Skip Header

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

Chymotrypsin-like elastase family member 2A

Gene

CELA2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts upon elastin.

Catalytic activityi

Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Charge relay systemBy similarity
Active sitei121 – 1211Charge relay systemBy similarity
Active sitei216 – 2161Charge relay systemBy similarity

GO - Molecular functioni

  1. serine hydrolase activity Source: MGI
  2. serine-type endopeptidase activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.155.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-like elastase family member 2A (EC:3.4.21.71)
Alternative name(s):
Elastase-2A
Gene namesi
Name:CELA2A
Synonyms:ELA2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24609. CELA2A.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. keratohyalin granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165750794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Propeptidei17 – 2812Activation peptidePRO_0000027693Add
BLAST
Chaini29 – 269241Chymotrypsin-like elastase family member 2APRO_0000027694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Disulfide bondi155 ↔ 222PROSITE-ProRule annotation
Disulfide bondi186 ↔ 202PROSITE-ProRule annotation
Disulfide bondi212 ↔ 243PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP08217.
PRIDEiP08217.

PTM databases

PhosphoSiteiP08217.

Miscellaneous databases

PMAP-CutDBP08217.

Expressioni

Tissue specificityi

Pancreas. Not detected in keratinocytes.1 Publication

Gene expression databases

BgeeiP08217.
GenevestigatoriP08217.

Interactioni

Subunit structurei

Interacts with CPA1.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000352639.

Structurei

3D structure databases

ProteinModelPortaliP08217.
SMRiP08217. Positions 29-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 267239Peptidase 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.
InParanoidiP08217.
KOiK01346.
OMAiAWWGSSV.
OrthoDBiEOG75B84T.
PhylomeDBiP08217.
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.

P08217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRTLLLSTL VAGALSCGDP TYPPYVTRVV GGEEARPNSW PWQVSLQYSS
60 70 80 90 100
NGKWYHTCGG SLIANSWVLT AAHCISSSRT YRVGLGRHNL YVAESGSLAV
110 120 130 140 150
SVSKIVVHKD WNSNQISKGN DIALLKLANP VSLTDKIQLA CLPPAGTILP
160 170 180 190 200
NNYPCYVTGW GRLQTNGAVP DVLQQGRLLV VDYATCSSSA WWGSSVKTSM
210 220 230 240 250
ICAGGDGVIS SCNGDSGGPL NCQASDGRWQ VHGIVSFGSR LGCNYYHKPS
260
VFTRVSNYID WINSVIANN
Length:269
Mass (Da):28,888
Last modified:August 1, 1988 - v1
Checksum:iA2E05143EFF4987C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021C → V in BAA00165 (PubMed:2834346).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti257 – 2571N → S.
Corresponds to variant rs2303193 [ dbSNP | Ensembl ].
VAR_051837

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16631 mRNA. Translation: AAA52374.1.
M16652 mRNA. Translation: AAA52380.1.
D00236 mRNA. Translation: BAA00165.1.
AK312198 mRNA. Translation: BAG35131.1.
AK056678 mRNA. Translation: BAG51782.1.
AL512883 Genomic DNA. Translation: CAC42421.1.
CH471167 Genomic DNA. Translation: EAW51727.1.
BC007031 mRNA. Translation: AAH07031.1.
CCDSiCCDS157.1.
PIRiB26823.
RefSeqiNP_254275.1. NM_033440.2.
UniGeneiHs.631866.

Genome annotation databases

EnsembliENST00000359621; ENSP00000352639; ENSG00000142615.
GeneIDi63036.
KEGGihsa:63036.
UCSCiuc001awk.3. human.

Polymorphism databases

DMDMi119255.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16631 mRNA. Translation: AAA52374.1.
M16652 mRNA. Translation: AAA52380.1.
D00236 mRNA. Translation: BAA00165.1.
AK312198 mRNA. Translation: BAG35131.1.
AK056678 mRNA. Translation: BAG51782.1.
AL512883 Genomic DNA. Translation: CAC42421.1.
CH471167 Genomic DNA. Translation: EAW51727.1.
BC007031 mRNA. Translation: AAH07031.1.
CCDSiCCDS157.1.
PIRiB26823.
RefSeqiNP_254275.1. NM_033440.2.
UniGeneiHs.631866.

3D structure databases

ProteinModelPortaliP08217.
SMRiP08217. Positions 29-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000352639.

Protein family/group databases

MEROPSiS01.155.

PTM databases

PhosphoSiteiP08217.

Polymorphism databases

DMDMi119255.

Proteomic databases

PaxDbiP08217.
PRIDEiP08217.

Protocols and materials databases

DNASUi63036.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359621; ENSP00000352639; ENSG00000142615.
GeneIDi63036.
KEGGihsa:63036.
UCSCiuc001awk.3. human.

Organism-specific databases

CTDi63036.
GeneCardsiGC01P015783.
HGNCiHGNC:24609. CELA2A.
MIMi609443. gene.
neXtProtiNX_P08217.
PharmGKBiPA165750794.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
InParanoidiP08217.
KOiK01346.
OMAiAWWGSSV.
OrthoDBiEOG75B84T.
PhylomeDBiP08217.
TreeFamiTF330455.

Miscellaneous databases

GeneWikiiCELA2A.
GenomeRNAii63036.
NextBioi65535.
PMAP-CutDBP08217.
PROiP08217.
SOURCEiSearch...

Gene expression databases

BgeeiP08217.
GenevestigatoriP08217.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of human pancreatic elastase 2 determined by sequence analysis of the cloned mRNA."
    Fletcher T.S., Shen W.F., Largman C.
    Biochemistry 26:7256-7261(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas."
    Kawashima I., Tani T., Shimoda K., Takiguchi Y.
    DNA 6:163-172(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning and expression in Escherichia coli of a cDNA encoding human pancreatic elastase 2."
    Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y., Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y., Tanaka J., Ikenaga H.
    J. Biochem. 102:1555-1563(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas and Prostate.
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  8. "Further studies on the human pancreatic binary complexes involving procarboxypeptidase A."
    Moulard M., Michon T., Kerfelec B., Chapus C.
    FEBS Lett. 261:179-183(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-50, INTERACTION WITH CPA1.
  9. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCEL2A_HUMAN
AccessioniPrimary (citable) accession number: P08217
Secondary accession number(s): B2R5I4, Q14243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 143 of the entry and version 1 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

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. 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.