:23436.
UCSCi uc001bfk.3. human.

Organism-specific databases

CTDi 23436.
GeneCardsi GC01P022303.
HGNCi HGNC:15945. CELA3B.
HPAi HPA045650.
neXtProti NX_P08861.
PharmGKBi PA27737.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
InParanoidi P08861.
KOi K01345.
OMAi GCNTIKK.
OrthoDBi EOG75B84T.
PhylomeDBi P08861.
TreeFami TF330455.

Miscellaneous databases

GeneWikii CELA3B.
GenomeRNAii 23436.
NextBioi 45699.
PROi P08861.

Gene expression databases

Bgeei P08861.
CleanExi HS_ELA3B.
Genevestigatori P08861.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 144 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 (1 Publication) thought to be elastase 1.

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

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