CTTB2_EULMM
ID CTTB2_EULMM Reviewed; 1653 AA.
AC Q2IBF8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Eulemur macaco macaco (Black lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Eulemur.
OX NCBI_TaxID=30603;
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; DP000024; ABC87445.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2IBF8; -.
DR SMR; Q2IBF8; -.
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..1653
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260405"
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..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 268..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 488
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1653 AA; 179236 MW; C99EE1BB9C077D19 CRC64;
MATDGASCEP DASRAPEEAA GATAEAARKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
LSGKVIEEAQ KLEEVMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRS VSISVGTEGP
LTRSVACQTD LAVESTEHVK KSPLTVPVKP SPGSAKGSVG ANAALVRPGI DRQASHGDLI
GASLPTVPPA SANRIEENGP STGSPPDLTS SAAQSPAAAP HGLPPAHGSQ SGSQSPCASA
PPHSAPPHPG LNPRVQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD NLVAKQLARN
TVTQALSRFT SPPVGAAPRP GASPTGDVGA HPPVGRTSLK TPGVARVDRG NPPPIPPKKP
GLSQTPSPPH PQLKVIMDSS RASNAGAKVD NKTVASSPPS SLPQGNRVIS EENLPKSSSP
QLPPKPSIDL TVAPAGCAVS ALATSQVGAW PAETPGLNQP ACSGSSLVIP TTTAFRSSIN
PVSASSCRPG ASDSLLVTAS GWSPSLTPLL MSGGPAPLAG RPTLLQQAAA QGNVTLLSML
LNEEGLDINY SCEDGHSALY SAAKNGHTDC VRLLLNAEAQ VNAADKNGFT PLCAAAAQGH
FECVELLIAY DAHINHAADG GQTPLYLACK NGNKECIKLL LEAGTDRSVK TRDGWTPVHA
AVDTGNVDSL KLLMYHGAPA HGNSLNEEEP ESDASDLDEG EESSEGKSKP VVPADLINHA
DREGWTAAHI AASKGFKNCL EILCRHRGLE PERRDKCNRT VHDVATDDCK HLLENLNALK
IPLRISVGEI QPGNYGSNDF ECENTICALH IRKQTSWDDF SKAVSQALTN HFQAISSDGW
WSLEDTAFNN TADSDIGLST SSVRAIMLGS VPWSAGQSLA QSPWDFMRKT KAEQVTVLLS
GPQEGCLSSV TYTSMIPLQM LQNYLRLVEQ YHNVIFHGPE GSLQDYIVHQ LALCLKHRQM
AAGFSCEIVS AEVDAGFSKE QLVDLFISSA CLIPVKQSPV KKKIIIILEN LEKSSLSELL
GDFLAPLEIR STESPCTFQK GNGLSECYYF HENCFLMGTI AKACLQGPDL LVQQHFRWVQ
LRWDGEPMQG LLQRFLRRKL VNKFRGQMPS PCDPVCKTIA WALSVWRQLN SCLARLGTPE
ALLGPKYFLP CPVVPGHAQA TVKWMSKLWN AVIAPRVQEA ILSRASVKRQ PGFGQTTTKK
HPSQGQQAVV KAALSILLNK AVLHGCPLPR AELDQHTADF KGGSFPLSLV SNYNSCSKKK
ESGAWRKVNT SPRRKSGRFS SPTWNKPDLS NEGIKNKTIS QLNCNKNASL SKQKSLENDL
SLMLNLDQSL SLGSDDEADL VRELQSMCSS KSESDISKIA DSRDDLRTFD SSGNNPAFSA
TANNPRMPVS QKEVSPLSSH QTTECSNNKS KTEPGVSRVK SFLPVPRSKV TQCSQNTKRS
SSSSNTRQIE INNNSKEENW NLHKNEHIEK LNK
