CTTB2_RABIT
ID CTTB2_RABIT Reviewed; 1664 AA.
AC Q09YM8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN,
CC STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic
CC spine distribution of STRN and STRN4 in hippocampal neurons. Activation
CC of glutamate receptors weakens the interaction with STRN and STRN4.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Remains associated with
CC dendritic spines even after glutamate stimulation. {ECO:0000250}.
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DR EMBL; DP000006; AAY89019.2; -; Genomic_DNA.
DR RefSeq; NP_001164508.1; NM_001171037.1.
DR AlphaFoldDB; Q09YM8; -.
DR SMR; Q09YM8; -.
DR STRING; 9986.ENSOCUP00000001196; -.
DR PRIDE; Q09YM8; -.
DR GeneID; 100126566; -.
DR KEGG; ocu:100126566; -.
DR CTD; 83992; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR InParanoid; Q09YM8; -.
DR OrthoDB; 264951at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF09727; CortBP2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1664
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260413"
FT REPEAT 710..740
FT /note="ANK 1"
FT REPEAT 744..773
FT /note="ANK 2"
FT REPEAT 777..806
FT /note="ANK 3"
FT REPEAT 810..839
FT /note="ANK 4"
FT REPEAT 843..872
FT /note="ANK 5"
FT REPEAT 913..943
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 383..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1664 AA; 179481 MW; EE1E563D6AAC5466 CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGASDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALD QEHQKLAARL EEERGKNRHV VLMLVKECKQ
LSGKVIEEAQ KLEEVMASLE EEKKKTNDLE EQLCTEKRRS AEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL ASVSVATEGP
VTRAVACQTD PVTESTDHVR KLPLTVPAKP SAGSPLVSAN TKGNVCPHAA PGRPGMDRQA
SHGDLMGSSA PTIPAASASR MEANGPSPGS TPDLTSSTPP IPSGTTPAPA HAPGVATQSP
VPAAPGHGLH SPCATTALHP GLNPRIQAAR FRFQGNANDP DQNGNTTQSP PSRDVSPTSR
DNLVAKQLAR NTVTQALSRF TSPQVGTPPR PGVPPTGDVA THPPVSRSGL KTPGGARVDR
GNPPPIPPKK PGLSQTPSPP HPQLKIPVDS SRASSAGAKV ENKTVASPPS SLPPGSRVIT
EENPPKSSSP QLPPKPSIEL TVAPAGCAVS ALAASQVGAW PAETLGLKPP ACSDSSLVIP
NTIAFRSSIN PVSASTSRPG ASDSLLVTAS GWSPSLTPLL MSGGPAPLAG RPTLLQQAAA
QGNVTLLSML LNEEGLDTNY SCEDGHSALY SAATNGHADC VRLLLNAEAQ VNAAEKNGFT
PLCAAAAQGH FECLELLLAS DADVNHAADG GQTPLYLACK NGNTDCIKLL LEAGTDRSIK
TRDGWTPVHA AVDTGNVDSL KLLMYYQAPA RGNSSNEEEP ESGAFARDGG EESSEGTSEP
VVSADLINHA DREGWTAAHI AASKGFKNCL EILCRHGGLE PEKRDKCNRT VHDVATDDCK
HLLENLNALK IPLRISVGEI QPDNCGSDDF ECENIICTLS IRKQTSWDDF SKAVSQALTN
HFQAISSDGW WSLEDVAFNN TTDSSIGLSA SSVRSITLGN MPWPAGRSFA PSPWDFVRKN
KTEQVTALLS GPQEGCLSSV TYASMIPLKT LQNYLRLVEQ YHNVIFHGPE GSLQDFIAHQ
LALCMKHRQM AAGFSCEIVR AEVDAGFSKE QLLDLFISSA CLIPVKQSPV KKKIIIILEN
LENSSLSELL GDFLAPLENR STESPCTFQK GNGASECYYF HENCFLMGTI AKACLQGSDL
LVQQHFRWVQ LRWDGEPMQG LLPRFLRRKV VNKFRGQVPA PCDPVHKTVA WALSVWRQLN
SCLAHLGTPE ALLGPKYFLS CPVVPGRAQA TVKWMSKLWN AVIAPRVQAA ILSRASVKRQ
PGLGQTAAKK HPSHGQQAVV KAALSILLNK AVLHGCPLPR AELDQHTADF RGGSFPLSIV
SSYNSCSKKK GESGAWRKVS TSPRKKSGRF SSPIWNEPDL SPGGIKNKAI SQLNCGRNTS
LSKQKSLENE LSLTLNLDQR FSLGSDDAAD LVKELQSMCS SKSESDLSKI ADSREELRTF
HSSGSNPAFS APVNNPRMPV APKEVSPLSS HQATECSTSK SKTELGVSRV KSFLPVPRSK
IAQCSQNTKR SSSSSNTRQP EINNNSKEEN WNLHKHEQVE KPNT
