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ANKR1_RAT
ID   ANKR1_RAT               Reviewed;         319 AA.
AC   Q8R560; Q9Z1F0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Ankyrin repeat domain-containing protein 1;
DE   AltName: Full=Cardiac adriamycin-responsive protein;
DE   AltName: Full=Cardiac ankyrin repeat protein;
GN   Name=Ankrd1; Synonyms=Carp;
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], INTERACTION WITH YBX1, SUBCELLULAR LOCATION,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=9043061; DOI=10.1242/dev.124.4.793;
RA   Zou Y., Evans S., Chen J., Kuo H.-C., Harvey R.P., Chien K.R.;
RT   "CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5
RT   homeobox gene pathway.";
RL   Development 124:793-804(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY DOXORUBICIN, SUBCELLULAR LOCATION,
RP   AND FUNCTION.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9278441; DOI=10.1074/jbc.272.36.22800;
RA   Jeyaseelan R., Poizat C., Baker R.K., Abdishoo S., Isterabadi L.B.,
RA   Lyons G.E., Kedes L.;
RT   "A novel cardiac-restricted target for doxorubicin. CARP, a nuclear
RT   modulator of gene expression in cardiac progenitor cells and
RT   cardiomyocytes.";
RL   J. Biol. Chem. 272:22800-22808(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play an important role in endothelial cell activation.
CC       May act as a nuclear transcription factor that negatively regulates the
CC       expression of cardiac genes. {ECO:0000269|PubMed:9043061,
CC       ECO:0000269|PubMed:9278441}.
CC   -!- SUBUNIT: Interacts with TTN/titin (By similarity). Interacts with YBX1.
CC       {ECO:0000250, ECO:0000269|PubMed:9043061}.
CC   -!- INTERACTION:
CC       Q8R560; Q5VU43-11: PDE4DIP; Xeno; NbExp=2; IntAct=EBI-10817505, EBI-10769071;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9043061,
CC       ECO:0000269|PubMed:9278441}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, cardiac muscle.
CC       {ECO:0000269|PubMed:9043061}.
CC   -!- INDUCTION: Down-regulated by doxorubicin (adriamycin), in vitro.
CC       {ECO:0000269|PubMed:9278441}.
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DR   EMBL; L81174; AAL77519.1; -; mRNA.
DR   EMBL; U50736; AAD10401.1; -; mRNA.
DR   EMBL; BC072699; AAH72699.1; -; mRNA.
DR   RefSeq; NP_037352.1; NM_013220.1.
DR   AlphaFoldDB; Q8R560; -.
DR   SMR; Q8R560; -.
DR   IntAct; Q8R560; 1.
DR   STRING; 10116.ENSRNOP00000025258; -.
DR   PaxDb; Q8R560; -.
DR   PRIDE; Q8R560; -.
DR   Ensembl; ENSRNOT00000108356; ENSRNOP00000083877; ENSRNOG00000018598.
DR   GeneID; 27064; -.
DR   KEGG; rno:27064; -.
DR   UCSC; RGD:61989; rat.
DR   CTD; 27063; -.
DR   RGD; 61989; Ankrd1.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000153956; -.
DR   HOGENOM; CLU_000134_11_1_1; -.
DR   InParanoid; Q8R560; -.
DR   OMA; HSTALHW; -.
DR   OrthoDB; 1514637at2759; -.
DR   PhylomeDB; Q8R560; -.
DR   TreeFam; TF331650; -.
DR   PRO; PR:Q8R560; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018598; Expressed in heart and 17 other tissues.
DR   Genevisible; Q8R560; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR   GO; GO:0030016; C:myofibril; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR   GO; GO:0002039; F:p53 binding; ISO:RGD.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0031432; F:titin binding; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR   GO; GO:0003712; F:transcription coregulator activity; TAS:RGD.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR   GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR   GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..319
FT                   /note="Ankyrin repeat domain-containing protein 1"
FT                   /id="PRO_0000240483"
FT   REPEAT          152..181
FT                   /note="ANK 1"
FT   REPEAT          185..214
FT                   /note="ANK 2"
FT   REPEAT          218..247
FT                   /note="ANK 3"
FT   REPEAT          251..280
FT                   /note="ANK 4"
FT   REPEAT          284..315
FT                   /note="ANK 5"
FT   COILED          55..89
FT                   /evidence="ECO:0000255"
FT   CONFLICT        287
FT                   /note="T -> I (in Ref. 2; AAD10401)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  36064 MW;  E760BF7BFD6049E0 CRC64;
     MMVFRVEELV TGKKNSNGSS GEFLPGEFRN GEYEAAVALE KQEDLKTLPA NSVNLGEEQR
     KSEKVREAEL KKKKLEQRSK LENLEDLEII VQLKKRKKYK KTKVPVVKEP EPEIITEPVD
     VPRFLKAALE NKLPVVEKFL SDKNSPDVCD EYKRTALHRA CLEGHLAIVE KLMEAGAQIE
     FRDMLESTAI HWACRGGNLD VLKLLLNKGA KISARDKLLS TALHVAVRTG HYECAEHLIA
     CEADLNAKDR EGDTPLHDAV RLNRYKMIRL LMTFGADLNV KNCAGKTPMD LVLHWQNGTK
     AIFDSLKENA YKNSRIATF
 
 
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