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CAN8_RAT
ID   CAN8_RAT                Reviewed;         703 AA.
AC   Q78EJ9; Q64698; Q78EJ8; Q8K407;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Calpain-8;
DE            EC=3.4.22.53;
DE   AltName: Full=Calpain large subunit 4;
DE   AltName: Full=New calpain 2;
DE            Short=nCL-2;
DE   AltName: Full=Stomach-specific M-type calpain;
GN   Name=Capn8; Synonyms=Cls4, Ncl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Gastric mucosa;
RX   PubMed=7690035; DOI=10.1016/s0021-9258(19)36540-8;
RA   Sorimachi H., Ishiura S., Suzuki K.;
RT   "A novel tissue-specific calpain species expressed predominantly in the
RT   stomach comprises two alternative splicing products with and without
RT   Ca(2+)-binding domain.";
RL   J. Biol. Chem. 268:19476-19482(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=12150941; DOI=10.1016/s0006-291x(02)00655-1;
RA   Duan W.R., Ito M., Lee E.J., Chien P.-Y., Jameson J.L.;
RT   "Estrogen regulates a tissue-specific calpain in the anterior pituitary.";
RL   Biochem. Biophys. Res. Commun. 295:261-266(2002).
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Involved in
CC       membrane trafficking in the gastric surface mucus cells (pit cells) and
CC       may involve the membrane trafficking of mucus cells via interactions
CC       with coat protein. Proteolytically cleaves the beta-subunit of coatomer
CC       complex (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds 2 calcium ions. {ECO:0000305};
CC   -!- SUBUNIT: Monomer and homooligomer. Interacts with COPS1/GPS1, COPB1,
CC       EYA2, NME2, NME4 and TOMM70 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7690035}. Golgi
CC       apparatus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=nCL-2;
CC         IsoId=Q78EJ9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Calpain 8b, nCL-2';
CC         IsoId=Q78EJ9-2; Sequence=VSP_035308, VSP_035309;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the stomach. Localizes
CC       strictly to the surface mucus cells in the gastric epithelium and the
CC       mucus-secreting goblet cells in the duodenum. Detected in the pituitary
CC       after estrogen stimulation. {ECO:0000269|PubMed:12150941,
CC       ECO:0000269|PubMed:7690035}.
CC   -!- DOMAIN: The domain III mediates oligomerization. {ECO:0000250}.
CC   -!- PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which gives
CC       rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the
CC       EF-hand 2 domain and from Ala-6 to the beginning of domain III.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; D14478; BAA03369.1; -; Transcribed_RNA.
DR   EMBL; D14479; BAA03370.1; -; mRNA.
DR   EMBL; D14480; BAA03371.1; -; mRNA.
DR   EMBL; AF514419; AAM94284.1; -; Genomic_DNA.
DR   PIR; A48764; A48764.
DR   RefSeq; NP_579843.2; NM_133309.2. [Q78EJ9-1]
DR   AlphaFoldDB; Q78EJ9; -.
DR   SMR; Q78EJ9; -.
DR   STRING; 10116.ENSRNOP00000062898; -.
DR   MEROPS; C02.007; -.
DR   iPTMnet; Q78EJ9; -.
DR   PhosphoSitePlus; Q78EJ9; -.
DR   PaxDb; Q78EJ9; -.
DR   Ensembl; ENSRNOT00000004649; ENSRNOP00000004649; ENSRNOG00000003468. [Q78EJ9-2]
DR   Ensembl; ENSRNOT00000067005; ENSRNOP00000062898; ENSRNOG00000003468. [Q78EJ9-1]
DR   GeneID; 170808; -.
DR   KEGG; rno:170808; -.
DR   UCSC; RGD:620085; rat. [Q78EJ9-1]
DR   CTD; 388743; -.
DR   RGD; 620085; Capn8.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000160090; -.
DR   HOGENOM; CLU_010982_0_1_1; -.
DR   InParanoid; Q78EJ9; -.
DR   OMA; IGEPCCT; -.
DR   OrthoDB; 704215at2759; -.
DR   PhylomeDB; Q78EJ9; -.
DR   TreeFam; TF314748; -.
DR   Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR   PRO; PR:Q78EJ9; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003468; Expressed in stomach and 8 other tissues.
DR   Genevisible; Q78EJ9; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:1990092; P:calcium-dependent self proteolysis; ISO:RGD.
DR   GO; GO:0007586; P:digestion; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00214; Calpain_III; 1.
DR   CDD; cd00044; CysPc; 1.
DR   InterPro; IPR033883; C2_III.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR029543; CAPN8.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183:SF374; PTHR10183:SF374; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Autocatalytic cleavage; Calcium; Cytoplasm;
KW   Golgi apparatus; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Repeat; Thiol protease.
FT   CHAIN           1..703
FT                   /note="Calpain-8"
FT                   /id="PRO_0000349282"
FT   DOMAIN          45..344
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          532..566
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          575..608
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          605..640
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          670..703
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          355..512
FT                   /note="Domain III"
FT   REGION          513..531
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          532..703
FT                   /note="Domain IV"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   BINDING         588
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         590
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         592
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         594
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         599
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         618
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         620
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         624
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         629
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         380..381
FT                   /note="TY -> SS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7690035"
FT                   /id="VSP_035308"
FT   VAR_SEQ         382..703
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7690035"
FT                   /id="VSP_035309"
FT   CONFLICT        103
FT                   /note="G -> V (in Ref. 1; BAA03369)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   703 AA;  79555 MW;  C0688B055FC0D6EC CRC64;
     MAALAAGVSK QRAVAEGLGS NQNAVKYLGQ DFETLRKQCL NSGVLFKDPE FPACPSALGY
     KDLGPGSPDT QGIVWKRPTE LCPNPQFIVG GATRTDIRQG GLGDCWLLAA IASLTLNEKL
     LYRVLPRDQS FQKDYAGIFH FQFWQYGEWV EVVIDDRLPT KNGQLLFLHS EEGNEFWSAL
     LEKAYAKLNG SYEALVGGST IEGFEDFTGG ISEFYDLKKP PENLYYIIQK ALRKGSLLGC
     SIDVSTAAEA EATTRQKLVK GHAYSVTGVE EVNFHGRPEK LIRLRNPWGE VEWSGAWSDN
     APEWNYIDPR RKEELDKKAE DGEFWMSFSD FLKQYSRLEI CNLSPDSLSS EEIHKWNLVL
     FNGRWTRGST AGGCLNYPGT YWTNPQFKIH LDEVDEDQEE GTSEPCCTVL LGLMQKNRRR
     QKRIGQGMLS IGYAVYQIPK ELESHTDAHL GRDFFLGRQP STCSSTYMNL REVSSRVRLP
     PGQYLVVPST FEPFKDGDFC LRVFSEKKAK ALEIGDTVSG HPHEPHPRDM DEEDEHVRSL
     FEEFVGKDSE ISANQLKRVL NEVLSKRTDM KFDGFNINTC REMISLLDSD GTGSLGPMEF
     KTLWLKIRTY LEIFQEMDHN HVGTIEAHEM RTALKKAGFT LNNQVQQTIA MRYACSKLGV
     DFNGFVACMI RLETLFKLFR LLDKDQNGIV QLSLAEWLCC VLV
 
 
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