Q9UNI1 (CELA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara exocrine pancreas development Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara pancreas morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell differentiation Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 8	8	By similarity
	Propeptide	9 – 18	10	Activation peptide		PRO_0000027677
	Chain	19 – 258	240	Chymotrypsin-like elastase family member 1		PRO_0000027678
Regions
	Domain	19 – 256	238	Peptidase S1
Sites
	Active site	63	1	Charge relay system By similarity
	Active site	111	1	Charge relay system By similarity
	Active site	206	1	Charge relay system By similarity
	Metal binding	77	1	Calcium By similarity
	Metal binding	82	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	87	1	Calcium By similarity
Amino acid modifications
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	145 ↔ 212		By similarity
	Disulfide bond	176 ↔ 192		By similarity
	Disulfide bond	202 ↔ 232		By similarity
Natural variations
	Natural variant	10	1	Q → H. Corresponds to variant rs17860287 [ dbSNP | Ensembl ].		VAR_033645
	Natural variant	44	1	R → W. Corresponds to variant rs17860299 [ dbSNP | Ensembl ].		VAR_033646
	Natural variant	59	1	M → V. Corresponds to variant rs17860300 [ dbSNP | Ensembl ].		VAR_033647
	Natural variant	76	1	G → A in a breast cancer sample; somatic mutation. Ref.5		VAR_036295
	Natural variant	243	1	Q → R. Corresponds to variant rs17860364 [ dbSNP | Ensembl ].		VAR_033648
Experimental info
	Sequence conflict	220	1	V → L in AAD28441. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UNI1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 684EDE8F1F011F8D	FASTA	258	27,798
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00019729.
RefSeq	NP_001962.3. NM_001971.5.
UniGene	Hs.348395.
3D structure databases
ProteinModelPortal	Q9UNI1.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000293636.
Protein family/group databases
MEROPS	S01.153.
Polymorphism databases
DMDM	62298049.
Proteomic databases
PaxDb	Q9UNI1.
PRIDE	Q9UNI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293636; ENSP00000293636; ENSG00000139610.
GeneID	1990.
KEGG	hsa:1990.
UCSC	uc001ryi.1. human.
Organism-specific databases
CTD	1990.
GeneCards	GC12M051723.
HGNC	HGNC:3308. CELA1.
MIM	130120. gene.
neXtProt	NX_Q9UNI1.
PharmGKB	PA27734.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000251820.
InParanoid	Q9UNI1.
KO	K01326.
OMA	XNGQLAQ.
OrthoDB	EOG4V171P.
PhylomeDB	Q9UNI1.
Enzyme and pathway databases
BRENDA	3.4.21.36. 2681.
Gene expression databases
ArrayExpress	Q9UNI1.
Bgee	Q9UNI1.
CleanEx	HS_ELA1.
Genevestigator	Q9UNI1.
GermOnline	ENSG00000139610. Homo sapiens.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UNI1.
ChEMBL	CHEMBL3000.
GenomeRNAi	1990.
NextBio	8047.
PMAP-CutDB	Q9UNI1.
SOURCE	Search...

Entry information

Entry name

CELA1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.