ID   CTTB2_ATEGE             Reviewed;        1660 AA.
AC   Q09YK4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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   Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Ateles.
OX   NCBI_TaxID=9509;
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; DP000177; ABI75276.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09YK4; -.
DR   SMR; Q09YK4; -.
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; 3.
PE   3: Inferred from homology;
KW   ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW   Phosphoprotein; Repeat; Synapse.
FT   CHAIN           1..1660
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260401"
FT   REPEAT          709..739
FT                   /note="ANK 1"
FT   REPEAT          743..772
FT                   /note="ANK 2"
FT   REPEAT          776..805
FT                   /note="ANK 3"
FT   REPEAT          809..838
FT                   /note="ANK 4"
FT   REPEAT          842..871
FT                   /note="ANK 5"
FT   REPEAT          912..942
FT                   /note="ANK 6"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1445..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1617..1660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        393..407
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..557
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1644..1660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         498
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1660 AA;  180725 MW;  AC6691E1F2A09AC0 CRC64;
     MATDGASCEP DLSRAPEDAA GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
     LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
     VTRSVACQTD LVTESADHVK KLPLTTPVKP STGSPLASAN AKGSVCTSAA MARPGIDRQA
     SHGDLIGVSV PAFPPSSANR IEENGPSTGS TPDPTSSTPP LPSNAAPPTA QTPGITPQNS
     QAPPMHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
     NLVAKQLARN TVTQALSRFT GPQAGAPPRP GAPPTADVGT HPSVGRTSVK THGVARVDRG
     NPPPIPPKKP GLSQTPSPPH PQLKVLIDSS RASNTGAKGD NKTVASPPSS LPQGNRVINE
     ENLSKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
     TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
     GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQV NAADKNGFTP
     LCAAAAQGHF ECVELLVAYD AHINHAADGG QTPLYLACKN GNKECIKLLL EAGADRSVKT
     TDGWTSVHAA VDTGNVDSLK LLMYHRVPAH GNSFSEEESE SGVFDLDGEE ESPEGKSKPV
     VTADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLET ERRDKCNRTA HDVATDDCKH
     LLENLNALKI PLRILVDEVE PSNYGSDDFE CENTICALNI RKQTSWDDFS KAVSQALTNH
     FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGQSFAQ SPWDFMMKNK
     AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
     ALCLKHRQMA AGFSCEIVRA EVDASFSKKQ LLDLFISSAC LIPVKQSPVK KKIIIILENL
     EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
     VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFRGQVPPP CDPVCKIVDW ALSVWRQLNS
     CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VITPRVQEAI LSRASVKRQP
     GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELAQHTADFK GGSFPLSIVS
     SYNSCSKKKG ESGSWRKVNT SPRRKSGRFS LPTWNKPDLS TEGIKNKTLS QLNCNRNASL
     SKQKSLENDV SLTLNLDQSL FLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRTFD
     SSGNNPVFLA TINNLRMPVS QKEVCPLSSH QTTECSNSKS KTELDVSRVK SFLPVPRSKV
     TQCSQNTKSS SSNTRQIEIN NSKEENWNFH KNEHLEKPNK