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Protein

Chymotrypsin-like elastase family member 1

Gene

CELA1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei71Charge relay system2 Publications1
Metal bindingi85Calcium1
Metal bindingi90Calcium; via carbonyl oxygen1
Metal bindingi95Calcium1
Active sitei119Charge relay system1 Publication1
Active sitei214Charge relay system1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.36. 6170.

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
Gene namesi
Name:CELA1
Synonyms:ELA1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3517.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Add BLAST16
PropeptideiPRO_000002768117 – 26Activation peptide2 Publications10
ChainiPRO_000002768227 – 266Chymotrypsin-like elastase family member 1Add BLAST240

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 72PROSITE-ProRule annotation1 Publication
Disulfide bondi153 ↔ 220
Disulfide bondi184 ↔ 200
Disulfide bondi210 ↔ 240

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00772.
PRIDEiP00772.

Expressioni

Tissue specificityi

Pancreas. Basal layers of the epidermis, hair follicle and sebaceous gland epithelia (at protein level).1 Publication

Gene expression databases

GenevisibleiP00772. SS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SERPINA1P010092EBI-986248,EBI-986224From a different organism.

Protein-protein interaction databases

BioGridi1148920. 1 interactor.
DIPiDIP-378N.
IntActiP00772. 1 interactor.
MINTiMINT-1519161.
STRINGi9823.ENSSSCP00000026330.

Chemistry databases

BindingDBiP00772.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni35 – 37Combined sources3
Beta strandi41 – 48Combined sources8
Beta strandi51 – 62Combined sources12
Beta strandi65 – 68Combined sources4
Helixi70 – 73Combined sources4
Beta strandi74 – 76Combined sources3
Beta strandi79 – 84Combined sources6
Beta strandi87 – 90Combined sources4
Beta strandi96 – 105Combined sources10
Beta strandi111 – 113Combined sources3
Helixi114 – 116Combined sources3
Beta strandi121 – 127Combined sources7
Beta strandi132 – 134Combined sources3
Beta strandi153 – 158Combined sources6
Beta strandi160 – 162Combined sources3
Beta strandi172 – 175Combined sources4
Helixi181 – 184Combined sources4
Turni187 – 190Combined sources4
Helixi191 – 193Combined sources3
Beta strandi198 – 201Combined sources4
Beta strandi204 – 206Combined sources3
Turni211 – 215Combined sources5
Beta strandi217 – 222Combined sources6
Beta strandi225 – 234Combined sources10
Beta strandi239 – 242Combined sources4
Beta strandi247 – 251Combined sources5
Helixi252 – 254Combined sources3
Helixi256 – 264Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
3UOUX-ray2.00A27-266[»]
4ESTX-ray1.78E27-266[»]
4GVUX-ray1.55A27-266[»]
4YM9X-ray1.80A27-266[»]
5AVDX-ray0.86A27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772.
SMRiP00772.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 264Peptidase S1PROSITE-ProRule annotationAdd BLAST238

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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119027.
InParanoidiP00772.
KOiK01326.
OMAiDYAICSS.
OrthoDBiEOG091G0DF7.
TreeFamiTF330455.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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.

P00772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS
60 70 80 90 100
SWAHTCGGTL IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV
110 120 130 140 150
QKIVVHPYWN TDDVAAGYDI ALLRLAQSVT LNSYVQLGVL PRAGTILANN
160 170 180 190 200
SPCYITGWGL TRTNGQLAQT LQQAYLPTVD YAICSSSSYW GSTVKNSMVC
210 220 230 240 250
AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC NVTRKPTVFT
260
RVSAYISWIN NVIASN
Length:266
Mass (Da):28,821
Last modified:April 1, 1988 - v1
Checksum:iBF07D6855BB50FE2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti92D → N AA sequence (PubMed:4578945).Curated1
Sequence conflicti126A → G in BAA00118 (PubMed:3648024).Curated1
Sequence conflicti184C → L in BAA00118 (PubMed:3648024).Curated1
Sequence conflicti204D → N AA sequence (PubMed:4578945).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04036 Transcribed RNA. Translation: CAA27670.1.
D00160 mRNA. Translation: BAA00118.1.
PIRiJS0013. ELPG.
RefSeqiNP_998988.1. NM_213823.1.
XP_005655631.1. XM_005655574.2.
UniGeneiSsc.5575.
Ssc.89635.

Genome annotation databases

EnsembliENSSSCT00000030908; ENSSSCP00000026330; ENSSSCG00000029782.
GeneIDi396766.
KEGGissc:396766.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04036 Transcribed RNA. Translation: CAA27670.1.
D00160 mRNA. Translation: BAA00118.1.
PIRiJS0013. ELPG.
RefSeqiNP_998988.1. NM_213823.1.
XP_005655631.1. XM_005655574.2.
UniGeneiSsc.5575.
Ssc.89635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
3UOUX-ray2.00A27-266[»]
4ESTX-ray1.78E27-266[»]
4GVUX-ray1.55A27-266[»]
4YM9X-ray1.80A27-266[»]
5AVDX-ray0.86A27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772.
SMRiP00772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1148920. 1 interactor.
DIPiDIP-378N.
IntActiP00772. 1 interactor.
MINTiMINT-1519161.
STRINGi9823.ENSSSCP00000026330.

Chemistry databases

BindingDBiP00772.
ChEMBLiCHEMBL3517.

Protein family/group databases

MEROPSiS01.153.

Proteomic databases

PaxDbiP00772.
PRIDEiP00772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000030908; ENSSSCP00000026330; ENSSSCG00000029782.
GeneIDi396766.
KEGGissc:396766.

Organism-specific databases

CTDi1990.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119027.
InParanoidiP00772.
KOiK01326.
OMAiDYAICSS.
OrthoDBiEOG091G0DF7.
TreeFamiTF330455.

Enzyme and pathway databases

BRENDAi3.4.21.36. 6170.

Miscellaneous databases

EvolutionaryTraceiP00772.
PROiP00772.

Gene expression databases

GenevisibleiP00772. SS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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...

Entry informationi

Entry nameiCELA1_PIG
AccessioniPrimary (citable) accession number: P00772
Secondary accession number(s): Q29625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.