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Q9UNI1 (CELA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsin-like elastase family member 1

EC=3.4.21.36
Alternative name(s):
Elastase-1
Pancreatic elastase 1
Gene names
Name:CELA1
Synonyms:ELA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts upon elastin.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Tissue specificity

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

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

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 (Ref.1).

Sequence caution

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

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

exocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

pancreas morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 88 By similarity
Propeptide9 – 1810Activation peptide
PRO_0000027677
Chain19 – 258240Chymotrypsin-like elastase family member 1
PRO_0000027678

Regions

Domain19 – 256238Peptidase S1

Sites

Active site631Charge relay system By similarity
Active site1111Charge relay system By similarity
Active site2061Charge relay system By similarity
Metal binding771Calcium By similarity
Metal binding821Calcium; via carbonyl oxygen By similarity
Metal binding871Calcium By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 64 By similarity
Disulfide bond145 ↔ 212 By similarity
Disulfide bond176 ↔ 192 By similarity
Disulfide bond202 ↔ 232 By similarity

Natural variations

Natural variant101Q → H.
Corresponds to variant rs17860287 [ dbSNP | Ensembl ].
VAR_033645
Natural variant441R → W.
Corresponds to variant rs17860299 [ dbSNP | Ensembl ].
VAR_033646
Natural variant591M → V.
Corresponds to variant rs17860300 [ dbSNP | Ensembl ].
VAR_033647
Natural variant761G → A in a breast cancer sample; somatic mutation. Ref.5
VAR_036295
Natural variant2431Q → R.
Corresponds to variant rs17860364 [ dbSNP | Ensembl ].
VAR_033648

Experimental info

Sequence conflict2201V → L in AAD28441. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UNI1 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 684EDE8F1F011F8D

FASTA25827,798
        10         20         30         40         50         60 
MLVLYGHSTQ DLPETNARVV GGTEAGRNSW PSQISLQYRS GGSRYHTCGG TLIRQNWVMT 

        70         80         90        100        110        120 
AAHCVDYQKT FRVVAGDHNL SQNDGTEQYV SVQKIVVHPY WNSDNVAAGY DIALLRLAQS 

       130        140        150        160        170        180 
VTLNSYVQLG VLPQEGAILA NNSPCYITGW GKTKTNGQLA QTLQQAYLPS VDYAICSSSS 

       190        200        210        220        230        240 
YWGSTVKNTM VCAGGDGVRS GCQGDSGGPL HCLVNGKYSV HGVTSFVSSR GCNVSRKPTV 

       250 
FTQVSAYISW INNVIASN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-76.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Elastase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8812.1.
RefSeqNP_001962.3. NM_001971.5.
UniGeneHs.348395.

3D structure databases

ProteinModelPortalQ9UNI1.
SMRQ9UNI1. Positions 19-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000293636.

Chemistry

BindingDBQ9UNI1.
ChEMBLCHEMBL3000.

Protein family/group databases

MEROPSS01.153.

Polymorphism databases

DMDM62298049.

Proteomic databases

PaxDbQ9UNI1.
PRIDEQ9UNI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293636; ENSP00000293636; ENSG00000139610.
GeneID1990.
KEGGhsa:1990.
UCSCuc001ryi.1. human.

Organism-specific databases

CTD1990.
GeneCardsGC12M051723.
HGNCHGNC:3308. CELA1.
MIM130120. gene.
neXtProtNX_Q9UNI1.
PharmGKBPA27734.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidQ9UNI1.
KOK01326.
OMAKSGSSWY.
OrthoDBEOG7RRF7Z.
PhylomeDBQ9UNI1.
TreeFamTF330455.

Enzyme and pathway databases

BRENDA3.4.21.36. 2681.

Gene expression databases

ArrayExpressQ9UNI1.
BgeeQ9UNI1.
CleanExHS_ELA1.
GenevestigatorQ9UNI1.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCELA1.
GenomeRNAi1990.
NextBio8047.
PMAP-CutDBQ9UNI1.
PROQ9UNI1.
SOURCESearch...

Entry information

Entry nameCELA1_HUMAN
AccessionPrimary (citable) accession number: Q9UNI1
Secondary accession number(s): Q5MLF0, Q6DJT0, Q6ISM6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM