Skip Header

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

P00772

- CELA1_PIG

UniProt

P00772 - CELA1_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Chymotrypsin-like elastase family member 1

Gene

CELA1

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

Ca2+Note: Binds 1 Ca(2+) 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. 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Propeptidei17 – 2610Activation peptide2 PublicationsPRO_0000027681
Chaini27 – 266240Chymotrypsin-like elastase family member 1PRO_0000027682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 721 PublicationPROSITE-ProRule annotation
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 – 373Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 6212Combined sources
Beta strandi65 – 684Combined sources
Helixi70 – 734Combined sources
Beta strandi74 – 763Combined sources
Beta strandi79 – 846Combined sources
Beta strandi87 – 904Combined sources
Beta strandi96 – 10510Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 1163Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi172 – 1754Combined sources
Helixi181 – 1844Combined sources
Turni187 – 1904Combined sources
Helixi191 – 1933Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi204 – 2063Combined sources
Turni211 – 2155Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi225 – 23410Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi247 – 2515Combined sources
Helixi252 – 2543Combined sources
Helixi256 – 26510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 264238Peptidase 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.
InParanoidiP00772.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921D → N AA sequence (PubMed:4578945)Curated
Sequence conflicti126 – 1261A → G in BAA00118. (PubMed:3648024)Curated
Sequence conflicti184 – 1841C → L in BAA00118. (PubMed:3648024)Curated
Sequence conflicti204 – 2041D → N AA sequence (PubMed:4578945)Curated

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_005655574.1.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000119027.
InParanoidi P00772.
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: November 26, 2014
This is version 150 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