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IBTK_XENLA
ID   IBTK_XENLA              Reviewed;        1339 AA.
AC   Q6NRS1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Inhibitor of Bruton tyrosine kinase;
DE            Short=IBtk;
GN   Name=ibtk;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as an inhibitor of BTK tyrosine kinase activity, thereby
CC       playing a role in B-cell development. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
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DR   EMBL; BC070653; AAH70653.1; -; mRNA.
DR   RefSeq; NP_001084927.1; NM_001091458.1.
DR   AlphaFoldDB; Q6NRS1; -.
DR   SMR; Q6NRS1; -.
DR   MaxQB; Q6NRS1; -.
DR   DNASU; 431983; -.
DR   GeneID; 431983; -.
DR   KEGG; xla:431983; -.
DR   CTD; 431983; -.
DR   Xenbase; XB-GENE-5756000; ibtk.L.
DR   OrthoDB; 94875at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 431983; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 2.130.10.30; -; 1.
DR   Gene3D; 3.30.710.10; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00651; BTB; 2.
DR   Pfam; PF00415; RCC1; 3.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00225; BTB; 2.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   SUPFAM; SSF54695; SSF54695; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50097; BTB; 2.
DR   PROSITE; PS50012; RCC1_3; 3.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cytoplasm; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..1339
FT                   /note="Inhibitor of Bruton tyrosine kinase"
FT                   /id="PRO_0000280278"
FT   REPEAT          51..81
FT                   /note="ANK 1"
FT   REPEAT          86..115
FT                   /note="ANK 2"
FT   REPEAT          119..154
FT                   /note="ANK 3"
FT   REPEAT          142..195
FT                   /note="RCC1 1"
FT   REPEAT          196..247
FT                   /note="RCC1 2"
FT   REPEAT          249..302
FT                   /note="RCC1 3"
FT   DOMAIN          555..636
FT                   /note="BTB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          758..826
FT                   /note="BTB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          685..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1058..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1208..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1339 AA;  149341 MW;  483977396F30E5B4 CRC64;
     MERVWPECTT RCRSLQHALD VISVVTRASE QHIKVFLSSY CCNAVTLKDD FGRNATHIAA
     SCGKKNVLDW LITGKGVDLA VKDKESGWTA LHRSIFYGHI DCALSLLKHG SNLYIQDKDG
     YTPLDLVMKD RPPHIVFKTS DPTELYTWGD NVNFTLGHGT QQSKHHPELV EMFPRSGVYI
     KQMVLCKFHS VFLSQKGQVY TCGHGQGGRL GHGDELTCLV PRLVEGLRGH PCTQVAGAKD
     HTVVLTEDGY VYTFGLNTFH QLGIQPPPPN SNVPRQIQAK TMKGKTVLGV AAGRFHTVLW
     TKDAVYTVGL NGGQLGYLQD PNGEKFVSCP RQVSALHHKD INITLVSASD GATVCVSERG
     DIYLLSEYQC KKLASKQLNL KKVLVSGGIL EHKAAPEHLK ENGGQPASVF ALDQAGRVFC
     WKSPGSSLKQ CWWVYGRQLF MSDVALNKNE IMFVTQDGEG FTGKWMLEKK KKENTISNIM
     CHSDSQNVYE KISMQKLPFV HRAVSVATDP SGCNFAVLQS DPKTSLFEVP SVSSSVFAED
     FEKLLNEANE TDSIHDVTFQ VGTKIFPAHK YILALRCDFF SKLFSSGEIN SLDFPEVHQK
     GEDAAGCDLF VIEKIPPELF SHVLQFIYSD TCDMLLQGHK PKLWHKEENE NTIICNFQKM
     GFREDIEGKS AYEVYKNSRI CAENEKQKGK TKQSKKTRSI GDETSPVKML QNTAKKFGLS
     NLSSRLDGVR YENGRINVFH KKSENKLRFN QKKCSSHYDV MMKSEDGKEF HCHKCVLCAR
     LEYFNSMLSS SWIEASCCSQ LEMPIHSDVL QVILDYIYTD EVLTVKESAN VEFVCNVLVI
     ADQLLIVRLK EICEVTIAER ITLKNAAELL EFAALYNADQ LKLSCLQFVG LNMGALLEAR
     SLDVLSDDVL KDLSEAYRKM IPSMNKRIIT PYLDGPDISI LQSEDIESLI SVQDDIYSYQ
     ITQEATLKKS KAKPKKKQRK RLDSSGGYNL SDIIQSPTST GFVKPEKTNS VESLQDLLTS
     DSEGSFVGAS SPRDLQSPDL FPVFTHETKE TICVERNRSS PPVANGAAST KMPIPTTSSP
     KAIPMSRITP STSPNWVAMP CSPASPVTMD LRAIMELEEN IQKCGAMPKL NAGGTKPGTH
     VMKLSQKQRK MMAMSSKESN NENKPAKVTV APTTIKSPAK TWAAAFHLGE NKSFRDLLLE
     EKQSVTSFPS LSSDVKKSKH TEELDPSELA RRPSGTLNQE AKLKCDVPNQ DNSNPWHLTL
     SKNNASSAPV TFTAIVEEEE KQEAALIRSR EKPLALIQIE ERAIQDLLLH YQAIDNPEEY
     ITIERAAQIP MATPMWNKH
 
 
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