ID   CTTB2_NEONE             Reviewed;        1658 AA.
AC   Q07E28;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Neofelis nebulosa (Clouded leopard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC   Neofelis.
OX   NCBI_TaxID=61452;
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; DP000182; ABI93648.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07E28; -.
DR   SMR; Q07E28; -.
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..1658
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260411"
FT   REPEAT          706..736
FT                   /note="ANK 1"
FT   REPEAT          740..769
FT                   /note="ANK 2"
FT   REPEAT          773..802
FT                   /note="ANK 3"
FT   REPEAT          806..835
FT                   /note="ANK 4"
FT   REPEAT          839..868
FT                   /note="ANK 5"
FT   REPEAT          909..939
FT                   /note="ANK 6"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1448..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1611..1642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        404..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1543..1558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1612..1642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         495
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1658 AA;  180324 MW;  1DD877AAB9C1AD97 CRC64;
     MATDGASCEP DFSRAPEDAA GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSTQLA AAESRQKKLE MEKLQLQAVE QEHQKLAARL EEERGKNKHV VLMLVKECKQ
     LSGKVIEEAQ KLEEVMVKLE EEKTKTSALE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLHREEA HTTDLKEEID KMKKMIEQLK RGNDSKPSLS LPRKTKDRRM VSISVGTEGP
     VTRSVACQTD LVIESTDHVK KLPLTVPVKP SAGSPLVPAN TKGNVCTGAA LGRPGIDRQA
     SHGDLIGSSP PTVPPPSANR IEENGPSAGS ASSTPPLPNS TAPPTVQTPG IAPQSYSQAP
     PVHSLHSPCA NASLHPGLNP RIQAARFRFQ GNANDPDQNG NTTQSPPSRD VSPTSRDNLV
     AKQLARNTVT QALSRFTSPQ AGAPPRPGAA PTGDGGTCPP VGRTSLKTPG VARVDRGNPP
     PIPPKKPGLS QTPSPPHPQL KVIMDSSRAS NAGAKVDNKT MASPPSSLPQ GNRVINEENL
     PKSSSPQLPP KPSIDLTVAP AGCAVSALAT SQVGAWPAET PGLNQPACSE SSLVIPTTIA
     FCSSINTVSA SSCRTGASDS LLVTASGWSP SLTPLLMSGG PAPLAGRPTL LQQAATQGNV
     TLLSMLLNEE GLDINYSCED GHSALYSAAK NGHTDCVRLL LNAGAQVNAA DTNGFTPLCA
     AAAQGHFKCV ELLISYDANI NHAADEGQTP LYLACKNGNK ECIQLLLEAG TDRSVKTRDG
     WTPVHAAVDT GNVDSLKLLM YHRAPACRNS LHEEESESVV FDLDQGEESP EGTSKPVVPA
     ELINHADREG WTAAHIAASK GFKNCLEILC MHGGLEPERK DKCHRTAHDV ATDDCKHLLE
     NLNALKIPLR ISVGETEPGS YGSDDFECEN TICALNIRKQ TSWDDFSKAV SQALTNHFQA
     ISSDGWWSLE DVTLNNTTDS SIGLGTSSVR SIMLGNAPWS AGQSFTQSPW DFMKKNKAER
     VTVLLSGPQE GCLSSVTYAS MIPLQMLQNY LRLVEQYHNV IFHGPEGSLQ DYIAHQLALC
     MKHRQMAAGF TCEIVRAEVD AGFSKEQLID LFINSACLIP VKQSPVNKKI IIILENLEKS
     SLSELLGDFL APLENRSTES PWTFQKGNGT SECYYFHENC FLMGTIAKAC LQGSDLLVQQ
     HFRWVQLRWD GEPMQGLLQR FLRRKVVNKF RGQVPSPCDP VCKTVDWALA VWRQLNSCLA
     RLGTPEALLG PKYFLSCPVV PGHAQATVKW MAKLWNAIIA PRVQEAILSR ASVKRQPGLG
     LATAKKHPSQ GQQAVVKAAL SILLNKAVLH GCPLPRAELD QHAADFRGGS FPLSIVSSYH
     SYSKKKGESG AWRKVSTSPR KKSGRFSPPS WNKPGLSEEG IRIKAVSQQN CNRNASLSKQ
     KSLENDLSLT LNLDQRLSLG SDDEADLVKE LQSMCSSRSE SDISKIADSR DDLRRFDGSR
     NNPAFSTVNP RMPVSPKEVS PLSSHETTEC SNSQSKIELG VSRVKSFLPV PRSKVTQCSQ
     NTKRSSSSSN TRQIEINNNT KEDIWNFHQN EQVEKPNQ