ID   CTTB2_MICMU             Reviewed;        1647 AA.
AC   Q2QL82;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Microcebus murinus (Gray mouse lemur) (Lemur murinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Cheirogaleidae; Microcebus.
OX   NCBI_TaxID=30608;
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; DP000022; ABB89827.1; -; Genomic_DNA.
DR   RefSeq; XP_012616549.1; XM_012761095.1.
DR   AlphaFoldDB; Q2QL82; -.
DR   SMR; Q2QL82; -.
DR   Ensembl; ENSMICT00000005790; ENSMICP00000005282; ENSMICG00000005787.
DR   GeneID; 105869364; -.
DR   KEGG; mmur:105869364; -.
DR   CTD; 83992; -.
DR   GeneTree; ENSGT00940000158293; -.
DR   OrthoDB; 264951at2759; -.
DR   Proteomes; UP000694394; Chromosome 11.
DR   Bgee; ENSMICG00000005787; Expressed in frontal cortex and 6 other tissues.
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..1647
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000227003"
FT   REPEAT          695..725
FT                   /note="ANK 1"
FT   REPEAT          729..758
FT                   /note="ANK 2"
FT   REPEAT          762..791
FT                   /note="ANK 3"
FT   REPEAT          795..824
FT                   /note="ANK 4"
FT   REPEAT          828..857
FT                   /note="ANK 5"
FT   REPEAT          898..928
FT                   /note="ANK 6"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1436..1467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1542..1647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          120..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        356..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..543
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..878
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1449..1467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1544..1590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1602..1631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1632..1647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         484
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1647 AA;  178745 MW;  58BAE5143C0C369F CRC64;
     MATDGASCEP DASRAPEEAA GATAEAARKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMATQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
     LSGKVIEEAQ KLEEAMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGP
     LTRSVACQTD LAIEGTDHVK KSPLTVPGKP SPGSAKGSVC ANAAHVRPGM DRQASHGDLT
     GSSAPSLPPA SANRIEENGP STGSTADLPS STAPAPGSAA QSPVAAALGP AHSAQSPCTP
     APAQPGLNPR VQAARFRFQG NANDPDQNGN TTQSPPSRDV SPTSRDNLVA KQLARNTVTQ
     ALSRFTSPAV GAAPRPGAPP TGDAGAYPPV GRTSLKTPGV ARVDRGNPPP IPPKKPGLSQ
     TPSPPHPQLK VIMDSSRASN AGAKVDNKTV ASPPSSLPQG NRVISEENLP KSSSPQLPPK
     PSIDLTVAPA GCAVSALATS QVGAWPAETP GLNQPACSDS SLVIPTTTAF RSSINPVSAS
     SCRPGASDSL LVTASGWSPS LTPLLMSGGP APLAGRPTLL QQAAAQGNVT LLSMLLNEEG
     LDINYSCEDG HSALYSAAKN GHTDCVRLLL NAEAQVNAAD KNGFTPLCAA AAQGHFECVE
     LLIAYDANIN HAADGGQTPL YLACKNGNKE CIKLLLEAGT DRSVKTRDGW TPVHAAVDTG
     NVDSLKLLMY HRAPAHGNSL NEEEPESDVS DLDDGEESSE GESKPVVPAD LINHADREGW
     TAAHIAASKG FKNCLEILCR HRGLEPERRD KCNRTVHDVA TDDCKHLLEN LNALKIPLRI
     SVGEIQSGNY GSSDFECENT ICVLHIRKQT SWDDFSKAVS QALTNHFQAI SSDGWWSLED
     TAFNNTADSD IGLSLDSVRA IMLGSVPWSA GQSFTQSPWD FMRKNKAEQV TVLLSGPQEG
     CLSSVAYASM IPLQMLQNYL RLVEQYHNVI FHGPEGSLQD YIVHQLALCL KHRQMAAGFS
     CEIVRAEVDA GFSKEQLVDL FISSACLIPV KQSPVKKKII IILENLEKSS LSELLGDFLA
     PLEIRSPESP CTFQKGNGTS ECYYFHENCF LMGTIAKACL QGADLLVQQH FRWVQLRWDG
     EPMHGLLQRF LRRKLVNKFR GQAPSPCDPV CKTIDWALSV WRQLNSCLAR LGTPEALLGP
     KYFLSCPVVP GHAQATVKWM SKLWNAVIAP RVQEAILSRA SVKRQPGFGQ TTTKKHPSQG
     QQAVVKAALS ILLNKAVLHG CPLPRAELDQ HTADFKGGSF PLSLVSNYNS CSKKKENGAW
     RKVNTSPRRK SGRFSSPTWN KPDLSNEGIK NKTISQLNCN KNASLSKQKS LENDLSLMLN
     LDPRLSLGSD DEADLVKELQ SMCSSKSESD ISKIADSRDD LRTFDSSGNN PAFSATVNNP
     RMPVSQKEVS PLSSHQTTEC SNNKSKTEPG VSRVKSFLPV PRSKVTQCSQ NTKRSSSSSN
     TRQIEINNNS KEENWNLHKN EQTHRKT