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KDISB_DANRE
ID   KDISB_DANRE             Reviewed;        1680 AA.
AC   Q7T163; Q5TZ97; Q6P7Y1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Kinase D-interacting substrate of 220 kDa B {ECO:0000305};
DE   AltName: Full=Ankyrin repeat-rich membrane-spanning protein B {ECO:0000305};
GN   Name=kidins220b {ECO:0000312|ZFIN:ZDB-GENE-030131-7824};
GN   Synonyms=arms {ECO:0000312|ZFIN:ZDB-GENE-030131-7824},
GN   kidins220 {ECO:0000303|PubMed:22609016};
GN   ORFNames=si:dkeyp-7f8.3, si:dz119j18.2, zgc:63531;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH PDZRN3B, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   MOTIF.
RX   PubMed=22609016; DOI=10.1016/j.biochi.2012.05.002;
RA   Andreazzoli M., Gestri G., Landi E., D'Orsi B., Barilari M., Iervolino A.,
RA   Vitiello M., Wilson S.W., Dente L.;
RT   "Kidins220/ARMS interacts with Pdzrn3, a protein containing multiple
RT   binding domains.";
RL   Biochimie 94:2054-2057(2012).
CC   -!- FUNCTION: Downstream target for both neurotrophin and ephrin receptors.
CC       May play a role in nerve growth factor (NGF)-induced recruitment of
CC       rapgef2 to late endosomes and neurite outgrowth.
CC       {ECO:0000250|UniProtKB:Q9EQG6}.
CC   -!- SUBUNIT: Interacts (via PDZ-binding motif) with pdzrn3b (via PDZ domain
CC       1). {ECO:0000269|PubMed:22609016}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9EQG6}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:22609016}.
CC   -!- DEVELOPMENTAL STAGE: Detected in notochord and brain at the 14-somite
CC       stage. Expressed in the ventral region of the eye and in spinal motor
CC       neurons at 32 hours post-fertilization. {ECO:0000269|PubMed:22609016}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH61450.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL954721; CAE17588.1; -; Genomic_DNA.
DR   EMBL; BX293564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC061450; AAH61450.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q7T163; -.
DR   SMR; Q7T163; -.
DR   STRING; 7955.ENSDARP00000092376; -.
DR   PaxDb; Q7T163; -.
DR   ZFIN; ZDB-GENE-030131-7824; kidins220b.
DR   eggNOG; KOG0502; Eukaryota.
DR   InParanoid; Q7T163; -.
DR   PhylomeDB; Q7T163; -.
DR   Reactome; R-DRE-170984; ARMS-mediated activation.
DR   Reactome; R-DRE-9696270; RND2 GTPase cycle.
DR   Reactome; R-DRE-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q7T163; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:ZFIN.
DR   GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; -; 4.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011646; KAP_P-loop.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF07693; KAP_NTPase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 11.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 10.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Endosome; Membrane; Neurogenesis;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1680
FT                   /note="Kinase D-interacting substrate of 220 kDa B"
FT                   /id="PRO_0000322121"
FT   TOPO_DOM        1..508
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        530..533
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        555..668
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        669..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        690..696
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        697..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        718..1680
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          78..107
