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CELA1_BOVIN
ID   CELA1_BOVIN             Reviewed;         266 AA.
AC   Q28153; A6QPW5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Chymotrypsin-like elastase family member 1;
DE            EC=3.4.21.36;
DE   AltName: Full=Elastase I;
DE   AltName: Full=Elastase-1;
DE   Flags: Precursor;
GN   Name=CELA1; Synonyms=ELA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein-Friesian; TISSUE=Pancreas;
RX   PubMed=9418008; DOI=10.1016/s0305-0491(97)00031-x;
RA   Gestin M., le Huerou-Luron I., Wicker-Planquart C., le Drean G.,
RA   Chaix J.-C., Puigserver A., Guilloteau P.;
RT   "Bovine pancreatic preproelastases I and II: comparison of nucleotide and
RT   amino acid sequences and tissue specific expression.";
RL   Comp. Biochem. Physiol. 118B:181-187(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pancreas;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts upon elastin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins, including elastin. Preferential
CC         cleavage: Ala-|-Xaa.; EC=3.4.21.36;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; M80838; AAA98525.1; -; mRNA.
DR   EMBL; BC149525; AAI49526.1; -; mRNA.
DR   RefSeq; NP_776473.1; NM_174048.2.
DR   RefSeq; XP_005206313.1; XM_005206256.3.
DR   AlphaFoldDB; Q28153; -.
DR   SMR; Q28153; -.
DR   BioGRID; 158500; 1.
DR   STRING; 9913.ENSBTAP00000011718; -.
DR   BindingDB; Q28153; -.
DR   MEROPS; S01.153; -.
DR   PaxDb; Q28153; -.
DR   Ensembl; ENSBTAT00000011718; ENSBTAP00000011718; ENSBTAG00000008900.
DR   GeneID; 281139; -.
DR   KEGG; bta:281139; -.
DR   CTD; 1990; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008900; -.
DR   VGNC; VGNC:27166; CELA1.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234528; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q28153; -.
DR   OMA; KQGCNVS; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF330455; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000008900; Expressed in abomasum and 97 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0060309; P:elastin catabolic process; IEA:Ensembl.
DR   GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0061113; P:pancreas morphogenesis; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0045595; P:regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0048771; P:tissue remodeling; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   PROPEP          17..26
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027671"
FT   CHAIN           27..266
FT                   /note="Chymotrypsin-like elastase family member 1"
FT                   /id="PRO_0000027672"
FT   DOMAIN          27..264
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        71
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        153..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        184..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        210..240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   266 AA;  28518 MW;  927E29C69BAF67E7 CRC64;
     MLRLLVFTSL VLYGHSTQDF PETNARVVGG TAVSKNSWPS QISLQYKSGS SWYHTCGGTL
     IKQKWVMTAA HCVDSQMTFR VVLGDHNLSQ NDGTEQYISV QKIVVHPSWN SNNVAAGYDI
     AVLRLAQSAT LNSYVQLGVL PQSGTILANN TPCYITGWGR TKTNGQLAQT LQQAYLPSVD
     YATCSSSSYW GSTVKTTMVC AGGDGVRAGC QGDSGGPLHC LVNGQYAVHG VTSFVSSLGC
     NVSKKPTVFT RVSAYISWIN NAIASN
 
 
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