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CTTB2_PLEMO
ID   CTTB2_PLEMO             Reviewed;        1663 AA.
AC   Q2QLB3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC   Pitheciidae; Callicebinae; Plecturocebus.
OX   NCBI_TaxID=9523;
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 (NOV-2005) 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; DP000019; ABB89796.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QLB3; -.
DR   SMR; Q2QLB3; -.
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..1663
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000227000"
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          355..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..614
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          1446..1482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1617..1663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..275
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        380..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..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;  180960 MW;  654C7B7735856746 CRC64;
     MATDGASCEP DLSRAPEDAA GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
     LSGRVIEEAQ KLKDVMAKLE EEKKKTNELE EELSAEKQRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK KGGDSKPSLS LPRKTKDRRL VSISVGTEGT
     VTRSVACQTD LVTESADHVK KLPLTMPVKP STGSPLASAN AKGSVCTSAA MARPSIDRQP
     SHGDLIGVSV PAFPPSSANR IEENGPSTDS TPDPTSSTPL LSSNAAPPTA QTPGITPQNS
     QAPPMHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
     NLVAKQLARN TVTQALSRFT GPQAGAPPRP GAPPTGDVGT 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 NAADTNGFTP
     LCAAAAQGHF ECVELLIAYD ANINHAAGGG QTPLYLACKN GNKECIKLLL EAGTDRCVKT
     TDGWTPVHAA VDTGNVDSLK LLMYHRVPAH GNSFSEEESE SGVFDLDGEE ESPEGKSKPV
     VTADLINHAN REGWTAAHIA AAKGFKNCLE ILCRHGGLEP ERRDKCNRTV HDVATDDCKH
     LLENLNALKI PLRISVGEIE PSDYGSDDFE CENTICSLNI RKQTSWDDFS KAVNQALTNH
     FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGESFAQ SPWDFMMKNK
     AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
     ALCLKHRQMA AGFSCEIVRA EVDSGFSKKQ LLDLFISNAC LIPVKQSPVK KKIIIILENL
     EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
     VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFRGQVPPP CDPVCKIVDW ALSVWRQLNS
     CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VITPRVQEAI LSRASVKRQP
     GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELEQHTADFK GGSFPLSIVS
     SFNSCSKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGIKNKTLS QLNCNRNASL
     SKQKSVENDV SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFN
     SPGNNPVFSA TVNNLRMPVS QKEVCPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
     TQCSQNTKSS SSSSNTRQIE INNNSKEENW NLHKNEHLEK ANK
 
 
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