FT                   /note="ANK 2"
FT   REPEAT          111..140
FT                   /note="ANK 3"
FT   REPEAT          145..174
FT                   /note="ANK 4"
FT   REPEAT          178..207
FT                   /note="ANK 5"
FT   REPEAT          211..240
FT                   /note="ANK 6"
FT   REPEAT          244..273
FT                   /note="ANK 7"
FT   REPEAT          277..306
FT                   /note="ANK 8"
FT   REPEAT          310..339
FT                   /note="ANK 9"
FT   REPEAT          343..372
FT                   /note="ANK 10"
FT   REPEAT          376..405
FT                   /note="ANK 11"
FT   DOMAIN          449..960
FT                   /note="KAP NTPase"
FT   REGION          1362..1554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1574..1643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1675..1680
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000269|PubMed:22609016"
FT   COMPBIAS        1364..1386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1407..1421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1466..1505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1514..1543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        474..475
FT                   /note="YA -> NT (in Ref. 2; AAH61450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="V -> L (in Ref. 2; AAH61450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1302
FT                   /note="T -> A (in Ref. 2; AAH61450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1680 AA;  185949 MW;  4FE8AB3377DD5E60 CRC64;
     MDTTTSIKMT TLAIQNLFSY VEEENLAAVK VHLDKFKEVD GRSDNGQTPL MLASEQGSLE
     IVQELIRRGA NVNLDDVDCW SALISAAKEG HVEVVKELLE NSAYIEHRDM GGWTALTWAS
     YKGRVEVATV LLENGANPNT TGQQYSVYPI IWAAGRGHAE IVKLLLEHGA KVNCSDKYGT
     TPLIWAARKG HYDCVMHLLE NGADVDQEGA NSMTALIVAV KGGYTEVVKE LLKRNPNVNM
     TDKDGNTALM IAAKEGYTEI VQDLLDAGTY VNIPDRSGDT VLIGAVRGGH VEIVRALLHK
     YADIDIRGQE NKTALYWAVE KGNATMVRDI LQCNPDTETT TKDSETPLIK ATKMRSIEVV
     ELLLDKGAKV SAVDKRGDTP LHIAIRGRSR RLAELLLRNP KDGRLLYRPN KAGETPYNID
     CSHQKSILTQ IFGARHLSPT ESDGDMLGYD LYSSALADIL SEPTMQPPIC VGLYAQWGSG
     KSFLLKKLED EMKTFAGQQV EPLFQFSWLV VLLSLLLCGS VALVLGFTVD PKLAIAISLS
     ILALLYVFFV VVYFGSRREG ESWNWAWVIS TRLARHIGYL ELLLKLMFVN PPELPEQTTR
     ALPVRFLFTD YNRLSSVGGE TSMAEMIATL SDACEREFGF LATRLFRVFK TEDTQGKKKW
     KKTCCIPSFV IFLFILGCLI MGMALLAVFK VDGQNQTVNA VLVSMASVVG LALLLNCRTW
     WQVTDSVLNS QRKRLHSAAN KMHKLKSEGF MKVLKNEVEL MAKMAKTIDG FTQNQTRLVV
     IIDGLDSCEQ DKVLQMLDTV RVLFSKGPFI SIFASDPHII IKAINQNLNS VLRDSNINGH
     DYMRNIVHLP VFLNSRGLSS AKKMCAPAPA NGETGNSEGW HEELDRKLSQ NSLGDQTKFG
     SKTTLNRRDT YRRRQMQRSV TRQMSFDLTK LLVTEDWFSD ISPQTMRRLL NIVSVTGRLL
     RANQISFNWD RLASWINLTE QWPYRTSWLI LYLEETDGIP DQTNLKTIYE RISKNIPTTK
     DVEPLLEIDG DVRSFEVFLS SRTPVLAARD IRTFLPCTVN LDPKLREIIA DVRAAREQVN
     MAGVTYPTLP LQEGRPISMY SQQSSACSPT ASFNGPYNPP GVSPQPHSAY FSGMAGPQHP
     FYNRGSASVV SGTPSILLSS MSTDVICERV KLIDGIDQNL ISQYTATIKK ANINGRVLSQ
     CNIDELKKEM NMNFGDWQLF RTSVLEMRHV ENQVLHEEAP SEQGSITVGH VEPCRHAGAA
     AQGVAGNTDT SPMYNFNLSF EELSNVGLEE PPRHVNATWM GTTHRTPSMS SLNSQESSNE
     ICKLTDKQQA EYRNAYEDYI ASMSQLELGM EKPVPPFVSQ LMHSSSEDKK KDGNDQDGRK
     SVSKRGSTKS GSDNTDYASA DAATLDPITE EDEKVDHGSS KSLLGRKTSG DKVSLFQGAD
     LKLKAGGGSR YQKLTSDDEE SEESDNAPLL KDGKKPEAKA SDGGDRSLTK GKDYLSDKKD
     SSDSGVRSNE SSPNHSLQDE EADLSQSERA NLIELDEENS ARKRGLPNSL SGLQDPTIAR
     MSICSEDQCS LLASSPEESW PSSKSYNLNR TPSNTTLNNN TNAQQGNHIR QPSDSSNTTS
     TTTGSDVIIN PGTSTTSATT QNENVRVVHL KRGLNPGDPP EILKVSSETV TFGEERESIL
 
 
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