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P00772

- CELA1_PIG

UniProt

P00772 - CELA1_PIG

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Protein

Chymotrypsin-like elastase family member 1

Gene
CELA1, ELA1
Organism
Sus scrofa (Pig)
Status
Reviewed - 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

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Charge relay system2 Publications
Metal bindingi85 – 851Calcium
Metal bindingi90 – 901Calcium; via carbonyl oxygen
Metal bindingi95 – 951Calcium
Active sitei119 – 1191Charge relay system1 Publication
Active sitei214 – 2141Charge relay system1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. exocrine pancreas development Source: Ensembl
  2. inflammatory response Source: Ensembl
  3. multicellular organism growth Source: Ensembl
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. pancreas morphogenesis Source: Ensembl
  6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. post-embryonic development Source: Ensembl
  8. regulation of cell differentiation Source: Ensembl
  9. regulation of cell proliferation Source: Ensembl
  10. Wnt signaling pathway Source: Ensembl
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
ProteomesiUP000008227: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Propeptidei17 – 2610Activation peptidePRO_0000027681
Chaini27 – 266240Chymotrypsin-like elastase family member 1PRO_0000027682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 721 Publication
Disulfide bondi153 ↔ 220
Disulfide bondi184 ↔ 200
Disulfide bondi210 ↔ 240

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP00772.

Expressioni

Tissue specificityi

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

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi1148920. 1 interaction.
DIPiDIP-378N.
IntActiP00772. 1 interaction.
MINTiMINT-1519161.
STRINGi9823.ENSSSCP00000000235.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 373
Beta strandi41 – 488
Beta strandi51 – 6212
Beta strandi65 – 684
Helixi70 – 734
Beta strandi74 – 763
Beta strandi79 – 846
Beta strandi87 – 904
Beta strandi96 – 10510
Beta strandi111 – 1133
Helixi114 – 1163
Beta strandi121 – 1277
Beta strandi132 – 1343
Beta strandi153 – 1586
Beta strandi160 – 1623
Beta strandi172 – 1754
Helixi181 – 1844
Turni187 – 1904
Helixi191 – 1933
Beta strandi198 – 2014
Beta strandi204 – 2063
Turni211 – 2155
Beta strandi217 – 2226
Beta strandi225 – 23410
Beta strandi239 – 2413
Beta strandi247 – 2515
Helixi252 – 2543
Helixi256 – 26510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772.
SMRiP00772. Positions 27-266.

Miscellaneous databases

EvolutionaryTraceiP00772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 264238Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00640000091262.
KOiK01326.
OMAiKSGSSWY.
OrthoDBiEOG7RRF7Z.
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.

