CTTB2_ATEAB
ID CTTB2_ATEAB Reviewed; 1654 AA.
AC Q00PJ1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae; Atelerix.
OX NCBI_TaxID=9368;
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 (OCT-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; DP000003; AAY88986.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00PJ1; -.
DR SMR; Q00PJ1; -.
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; Repeat; Synapse.
FT CHAIN 1..1654
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000274182"
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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 362..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1645
FT /note="Polar 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 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1654 AA; 180097 MW; 6888EBE9C978809B CRC64;
MATDGASCEP DFSRSPEDAA GATAEPAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLSACL DEERNKNKHV VLMLVKECKQ
LSGKVIEEAQ KLDEVMTKLE EEKKKTTALE EELSAEKQRS TEMEAQMEKQ LSEFDTEREQ
LRAKLHREEA HTADLKEEID KMKKMIEQLK RGSDSKPGLS LPRKTKDRRL ISVSVGTEVS
VTKSVACQTD SAIESIEPVK KLPLTVPAKP STGSPLVSAS TKGNMCTNAT LVRPGIDRQA
SHGDLTISSV PAAPTPSASR TEENGPSTGS APDPTSSTPP LPNNAAPPTV QTPGTAAQSY
SQAPPVHSLH SPCANVSLHP GLNPRIQAAR FRFQGNANDP DQNGNTSQSP PSRDVSPTSR
DNLVAKQLAR STVTQALSRF TSPQTGAPPR PGAAPTGDVS SHTPVSRTSL KTPGVSRVDR
GNPPPIPPKK PGLSQTPSPP HPQLKVIMDS SRAASAGVKV DNKTVAVPPS SLPQGNRVIS
EENLLKSSSP QLPPKPSIDL TVAPAGCAVS ALATSQVGAW PAEPPGLNQP ACSESSLVIP
NTIAFCSSIN PVSASSCRTG ASVSLLVTAS GWSPSLTPLL MSGGPAPLAG RPTLLQQAAA
QGNVTLLSML LNEEGLDINY SCEDGHSALY SAAKNGHTDC VRLLLNAQAQ VNAADKNGFT
PLCAAAAQGH FKCIELLIAN DANINHAADG GQTPLYLACK NGNNECIKLL LGAGSDRSVK
TRDGWTPVHA AVDTGNVDNL KLLMYYEAPI PGNSFNEEKL ESNIIDLDQE EESPEGIPKT
VVPADLINHA DREGWTAAHI AASKGFKNCL EILCRHRGLE PERRDKCSRT AHDVATDDCK
HLLENLHAFK IPLRISIAEI QPGNHGSDDF ECDNIICTLN IRKQTSWDDF SKAVSQALIN
HFQAVSSDGW WTLEDMTFNN TADSSIGLGA SSVQSIMLGN VPWSAGQNFT LFPWEFMRKN
KAEQVTVILS GPQEGCLSSV SYTSMIPLQM LQNYLRLVEQ YHNVIFHGPE GSLQDYIAHQ
LALCMKHRQI AAGFTCEIVK AQVHAGFSKE QLVDLFISSA CLIPVKQSPV NKKIIIILEN
LEKSSLSELL GDFLTPLENR STETPYTLQK GNGMSECYYF HENCFLMGTI AKACLQGSDL
LVQQHFRWVQ LRWDGEPMQG LLQRFLRRKV VNKFRGQLPS PCDPVCRTVD WALAVWCQLN
SCIARLGTPE ALLGPKYFLS CPVVPGHAQA TVKWMSHLWN AIIAPRVQEA ILSRASVKRQ
HSLGQTTAKK HPSQGQQAIV KAALSILLNK AVLHGCPLQR AELDQHTADF KGGSFPLSMV
SSYNSCSRKK AESGAWRKVS TSPRKKSGHF SSPVWNKPDL SEEGIKNKAI SQLNYNGSAL
LAKQKSLEND LSLTLDQRLS LGSDDETDLV KELQNMCSSK SESDISKIAD SRDDLRRLHS
SGNNPAFSAA VNNPKMPVSQ KEVSPLSSHQ TTECSNNKSK TELGVSRVRS FLPVPRSKVT
QCSQNTKRSS SSSNTRQIEI NNNSKEEIWN LRKK
