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P00772

- CELA1_PIG

UniProt

P00772 - CELA1_PIG

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
    • BLAST
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    • Comment

    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

    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

    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 – 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.
    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.
    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

    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:
    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: October 1, 2014
    This is version 148 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