Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UNI1

- CELA1_HUMAN

UniProt

Q9UNI1 - CELA1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ9UNI1.
CleanExiHS_ELA1.
ExpressionAtlasiQ9UNI1. baseline and differential.
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.
GeneTreeiENSGT00760000119027.
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

        10         20         30         40         50
MLVLYGHSTQ DLPETNARVV GGTEAGRNSW PSQISLQYRS GGSRYHTCGG
60 70 80 90 100
TLIRQNWVMT AAHCVDYQKT FRVVAGDHNL SQNDGTEQYV SVQKIVVHPY
110 120 130 140 150
WNSDNVAAGY DIALLRLAQS VTLNSYVQLG VLPQEGAILA NNSPCYITGW
160 170 180 190 200
GKTKTNGQLA QTLQQAYLPS VDYAICSSSS YWGSTVKNTM VCAGGDGVRS
210 220 230 240 250
GCQGDSGGPL HCLVNGKYSV HGVTSFVSSR GCNVSRKPTV FTQVSAYISW

INNVIASN
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.
GeneTreei ENSGT00760000119027.
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

Bgeei Q9UNI1.
CleanExi HS_ELA1.
ExpressionAtlasi Q9UNI1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 119 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