ID   CTTB2_OTOGA             Reviewed;        1655 AA.
AC   Q2QLG9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii(Bushbaby).";
RL   Submitted (MAR-2011) 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; DP000013; ABA90409.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QLG9; -.
DR   SMR; Q2QLG9; -.
DR   STRING; 30611.ENSOGAP00000001568; -.
DR   eggNOG; ENOG502QWG2; Eukaryota.
DR   InParanoid; Q2QLG9; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
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; 1.
DR   Pfam; PF13857; Ank_5; 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; 3.
PE   3: Inferred from homology;
KW   ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW   Phosphoprotein; Reference proteome; Repeat; Synapse.
FT   CHAIN           1..1655
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000227004"
FT   REPEAT          700..730
FT                   /note="ANK 1"
FT   REPEAT          734..763
FT                   /note="ANK 2"
FT   REPEAT          767..796
FT                   /note="ANK 3"
FT   REPEAT          800..829
FT                   /note="ANK 4"
FT   REPEAT          833..862
FT                   /note="ANK 5"
FT   REPEAT          903..933
FT                   /note="ANK 6"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1548..1655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          120..275
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        385..411
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..548
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1550..1597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1609..1638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1639..1655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         489
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1515
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1655 AA;  179282 MW;  3B22C6866B2B2679 CRC64;
     MATDGASCEP DSSRAPEDPA GATAEAPKKE FDVDTLSKTE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMATQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLLLVKECKQ
     LSGRVIEEAQ RLEEVMAKLE EEKKRTSELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
     LRAKLSREEA HTTDLKEEVD KMKKMIEQLK RGGDGKPSLS LPRKTKDRRL VSASVGTEGP
     LTRSVACQTD LAVESAEPVK KSPLTVHVKP SPGSPHVSVK GSGGKPGMDR QASHGELMGS
     ALPTLPPPSA SRIEENGPSP GSTPDAPGSA APPGSAAPPG SAAPPGSAAP PGSAAPHSFH
     SPCASAPPHP GLNPRIQAAR FRFQGNANDP DQNGNTTPSP PSRDVSPTSR DNLVAKQLAR
     NTVTQALSRF TSPPAGAAPR PGASPTGDGG AYPPVGRTGL KTPGVARVDR GNPPPIPPKK
     PGLSQTPSPP HPQLKVIMDS SRASNAGAKV DNKTVASPPS SLPQGSRVIN EENLPKSSSP
     QLPPKPSIDL TVAPAGCAVS ALATSQVGAW PAETPGLNHP ACSDSSLVIP TTTASRSAIN
     PVSASSCSPG ASDSLLVTAS GWSPSLTPLL MSGGPAPLAG RPTLLQQAAA QGNVTLLSML
     LNEEGLDINY SCEDGHSALY SAAKNGHTDC VRLLLNAEAQ VNAADKNGFT PLCAAAAQGH
     FECVELLIAY DAHINHAADE GQTPLYLACK NGNKECIKLL LEAGTNRNVK TRDGWTPVHA
     VVDTGDVDSL KLLMYHRAPA RGNSLNEEEP KSDIFDLDEG EESPEGISKP VIPADLINYA
     NREGWTAAHI AASKGFKNCL EILCRHRGLE PEKRDKCNRT VHDVATDDCK HLLENLNALK
     IPVRISVGEI QPGNYGSNDF ECENTICALH IRKQTSWDDF SKAVSQALTN HFQAISSDGW
     WSLEDTALND TADSNIGLST SSVRAIMLGH VPWSSGQSFT QSPWDFMKRN KVEQVTVLLS
     GPQEGCLSSV TYASMIPLHM LQNYLRLIEQ YRNVIFHGPE GSLQDYIVHQ LALCLKHRQM
     AAGFSCEIVT AEVDAGFSKE QLVDLFISSA CLIPVKQSPV KKKIIIIILE NLEKSSLSEL
     LGDFLAPLEN RSTESPCTVQ KGNGMSACYY FHENCFLMGT IAKACLQGSE LLVQQHFRWV
     QLRWDGEPMQ GLLQRFLRRK VVNKFRGQVP SPCDLVCKTV AWALSVWRQL NSCLARLGTP
     EALLGPKYFL SCPVIPGHAQ ATVKWMSKLW NAVIAPRVQE AILSRASMKR QPGFGQTTAK
     KHPSQGQQAV VKAALSILLN KAVLHGCPLP RAELDQHTAD FKGGSFPLSL VSSYNSCSKK
     KESGAWRKVN TSPRRKSGRF SSPTWNKADP SSEGLKNKTI SQLNCNKNAS LSKQKSLEND
     LSLMLNLDQR LSLGSDDEVD LVKELQSMCS SKSESDISKI ADSRDDLRTF DSSGNNPAFS
     ATVNNPRMPV SQKEVSPLSS HQTTECSNNS KSKPESGVSR AKSFLPVPRS KATQCSQNTK
     RSSSSSNTRQ IEINNNSKEE NWNLHKNEQI EKPNK