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P08861

- CEL3B_HUMAN

UniProt

P08861 - CEL3B_HUMAN

Protein

Chymotrypsin-like elastase family member 3B

Gene

CELA3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    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

    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 145 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