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P08217

- CEL2A_HUMAN

UniProt

P08217 - CEL2A_HUMAN

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Protein
Chymotrypsin-like elastase family member 2A
Gene
CELA2A, ELA2A
Organism
Homo sapiens (Human)
Status
Reviewed - 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 system By similarity
Active sitei121 – 1211Charge relay system By similarity
Active sitei216 – 2161Charge relay system By 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: 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 – 1616
Add
BLAST
Propeptidei17 – 2812Activation peptide
PRO_0000027693Add
BLAST
Chaini29 – 269241Chymotrypsin-like elastase family member 2A
PRO_0000027694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74 By similarity
Disulfide bondi155 ↔ 222 By similarity
Disulfide bondi186 ↔ 202 By similarity
Disulfide bondi212 ↔ 243 By similarity

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 267239Peptidase S1
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
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

MIRTLLLSTL VAGALSCGDP TYPPYVTRVV GGEEARPNSW PWQVSLQYSS    50
NGKWYHTCGG SLIANSWVLT AAHCISSSRT YRVGLGRHNL YVAESGSLAV 100
SVSKIVVHKD WNSNQISKGN DIALLKLANP VSLTDKIQLA CLPPAGTILP 150
NNYPCYVTGW GRLQTNGAVP DVLQQGRLLV VDYATCSSSA WWGSSVKTSM 200
ICAGGDGVIS SCNGDSGGPL NCQASDGRWQ VHGIVSFGSR LGCNYYHKPS 250
VFTRVSNYID WINSVIANN 269
Length:269
Mass (Da):28,888
Last modified:August 1, 1988 - v1
Checksum:iA2E05143EFF4987C
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021C → V in BAA00165. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS157.1.
PIRi B26823.
RefSeqi NP_254275.1. NM_033440.2.
UniGenei Hs.631866.

3D structure databases

ProteinModelPortali P08217.
SMRi P08217. Positions 29-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000352639.

Chemistry

BindingDBi P08217.

Protein family/group databases

MEROPSi S01.155.

PTM databases

PhosphoSitei P08217.

Polymorphism databases

DMDMi 119255.

Proteomic databases

PaxDbi P08217.
PRIDEi P08217.

Protocols and materials databases

DNASUi 63036.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359621 ; ENSP00000352639 ; ENSG00000142615 .
GeneIDi 63036.
KEGGi hsa:63036.
UCSCi uc001awk.3. human.

Organism-specific databases

CTDi 63036.
GeneCardsi GC01P015783.
HGNCi HGNC:24609. CELA2A.
MIMi 609443. gene.
neXtProti NX_P08217.
PharmGKBi PA165750794.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
KOi K01346.
OMAi AWWGSSV.
OrthoDBi EOG75B84T.
PhylomeDBi P08217.
TreeFami TF330455.

Miscellaneous databases

GeneWikii CELA2A.
GenomeRNAii 63036.
NextBioi 65535.
PMAP-CutDB P08217.
PROi P08217.
SOURCEi Search...

Gene expression databases

Bgeei P08217.
Genevestigatori P08217.

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. "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(1987) [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(1987) [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(1987) [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(2004) [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(2006) [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(2004) [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(1990) [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(2000) [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: July 9, 2014
This is version 139 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

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