P00772-1 [UniParc]FASTAAdd to Basket

« Hide

MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS    50
SWAHTCGGTL IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV 100
QKIVVHPYWN TDDVAAGYDI ALLRLAQSVT LNSYVQLGVL PRAGTILANN 150
SPCYITGWGL TRTNGQLAQT LQQAYLPTVD YAICSSSSYW GSTVKNSMVC 200
AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC NVTRKPTVFT 250
RVSAYISWIN NVIASN 266
Length:266
Mass (Da):28,821
Last modified:April 1, 1988 - v1
Checksum:iBF07D6855BB50FE2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921D → N AA sequence 1 Publication
Sequence conflicti126 – 1261A → G in BAA00118. 1 Publication
Sequence conflicti184 – 1841C → L in BAA00118. 1 Publication
Sequence conflicti204 – 2041D → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005655574.1.
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:
EMBL
GenBank
DDBJ
Links Updated
X04036 Transcribed RNA. Translation: CAA27670.1 .
D00160 mRNA. Translation: BAA00118.1 .
PIRi JS0013. ELPG.
RefSeqi NP_998988.1. NM_213823.1.
XP_005655631.1. XM_005655574.1.
UniGenei Ssc.5575.
Ssc.89635.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B0E X-ray 1.80 A 27-266 [» ]
1BMA X-ray 1.80 A 27-266 [» ]
1BTU X-ray 1.60 A 27-266 [» ]
1C1M X-ray 2.20 A 27-266 [» ]
1E34 X-ray 1.80 B 27-266 [» ]
1E35 X-ray 1.90 B 27-266 [» ]
1E36 X-ray 1.70 B 27-266 [» ]
1E37 X-ray 1.75 B 27-266 [» ]
1E38 X-ray 1.70 B 27-266 [» ]
1EAI X-ray 2.40 A/B 27-266 [» ]
1EAS X-ray 1.80 A 27-266 [» ]
1EAT X-ray 2.00 A 27-266 [» ]
1EAU X-ray 2.00 A 27-266 [» ]
1ELA X-ray 2.00 A 27-266 [» ]
1ELB X-ray 2.10 A 27-266 [» ]
1ELC X-ray 1.75 A 27-266 [» ]
1ELD X-ray 2.00 E 27-266 [» ]
1ELE X-ray 2.00 E 27-266 [» ]
1ELF X-ray 1.70 A 27-266 [» ]
1ELG X-ray 1.65 A 27-266 [» ]
1ESA X-ray 1.65 A 27-266 [» ]
1ESB X-ray 2.30 A 27-266 [» ]
1EST X-ray 2.50 A 27-266 [» ]
1FLE X-ray 1.90 E 27-266 [» ]
1FZZ X-ray 1.86 A 27-266 [» ]
1GVK X-ray 0.94 B 27-266 [» ]
1GWA X-ray 1.85 A 27-266 [» ]
1H9L X-ray 1.67 B 27-266 [» ]
1HAX X-ray 1.60 B 27-266 [» ]
1HAY X-ray 1.70 B 27-266 [» ]
1HAZ X-ray 1.40 B 27-266 [» ]
1HB0 X-ray 2.05 B 27-266 [» ]
1HV7 X-ray 1.70 A 27-266 [» ]
1INC X-ray 1.94 A 27-266 [» ]
1JIM X-ray 2.31 A 27-266 [» ]
1L0Z X-ray 1.50 A 27-266 [» ]
1L1G X-ray 1.50 A 27-266 [» ]
1LKA X-ray 1.70 A 27-266 [» ]
1LKB X-ray 1.70 A 27-266 [» ]
1LVY X-ray 1.87 A 27-266 [» ]
1MCV X-ray 1.80 A 27-266 [» ]
1MMJ X-ray 2.20 N 27-266 [» ]
1NES X-ray 1.65 E 27-266 [» ]
1OKX X-ray 2.80 A/B 27-266 [» ]
1QGF X-ray 1.70 A 27-266 [» ]
1QIX X-ray 1.90 B 27-266 [» ]
1QNJ X-ray 1.10 A 27-266 [» ]
1QR3 X-ray 1.60 E 27-266 [» ]
1UO6 X-ray 1.65 A 27-266 [» ]
1UVO X-ray 1.85 A 27-266 [» ]
1UVP X-ray 1.85 A 27-266 [» ]
2A7C X-ray 1.65 A 27-266 [» ]
2A7J X-ray 1.65 A 27-266 [» ]
2BB4 X-ray 1.60 A 27-266 [» ]
2BD2 X-ray 1.70 A 27-266 [» ]
2BD3 X-ray 1.60 A 27-266 [» ]
2BD4 X-ray 1.70 A 27-266 [» ]
2BD5 X-ray 1.80 A 27-266 [» ]
2BD7 X-ray 1.60 A 27-266 [» ]
2BD8 X-ray 1.70 A 27-266 [» ]
2BD9 X-ray 1.90 A 27-266 [» ]
2BDA X-ray 1.80 A 27-266 [» ]
2BDB X-ray 1.70 A 27-266 [» ]
2BDC X-ray 1.80 A 27-266 [» ]
2BLO X-ray 1.33 A 27-266 [» ]
2BLQ X-ray 1.33 A 27-266 [» ]
2CV3 X-ray 1.90 A 27-266 [» ]
2D26 X-ray 3.30 C 27-266 [» ]
2DE8 X-ray 1.50 A 27-266 [» ]
2DE9 X-ray 1.30 A 27-266 [» ]
2EST X-ray 2.50 E 27-266 [» ]
2FO9 X-ray 2.00 A 27-266 [» ]
2FOA X-ray 1.90 A 27-266 [» ]
2FOB X-ray 1.90 A 27-266 [» ]
2FOC X-ray 2.00 A 27-266 [» ]
2FOD X-ray 2.00 A 27-266 [» ]
2FOE X-ray 2.20 A 27-266 [» ]
2FOF X-ray 2.20 A 27-266 [» ]
2FOG X-ray 1.90 A 27-266 [» ]
2FOH X-ray 1.80 A 27-266 [» ]
2G4T X-ray 2.15 A 27-266 [» ]
2G4U X-ray 1.84 A 27-266 [» ]
2H1U X-ray 1.60 A 27-266 [» ]
2IOT X-ray 1.60 A 27-266 [» ]
2OQU X-ray 1.80 A 27-266 [» ]
2V0B X-ray 1.65 A 27-266 [» ]
2V35 X-ray 1.67 A 27-266 [» ]
3E3T X-ray 1.60 A 27-266 [» ]
3EST X-ray 1.65 A 27-266 [» ]
3HGN Other 1.65 A 27-266 [» ]
3HGP X-ray 0.94 A 27-266 [» ]
3MNB X-ray 1.20 A 27-266 [» ]
3MNC X-ray 1.12 A 27-266 [» ]
3MNS X-ray 1.50 A 27-266 [» ]
3MNX X-ray 1.39 A 27-266 [» ]
3MO3 X-ray 1.80 A 27-266 [» ]
3MO6 X-ray 1.66 A 27-266 [» ]
3MO9 X-ray 2.00 A 27-266 [» ]
3MOC X-ray 1.82 A 27-266 [» ]
3MTY X-ray 1.10 A 27-266 [» ]
3MU0 X-ray 1.40 A 27-266 [» ]
3MU1 X-ray 1.74 A 27-266 [» ]
3MU4 X-ray 1.10 A 27-266 [» ]
3MU5 X-ray 1.40 A 27-266 [» ]
3MU8 X-ray 1.55 A 27-266 [» ]
3ODD X-ray 1.10 A 27-266 [» ]
3ODF X-ray 1.10 A 27-266 [» ]
3UOU X-ray 2.00 A 27-266 [» ]
4EST X-ray 1.78 E 27-266 [» ]
4GVU X-ray 1.55 A 27-266 [» ]
5EST X-ray 2.09 E 27-266 [» ]
6EST X-ray 1.80 A 27-266 [» ]
7EST X-ray 1.80 E 27-266 [» ]
8EST X-ray 1.78 E 27-266 [» ]
9EST X-ray 1.90 A 27-266 [» ]
ProteinModelPortali P00772.
SMRi P00772. Positions 27-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1148920. 1 interaction.
DIPi DIP-378N.
IntActi P00772. 1 interaction.
MINTi MINT-1519161.
STRINGi 9823.ENSSSCP00000000235.

