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NKX61_RAT
ID   NKX61_RAT               Reviewed;         365 AA.
AC   O35762;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Homeobox protein Nkx-6.1;
DE   AltName: Full=Homeobox protein NK-6 homolog A;
GN   Name=Nkx6-1; Synonyms=Nkx6.1, Nkx6a;
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].
RC   STRAIN=Wistar; TISSUE=Pancreatic islet;
RX   PubMed=10567713; DOI=10.1016/s0014-5793(99)01436-2;
RA   Jorgensen M.C., Vestergard Petersen H., Ericson J., Madsen O.D., Serup P.;
RT   "Cloning and DNA-binding properties of the rat pancreatic beta-cell-
RT   specific factor Nkx6.1.";
RL   FEBS Lett. 461:287-294(1999).
CC   -!- FUNCTION: Transcription factor which binds to specific A/T-rich DNA
CC       sequences in the promoter regions of a number of genes. Involved in the
CC       development of insulin-producing beta cells in the islets of Langerhans
CC       at the secondary transition (By similarity). Together with NKX2-2 and
CC       IRX3 acts to restrict the generation of motor neurons to the
CC       appropriate region of the neural tube. Belongs to the class II proteins
CC       of neuronal progenitor factors, which are induced by SHH signals (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q99MA9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99MA9}.
CC   -!- TISSUE SPECIFICITY: Pancreatic beta cells.
CC   -!- DOMAIN: The C-terminal domain contributes to sequence-specific DNA-
CC       binding.
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DR   EMBL; AF004431; AAB61665.1; -; mRNA.
DR   RefSeq; NP_113925.1; NM_031737.1.
DR   AlphaFoldDB; O35762; -.
DR   SMR; O35762; -.
DR   STRING; 10116.ENSRNOP00000002928; -.
DR   PhosphoSitePlus; O35762; -.
DR   PaxDb; O35762; -.
DR   Ensembl; ENSRNOT00000002928; ENSRNOP00000002928; ENSRNOG00000002149.
DR   GeneID; 65193; -.
DR   KEGG; rno:65193; -.
DR   CTD; 4825; -.
DR   RGD; 69318; Nkx6-1.
DR   eggNOG; KOG0847; Eukaryota.
DR   GeneTree; ENSGT00940000160897; -.
DR   HOGENOM; CLU_064820_0_0_1; -.
DR   InParanoid; O35762; -.
DR   OMA; ALYWPAN; -.
DR   OrthoDB; 1263401at2759; -.
DR   PhylomeDB; O35762; -.
DR   TreeFam; TF327063; -.
DR   PRO; PR:O35762; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002149; Expressed in esophagus and 2 other tissues.
DR   Genevisible; O35762; RN.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; IMP:RGD.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD.
DR   GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR   GO; GO:0021953; P:central nervous system neuron differentiation; ISO:RGD.
DR   GO; GO:0031018; P:endocrine pancreas development; ISO:RGD.
DR   GO; GO:0045686; P:negative regulation of glial cell differentiation; ISO:RGD.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0022008; P:neurogenesis; IMP:RGD.
DR   GO; GO:0001764; P:neuron migration; IEA:InterPro.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR   GO; GO:0003310; P:pancreatic A cell differentiation; IEA:Ensembl.
DR   GO; GO:0045687; P:positive regulation of glial cell differentiation; ISO:RGD.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030516; P:regulation of axon extension; ISO:RGD.
DR   GO; GO:2001222; P:regulation of neuron migration; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0003323; P:type B pancreatic cell development; IEP:RGD.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IDA:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   InterPro; IPR000047; HTH_motif.
DR   InterPro; IPR033630; NKX-6.1.
DR   PANTHER; PTHR24340:SF31; PTHR24340:SF31; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00031; HTHREPRESSR.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Homeobox; Methylation; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..365
FT                   /note="Homeobox protein Nkx-6.1"
FT                   /id="PRO_0000048954"
FT   DNA_BIND        237..296
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          35..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..269
FT                   /note="Repressor domain"
FT                   /evidence="ECO:0000250"
FT   REGION          295..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..365
FT                   /note="Involved in DNA-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        49..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         190
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P78426"
SQ   SEQUENCE   365 AA;  37689 MW;  C4AAB702D051F1F2 CRC64;
     MLAVGAMEGP RQSAFLLSSP PLAALHSMAE MKTPLYPAAY PPLPTGPPSS SSSSSSSSSP
     SPPLGAHNPG GLKPPAAGGL SSLGSPPQQL SAATPHGIND ILSRPSMPVA SGAALPSASP
     SGSSSSSSSS ASATSASAAA AAAAAAAAAA ASSPAGLLAG LPRFSSLSPP PPPPGLYFSP
     SAAAVAAVGR YPKPLAELPG RTPIFWPGVM QSPPWRDARL ACTPHQGSIL LDKDGKRKHT
     RPTFSGQQIF ALEKTFEQTK YLAGPERARL AYSLGMTESQ VKVWFQNRRT KWRKKHAAEM
     ATAKKKQDSE TERLKGTSEN EEDDDDYNKP LDPNSDDEKI TQLLKKHKSS GGSLLLHASE
     AEGSS
 
 
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