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Q9UNI1

- CELA1_HUMAN

UniProt

Q9UNI1 - CELA1_HUMAN

Protein

Chymotrypsin-like elastase family member 1

Gene

CELA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Acts upon elastin.

    Catalytic activityi

    Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei63 – 631Charge relay systemBy similarity
    Metal bindingi77 – 771CalciumBy similarity
    Metal bindingi82 – 821Calcium; via carbonyl oxygenBy similarity
    Metal bindingi87 – 871CalciumBy similarity
    Active sitei111 – 1111Charge relay systemBy similarity
    Active sitei206 – 2061Charge relay systemBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. exocrine pancreas development Source: Ensembl
    2. inflammatory response Source: Ensembl
    3. multicellular organism growth Source: Ensembl
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. pancreas morphogenesis Source: Ensembl
    6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. post-embryonic development Source: Ensembl
    8. regulation of cell differentiation Source: Ensembl
    9. regulation of cell proliferation Source: Ensembl
    10. Wnt signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.21.36. 2681.

    Protein family/group databases

    MEROPSiS01.153.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymotrypsin-like elastase family member 1 (EC:3.4.21.36)
    Alternative name(s):
    Elastase-1
    Pancreatic elastase 1
    Gene namesi
    Name:CELA1
    Synonyms:ELA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3308. CELA1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27734.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 88By similarity
    Propeptidei9 – 1810Activation peptidePRO_0000027677
    Chaini19 – 258240Chymotrypsin-like elastase family member 1PRO_0000027678Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 64PROSITE-ProRule annotation
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi145 ↔ 212PROSITE-ProRule annotation
    Disulfide bondi176 ↔ 192PROSITE-ProRule annotation
    Disulfide bondi202 ↔ 232PROSITE-ProRule annotation
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9UNI1.
    PRIDEiQ9UNI1.

    Miscellaneous databases

    PMAP-CutDBQ9UNI1.

    Expressioni

    Tissue specificityi

    Basal layers of epidermis (at protein level). Not expressed in the pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9UNI1.
    BgeeiQ9UNI1.
    CleanExiHS_ELA1.
    GenevestigatoriQ9UNI1.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000293636.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNI1.
    SMRiQ9UNI1. Positions 19-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 256238Peptidase 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.
    InParanoidiQ9UNI1.
    KOiK01326.
    OMAiKSGSSWY.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiQ9UNI1.
    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.

    Q9UNI1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVLYGHSTQ DLPETNARVV GGTEAGRNSW PSQISLQYRS GGSRYHTCGG    50
    TLIRQNWVMT AAHCVDYQKT FRVVAGDHNL SQNDGTEQYV SVQKIVVHPY 100
    WNSDNVAAGY DIALLRLAQS VTLNSYVQLG VLPQEGAILA NNSPCYITGW 150
    GKTKTNGQLA QTLQQAYLPS VDYAICSSSS YWGSTVKNTM VCAGGDGVRS 200
    GCQGDSGGPL HCLVNGKYSV HGVTSFVSSR GCNVSRKPTV FTQVSAYISW 250
    INNVIASN 258
    Length:258
    Mass (Da):27,798
    Last modified:March 29, 2005 - v2
    Checksum:i684EDE8F1F011F8D
    GO

    Sequence cautioni

    The sequence AAV88109.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti220 – 2201V → L in AAD28441. (PubMed:10620133)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101Q → H.
    Corresponds to variant rs17860287 [ dbSNP | Ensembl ].
    VAR_033645
    Natural varianti44 – 441R → W.
    Corresponds to variant rs17860299 [ dbSNP | Ensembl ].
    VAR_033646
    Natural varianti59 – 591M → V.
    Corresponds to variant rs17860300 [ dbSNP | Ensembl ].
    VAR_033647
    Natural varianti76 – 761G → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036295
    Natural varianti243 – 2431Q → R.
    Corresponds to variant rs17860364 [ dbSNP | Ensembl ].
    VAR_033648

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF120493 mRNA. Translation: AAD28441.1.
    AC046135 Genomic DNA. No translation available.
    BC069454 mRNA. Translation: AAH69454.1.
    BC075091 mRNA. Translation: AAH75091.2.
    AY740424 Genomic DNA. Translation: AAV88109.1. Sequence problems.
    CCDSiCCDS8812.1.
    RefSeqiNP_001962.3. NM_001971.5.
    UniGeneiHs.348395.

    Genome annotation databases

    EnsembliENST00000293636; ENSP00000293636; ENSG00000139610.
    GeneIDi1990.
    KEGGihsa:1990.
    UCSCiuc001ryi.1. human.

    Polymorphism databases

    DMDMi62298049.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Elastase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF120493 mRNA. Translation: AAD28441.1 .
    AC046135 Genomic DNA. No translation available.
    BC069454 mRNA. Translation: AAH69454.1 .
    BC075091 mRNA. Translation: AAH75091.2 .
    AY740424 Genomic DNA. Translation: AAV88109.1 . Sequence problems.
    CCDSi CCDS8812.1.
    RefSeqi NP_001962.3. NM_001971.5.
    UniGenei Hs.348395.

    3D structure databases

    ProteinModelPortali Q9UNI1.
    SMRi Q9UNI1. Positions 19-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000293636.

    Chemistry

    BindingDBi Q9UNI1.
    ChEMBLi CHEMBL3000.

    Protein family/group databases

    MEROPSi S01.153.

    Polymorphism databases

    DMDMi 62298049.

    Proteomic databases

    PaxDbi Q9UNI1.
    PRIDEi Q9UNI1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293636 ; ENSP00000293636 ; ENSG00000139610 .
    GeneIDi 1990.
    KEGGi hsa:1990.
    UCSCi uc001ryi.1. human.

    Organism-specific databases

    CTDi 1990.
    GeneCardsi GC12M051723.
    HGNCi HGNC:3308. CELA1.
    MIMi 130120. gene.
    neXtProti NX_Q9UNI1.
    PharmGKBi PA27734.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    InParanoidi Q9UNI1.
    KOi K01326.
    OMAi KSGSSWY.
    OrthoDBi EOG7RRF7Z.
    PhylomeDBi Q9UNI1.
    TreeFami TF330455.

    Enzyme and pathway databases

    BRENDAi 3.4.21.36. 2681.

    Miscellaneous databases

    GeneWikii CELA1.
    GenomeRNAii 1990.
    NextBioi 8047.
    PMAP-CutDB Q9UNI1.
    PROi Q9UNI1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNI1.
    Bgeei Q9UNI1.
    CleanExi HS_ELA1.
    Genevestigatori Q9UNI1.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Keratinocyte.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Brain.
    4. NIEHS SNPs program
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-194.
    5. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-76.

    Entry informationi

    Entry nameiCELA1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNI1
    Secondary accession number(s): Q5MLF0, Q6DJT0, Q6ISM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 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

    In spite of its original name "Pancreatic elastase 1", CELA1 is not detected in the pancreas. Elastase activity described in the pancreas may be in fact due to CELA2A (PubMed:10620133).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3