Chemistry

BindingDBi P00772.
ChEMBLi CHEMBL3517.

Protein family/group databases

MEROPSi S01.153.

Proteomic databases

PRIDEi P00772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000030908 ; ENSSSCP00000026330 ; ENSSSCG00000029782 .
GeneIDi 396766.
KEGGi ssc:396766.

Organism-specific databases

CTDi 1990.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00640000091262.
KOi K01326.
OMAi KSGSSWY.
OrthoDBi EOG7RRF7Z.
TreeFami TF330455.

Enzyme and pathway databases

BRENDAi 3.4.21.36. 6170.

Miscellaneous databases

EvolutionaryTracei P00772.

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

  1. "Isolation and expression in Escherichia coli of a cDNA clone encoding porcine pancreatic elastase."
    Shirasu Y., Yoshida H., Mikayama T., Matsuki S., Tanaka J., Ikenaga H.
    J. Biochem. 99:1707-1712(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region."
    Tani T., Kawashima I., Furukawa H., Ohmine T., Takiguchi Y.
    J. Biochem. 101:591-599(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Evidence for the amino acid sequence of porcine pancreatic elastase."
    Shotton D.M., Hartley B.S.
    Biochem. J. 131:643-675(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-266.
  4. "Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases."
    Shotton D.M., Hartley B.S.
    Nature 225:802-806(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-266.
  5. "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.
  6. "The atomic structure of crystalline porcine pancreatic elastase at 2.5-A resolution: comparisons with the structure of alpha-chymotrypsin."
    Sawyer L., Shotton D.M., Campbell J.W., Wendell P.L., Muirhead H., Watson H.C., Diamond R., Ladner R.C.
    J. Mol. Biol. 118:137-208(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  7. "Three-dimensional structure of tosyl-elastase."
    Shotton D.M., Watson H.C.
    Nature 225:811-816(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), ACTIVE SITE.
  8. "The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase."
    Huang K., Strynadka N.C., Bernard V.D., Peanasky R.J., James M.N.
    Structure 2:679-689(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH INHIBITOR.

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: June 11, 2014
This is version 147 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

External Data

Dasty 3

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