ID   CTTB2_MUNMU             Reviewed;        1642 AA.
AC   Q09YJ3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Muntiacus muntjak (Barking deer) (Indian muntjac).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Muntiacinae; Muntiacus.
OX   NCBI_TaxID=9888;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000178; ABI75287.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09YJ3; -.
DR   SMR; Q09YJ3; -.
DR   PRIDE; Q09YJ3; -.
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..1642
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260408"
FT   REPEAT          702..732
FT                   /note="ANK 1"
FT   REPEAT          736..765
FT                   /note="ANK 2"
FT   REPEAT          769..798
FT                   /note="ANK 3"
FT   REPEAT          802..831
FT                   /note="ANK 4"
FT   REPEAT          835..864
FT                   /note="ANK 5"
FT   REPEAT          904..934
FT                   /note="ANK 6"
FT   REGION          1..27
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          366..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1441..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        381..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..510
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..550
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1453..1469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1551..1594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1606..1642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         491
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1642 AA;  178144 MW;  ADC2D48C6881CBC3 CRC64;
     MATDGASCEP DFSRAPEDAA GAPAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGASDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKHV VLMLVKECKQ
     LSGKVLEEAQ KLEEVMAKLE EEKKKTSALE EELATEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLHREEA HTADLKEEID KMKKMIEQLK RGTDSKPGLS LPRKTKDRRS ISISVATEGP
     MTRSVACQTD LVMESAEPVK KLPLTVPVKP AAGSPPVAAG AKGNACASAA AVRPGVERQV
     SHGDLIGASL PAAPPPSANR IEENGPSTGS TADLTSSPTP VPSTVSPASG HTPAPPPHSL
     HSPCANAPLH PGLNPRIQAA RFRFQGSNAN DPDQNGNTTQ SPPSRDVSPT SRDNLVAKQL
     ARNTVTQALS RFTSPPAGAP PRPGAPPTGD VGTYPPVGRT SLKTPGGARV DRGNPPPIPP
     KKPGLSQTPS PPHPQLKVIM DSSRASSTGI KADNKTVASP PSTLPQGNRV MNEENLSKSS
     SPQLPPKPSI DLTVAPAGCA VSALATSQVG AWPAETPGLN QSACSERSLV IPTTTASSSS
     IHPVNASSRR AGASDSLLVT ASGWSPSLTP LLMSGGPAPL AGRPTLLQQA AAQGNVTLLS
     MLLNEEGLDI NYSCEDGHSA LYSAAKNGHT DCVRLLLNAE AQVNAADKNG FTPLCAAAAQ
     GHFKCVELLI AYDANINHAA DGGQTPLYLA CKNGNKECIK LLLEAGTDRS VKTRDGWTPI
     HAAVDTGNVD SLKLLMYHRA PAHGNKLREE PGLAIFDLDQ EEERHEGTSK PVVPADLINH
     ADSEGWTAAH IAASKGFKNC LEVLCRHGGL EPERRDKCNR TAHDVATDDC KHLLENLNAL
     KIPLRISVGE IEPGNYGADD FECENTICAL NIRKQTSWDD FSKAVSQALT NHFQAISSDG
     WWSLEDMTFN STTDSSIGLS ASSVRSITLG TVPWSAGQSF AQSPWDFVRT NKAEQVTVLL
     SGPQEGCLSS VTYASMIPLQ MLQNYLRLVE QYHNVIFHGP EGSLQDYITH QLALCLKHRQ
     MTAGFPCEIV RAEVDADFSK EQLVDLFISS ACLIPVKQSP ANKKIIVILE NLEKSSLSEL
     LGDFLGPLEN HSTESPCTFQ KGNGTSECYY FHENCFLMGT IAKACLQGSD LLVQQHFRWV
     QLRWDGEPMQ GLLRRFLRRK VVNKFRGQVP SPCDPVCKTV DWALAVWRQL NSCLARLGTP
     EALLGPKYFL SCPVIPGHAQ ATVKWMSKLW NAVIAPRVQE AILSRASVKR QPGLGQTTKN
     PSQGQQAVVR AALSILLNKA VLHGCPLQRA ELDQHTADFK GGSFPLSIVS SYSSCNKKKE
     SGAWRKVSTS PRKKSGRFSS PTWNKPDLSE EGIKSNTILQ LNCNRNASLS NQKSLENDLS
     LTLNLDQRLS LGSDDEADLV KELQSMCSSK SESDISKIAD SRDDLRRFDS SGNNPVFSAT
     VNNPRMPVSQ KEVSPLSSHQ TTECSNSKSK TELGVSRVKS FLPVPRSKVT QCSQNTKRSS
     SSSNTRQIEI NNNSRDLEPT QK