ID   CTTB2_ECHTE             Reviewed;        1666 AA.
AC   A1X157;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, 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   Echinops telfairi (Lesser hedgehog tenrec).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
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; DP000274; ABL76173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1X157; -.
DR   SMR; A1X157; -.
DR   PRIDE; A1X157; -.
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; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
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..1666
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000279860"
FT   REPEAT          712..742
FT                   /note="ANK 1"
FT   REPEAT          746..775
FT                   /note="ANK 2"
FT   REPEAT          779..808
FT                   /note="ANK 3"
FT   REPEAT          812..841
FT                   /note="ANK 4"
FT   REPEAT          845..874
FT                   /note="ANK 5"
FT   REPEAT          915..945
FT                   /note="ANK 6"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1620..1666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          120..274
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        378..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1549..1565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1567..1601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         501
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1666 AA;  180275 MW;  9B0AB5858945603C CRC64;
     MATDGASCEP DFARAPEDAA GAPAEAARKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSTQLA AAESRQKKLE MEKLQLQTLE QEHKTLAARL EEERVKNKHV VLMLVKECKQ
     LSGKVIEEAQ KVEEALAQLE EEKKRASGLE EELSGEKRRS AEMEAQMEKQ LSEFDTEREQ
     LRAKLSREEA HTTDLKGEID KMKKMTEQLK RGNDSKPSLS LPRKAKDRRW VSVSVGTEGP
     GTGSVACQTD LGVESTDHVK KLPLTVPAKP AAGSPLVAAS AKGSGGATAP LARPGVDRQA
     SHADLIVSSP PTIPPPNTNK IEENGPSTSS GPDTPSSTAP LPSNAAPPAI QTPNAAAQNY
     PAQAPSTHTV HSPCANAALH PALTPRVQAV RFRFQGNANN DQDQNGNNTQ SPPSRDVSPT
     SRDNLVAKQL ARNTVTQALS RFTSPQAGAP PRPGAPPTGE GSTHPPVGRT SLKTPGAARV
     DRGNPPPIPP KKPGLSQTPS PPHPQLKVLL DSSRASNAGP KVDHKTVALP PTSVPQGNRV
     INEESLPKSS SPQLPPKPSI DLTVAPAGCA VSALATSQVG AWRAETPGLK PPACSDRPLV
     IPTTIAFRCP INPVSASSCR PGASDSLLVT ASGWSPSLTP LLMSGGPAPL AGRPTLLQQA
     AAQGNVTLLS MLLNEEGLDI NHSCEDGHSA LYSAAKNGHT DCVRLLLNAE AQVNAADNDG
     FTPVCAAAAQ GHVKCVELLV AYHANINHAA AEGQTPLYLA CKNGNKECIK LLLEAGTDRS
     VKTRDGWTPV HAAVDTGSVD GLKLLLYHRA PACGDGLDTE ASRLGVFDLD EGEANPESTP
     TPVIPADLIN HANREGWTAA HIAASKGFKN CLKILCRHGG LEPERKDKCN RTVHDVATDD
     CKHLLENWNA LKIPLRISVG ETQGDNSGPD EFESEHTICA LNIRKPTSWD DFSKAVSQAL
     TSHFQAISSD GWWSLEDVTL NSPAEASIGL SATSVLSITL GNVPWSVGQS FTQSPWDFLR
     KHQAEQVTVL LSGPQEGCLS SVTYASMIPL PVLQNYLRLV EQYHTVIFHG PEGSLQDYIA
     LQLALCMKHR QAAVGFSCDI VRADVDAGFS KEQLVDLFIK SACLIPAKQS PASKKTIIIL
     ENLERASLSE LLGDFLAPLE NRSPESPYTF HKGNGTSECY YFHENCFLVG TIAKACLQGP
     DLLVQQHFRW VQLRWDGEPM QGLLQRFLRR KVVNKFRGKL PSPGEPVCKM VDWALSVWRQ
     LNSCLSHLGT PEALLGPKCF LSCPVVPGHA QATVKWMSKL WNAVIAPRVQ DAILSRASVN
     RQPGLGQTAA KKHPSPGQQA VVKAALSILL HKAVLHGCPL PRAELDQSMA DFKGGSFPLS
     LVSSYSSCSK KKGENGAWRK VSTSPRKKSG WFFSPTWSKP DLSDEGIKSK TISQPNCNRN
     ASLSRQKCLE NDLSLALNLD QRLSLGSDDE ADLVKELQSM CSSKSESDIS KIADTRDDLR
     RFDSSRNRPA PSATVTNPRM PVSQKEVSPL SSHQTMERSN RTLKTELGVS RVKSFLPVPR
     SKITQCSQNT KRSSSSSNTR QIEINNNSKD EIWNLRNNEQ IEKPNQ