ID   CTTB2_AOTNA             Reviewed;        1649 AA.
AC   Q07DV1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293;
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; DP000197; ABJ08891.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07DV1; -.
DR   SMR; Q07DV1; -.
DR   STRING; 37293.ENSANAP00000036080; -.
DR   Proteomes; UP000233020; Whole Genome Shotgun Assembly.
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..1649
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260400"
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..23
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..616
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          1444..1482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1616..1649
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..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1642
FT                   /note="Polar 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   1649 AA;  179243 MW;  7173AA79742449E0 CRC64;
     MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLATRL EEERGKNKQV VLMLVKECKQ
     LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELCAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
     VTRSVACQTD LVTESADHVK KLPLTMPVKP STGSPLASAN AKGSVCTSAA MARPGIDRQA
     SHGDLIGVSV PAFPPSSASR IEENGPSTGS TPDPTSSTPP LPSNAAPPTA QTPGITPQNS
     QAPPMHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
     NLVAKQLARN TVTQALSRFT GPQAGAPPRP GAPPAGDVGT HPSVGRTSVK THGVARVDRG
     NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTGAKGD NKTVASPPSS LPQGNRVINE
     ENLPKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
     TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
     GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQV NAADKNGFTP
     LCAAAAQGHF KCVELLIAYD ANINHAADGG QTPLYLACKN GNKECIKLLL EAGTDRSVKT
     TDGWTPVHAA VDTGNVDSLK LLMYHRVPAH GNSFSEEESE SGVFDLDGGE ESPEGKSKPV
     VTADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLET ERRDKCNRTV HDVATDDCKH
     LLENLNALKI PLRISVGEIE PSNYGSDDFE CENTICALNI RKQTSWDDFS KAVSQALTNH
     FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGQSFAQ SPWDFMMKNK
     AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
     ALCLKHRQMA AGFSCEIVRA EVDAGFSKKQ LLDLFISSAC LIPVKQSPVK KKIIIILENL
     EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
     VQQHFRWVQL RWDAEPMQGL LQRFLRRKVV NKFRGQVPPP CDPVCKTVDW ALSVWRQLNS
     CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VITPRVQEAI LSRASVKRQP
     GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELEQHTADFK GGSFPLSIVS
     SYNSCSKKKG ESGAWRRVNT SPRRKSSRFS LPTWNKPDLS NEGIKNKTLS QLNCNRNASL
     SKQKSLENDV SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFD
     SSGNHPVFSA TINNLRMPVS QKEVCPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
     TQCSQNTKRS SSSSNTRQIE INNNSKEEN