ID   CTTB2_DASNO             Reviewed;        1665 AA.
AC   Q07E41;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, 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   Dasypus novemcinctus (Nine-banded armadillo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX   NCBI_TaxID=9361;
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; DP000181; ABI93635.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07E41; -.
DR   SMR; Q07E41; -.
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..1665
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260404"
FT   REPEAT          711..741
FT                   /note="ANK 1"
FT   REPEAT          745..774
FT                   /note="ANK 2"
FT   REPEAT          778..807
FT                   /note="ANK 3"
FT   REPEAT          811..840
FT                   /note="ANK 4"
FT   REPEAT          844..873
FT                   /note="ANK 5"
FT   REPEAT          914..944
FT                   /note="ANK 6"
FT   REGION          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1447..1495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1575..1665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          120..277
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        384..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..559
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1575..1609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1619..1665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         500
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1665 AA;  181265 MW;  41CEA21CAE0EA79E CRC64;
     MATDGASCEP NFSRAPEDVG ATAEAAVATK EFDVDTLSKS ELRMLLSVME GELEARDLVI
     EALRARRKEV FIQERYGRFN LNDPFLALQR DYEAGAGEKE KKPVCTNPLS ILEAVMAHCR
     KMQERMSTQL AAAESRQKKL EMEKLQLQAL EQEHKKLATR LEEERGKNKH VVLMLVKECK
     QLSGKVIEEA QKLEEVMTKL EEEKKKTNEL EEELSAEKRR STEMEAQLEK QLSEFDIERE
     QLRAKLNREE AHTTDLKEEI DKMKKMIEQL KRGNDSKPSL SLPRKTKDRR LVSISVGTEG
     PVTRSVACQT DLVIESTDHV KKLPLTVPVK PSTGSPLVSA PAKGNVCPSV PLLRPGIDRQ
     ASHGDLIVSS VPAVPPPNAN RIEENGPSIG STPDLASSTP PLPSNAAPPT GQTSGIASQN
     YSQASSMHSL HSPCANASLH PGPNPRIQAA RFRFQGNAND QDQNGNTTQS PPSRDVSPTS
     RDNLVAKQLA RNTVTQALSR FTSPQASASP RPGAPPTGDI GTHPAVSRTS LKTPGLARVD
     RGNPPPIPPK KPGLSQAPSP PHPQLKAIMD SSRASNAGAK VDNKTVASPP ASLPQGNRVI
     NEENLPKSSS PQLPPKPSID LTVAPAGCAV SALATSQVGA RPAETPGPTQ PACSDSSLVI
     PTTIAFRSSI NPVSASASRP GASDSLLVTA SGWSPSLTPL LMSGGPAPLA GRPTLLQQAA
     AQGNVTLLSM LLNEEGLDIN YSCEDGHSAL YSAAKNGHTD CVRLLLNAKA QIDAADKNGF
     TPLCAAAAQG HFECVELLIA YHANIDHAAD GGQTPLYLAC KNGNKECIKV LLEAGTDRSV
     KTRDGWTPVH AAVDTGNVDS LKLLMYHRAP TLGHSLNEEE PEPGAFDLDQ GQEGSEGTAK
     PVVPTDLINH ANREGWTAAH IAASKGFKNC LEILCRHGGL EPERKDKCNR TVHDVATDDC
     KHLLENLNAL KIPLRISVGE TQPGSYGCDD FECENTICAL NIHKQTSWDD FSKAVSQALT
     NHFQAISSDG WWSLEDMTFN NTPEPSIGLS ARSILSITLG NVPWSAGQCF TQAPWDFMRK
     NKAEQVTVLL SGPQEGCLNS VTYASMIPLQ MLQNYLRLVE QYHNVIFHGP EGSLQDYIAH
     QLALCMKHRQ MAAGFSCEIV RAEVDAGFSK EQLIDLFINS ACLIPVKQSP VTKKIIIILE
     NLEKSSLSEL LGDFLAPLEN RSTESPCTFQ KGNGTSECYY FHENCFLMGT IAKTCLQGSD
     LLVQQHFRWV QLRWDGEPMH GLLQRFLRRK VVNKFRGQAP SPCDPVCKMV DWALAVWHQL
     NSCLARLGTP DALLGPKYFL SCPVVPGHAQ VTVKWMSKLW NAIIAPKVQE AILSRASVKR
     QPGLRQTTAK KPPSQGQQAV VKAALSILLN KAVLHGCPLL RAELDQYITD FKGGSFPLSI
     VSSYNSCSKK KGENGAWRKV STNPRKKSGR FSSPTWSKPD LGEEGTKNKT MSQPNCNRIA
     SLSKQKSSEN DPSSMLNLDQ RLSLGSDDEA DLVKELQSMC SSKSESDISK IADSRDDLRR
     FDSSENSPAF SAAINNLRMP VSQKEVSPVS SHQTTKRSTS TSKTELSVSR VKSFLPVPRS
     KVSQCSQNTK RSSSSSNTRQ TELNNNSKEE IWNLCKNEQV QKPNK