ID   CTTB2_PONAB             Reviewed;        1663 AA.
AC   Q2IBE6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
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 (DEC-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; DP000026; ABC87468.2; -; Genomic_DNA.
DR   RefSeq; NP_001162027.1; NM_001168555.1.
DR   AlphaFoldDB; Q2IBE6; -.
DR   SMR; Q2IBE6; -.
DR   STRING; 9601.ENSPPYP00000020119; -.
DR   GeneID; 100137031; -.
DR   KEGG; pon:100137031; -.
DR   CTD; 83992; -.
DR   eggNOG; ENOG502QWG2; Eukaryota.
DR   HOGENOM; CLU_004926_0_0_1; -.
DR   InParanoid; Q2IBE6; -.
DR   OMA; MCPVEAL; -.
DR   OrthoDB; 264951at2759; -.
DR   TreeFam; TF325130; -.
DR   Proteomes; UP000001595; Chromosome 7.
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   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
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..1663
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000279862"
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          359..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          498..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1580..1663
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..440
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..1485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1647..1663
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   1663 AA;  181215 MW;  3A1FA2108D75D958 CRC64;
     MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCKK
     MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
     LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELSTEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
     VTRSVACQTD LVTESADYMK KLPLTMPVKP STGSPLVSAN AKGSVCTSAT MARPGIDRQA
     SHGDLIGASV PAFPPPSANK IEENGPSTGS TPDPTSSTPP LPSNAAPPTA QTPGIAPQNS
     QAPPMHSLHS PCANTSLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
     NLVAKQLARN TVTQALSRFT SPQAGAPSRP GVPPTGDVGT HPPVGRTSLK THAVARVDRG
     NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTGAKVD NKTVASPPSS LPQGNRVINE
     ENLPKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLSQPA CSDSSLVIPT
     TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
     GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQV NAADKNGFTP
     LCAAAAQGHF ECVELLIAYD ANINHAADGG QTPLYLACKN GNKECVKLLL EAGTNRSVKT
     TDGWTPVHAA VDTGNVDSLK LLMYHRIPAR GNSFNEEESE SSVFDLDGGE DSPEGISKPV
     IPADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHRGLEP ERRDKCNRTV HDVATDDCKH
     LLENLNALKI PLRISVGEIE PSNYGSDDLE CENTICALNI RKQTSWDDFS KAVSQALTNH
     FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV LWSVGQSFVQ SPWDFMRKNK
     AEHITVLLSG PLEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
     ALCLKHRQMA AGFSCEIVRA EVDARFSKEQ LLDLFISSAC LIPVKQSPSK KKIIIILENL
     EKSSLSELLR DFLAPLENRS TESPCTFQKG NGISECYYFH ENCFLMGTIA KACLQGSDLL
     VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFKGQAPSP CDPVCKIVDW ALSVWRQLNS
     CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VIAPRVQEAI LSRASVKRQP
     GFGQTTAKRH PSQGQQAVIK AALSILLNKA VLHGCPLPRA ELDQHTADFK GGSFPLSIVS
     SYNSCNKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGMKNKTVS QLNCNRSASL
     SKQKSLENDL SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFD
     SSGNNPVLSA TINNLRMPVS QKEVSPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
     TQCSQNTKRS SSSSNTRQIE INNNSKEENW NLHKNEHLEK PNK