ID   CTTB2_CHLAE             Reviewed;        1662 AA.
AC   Q2IBA2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
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 (JAN-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; DP000029; ABC87492.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IBA2; -.
DR   SMR; Q2IBA2; -.
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..1662
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260402"
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          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1450..1474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1580..1602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1618..1662
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..479
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        1618..1648
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   1662 AA;  180999 MW;  650E144601D24C06 CRC64;
     MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCKK
     MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
     LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
     VTRSVACQTD LVTESADHVK KLPLTMPVKP STGSPLVSAN AKGSVCTSAT MARPGIDRQA
     SHSDLIGSSV PAFPPPSANR IEENGPSTDS TPDPTSSTPP LPSNAAPPTT QTPGIAPQNS
     QAPPMHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDMSPTSRD
     NLVAKQLARN TVTQALSRFT SPQAGAPSRP GAPPTGDVGT HPPVGRTSLK THGVARVDRG
     NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTGAKVD NKTVASPPSS LPQGNRVTNE
     DNLPKSSSPQ LPPKPSIDLT VAPAGCTVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
     TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
     GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQI NAADKNGFTP
     LCAAAAQGHF ECVELLIAYD ANINHAADGG QTPLYLACKN ENKECIKLLL EAGTNRSVKT
     TDGWTPVHAA VDTGNVDSLK LLMYHRIPAC GNSFNEEESE SGVFDLDGGE ESPEGIFKPV
     VPADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLEP ERRDKCNRTV HDVATDDCKH
     LLENLNALKI PLRISVGEIE PSNCGSDDLE CENTICALNI RKQTSWDDFS KAVSQALTNH
     FQAISSDGWW SLEDVTCNNT TDSNIGLSAA SIRSITLGNV PWSVGQSFTQ SPWDFMRKNK
     AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
     ALCLKHRQMA AGFSCEIVRA EIDAGFSKEQ LLDLFISSAC LIPVKQSPSK KKIIIILENL
     EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
     VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFKGQAPSP CDPVCKIVDW ALSVWRQLNS
     CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VIAPRVQEAI LSRASVKRQP
     GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELDQHTADFK GGSFPLSIVS
     SYNSCNKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGIKNKTIS QLNYNRNVSL
     SKQKSLENDL SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFD
     SSGNNPILSA TINNLRMPVS QKEVSPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
     TLCSQNTKRS SSSSNTRQIE INNNSKENWN LHKNEHLDKP NK