CTTB2_ORNAN
ID CTTB2_ORNAN Reviewed; 1635 AA.
AC Q07DZ5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-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 Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258;
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; DP000185; ABI93681.1; -; Genomic_DNA.
DR RefSeq; NP_001229664.1; NM_001242735.1.
DR AlphaFoldDB; Q07DZ5; -.
DR SMR; Q07DZ5; -.
DR STRING; 9258.ENSOANP00000026834; -.
DR GeneID; 100078686; -.
DR KEGG; oaa:100078686; -.
DR CTD; 83992; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR InParanoid; Q07DZ5; -.
DR OrthoDB; 264951at2759; -.
DR Proteomes; UP000002279; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; IBA:GO_Central.
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; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 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; 4.
PE 3: Inferred from homology;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1635
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260412"
FT REPEAT 697..727
FT /note="ANK 1"
FT REPEAT 731..760
FT /note="ANK 2"
FT REPEAT 764..793
FT /note="ANK 3"
FT REPEAT 797..826
FT /note="ANK 4"
FT REPEAT 830..859
FT /note="ANK 5"
FT REPEAT 893..923
FT /note="ANK 6"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..273
FT /evidence="ECO:0000255"
FT COMPBIAS 193..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1618
FT /note="Polar 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 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1635 AA; 176029 MW; ACA344FEF8F9848C CRC64;
MATAGGSGQP LCSGPPARTS ALPAKKEFDV DTLSKAELRM LLSVMEGELE ARDVVIEALR
ARRKEVFIQE RYGRFNLNDP FLALQRDYEA GAGEAEKKPV CTNPLSILEA VMAHCRKMQE
RMSAQLAAAE SRQKKLEMEK SQLHVLQQEH RKLSARLEDE RGKNKQVVLM LVKECKQLSS
KVGEEGEKLE EAASKLDAEK RKTGELEGAL SAERQKSSQM EARMEKQLSE FDTEREQLRA
KLSREEALTA DLREEIDKMR KTIEQLRKGN DHKPSLSLPR GKAKDRRSVS VSVGTEGPAS
RAAACQTDPV VEGADPVKKP PVAVPAKPSS AGPLASGTTK GGVGKPSVGR QFSHGDLLTS
SSPSIPGPPR IQENGPSSGS TPEPTGSALM PLLNNAPPPA ASQNHSLTSS TPNLHSPCAN
AASYPALNPR VQAARFRFQG NANDQDQNGN TTQSPPSREV SPTSRDNLVV RQLARNTVTQ
ALSRFTGPQA GAPASPRAPH PGEGGTGPPS GGRASAKTPN APRVDRGNPP PIPPKKPGLS
QTPSPPHPQL KVLKDSGRPA NAGAKVDSKT GVPPPSAPPH GIRVMNEENL AKSSSPQPPP
KPAGDLAPAV PAGCALPAVA ASQVGACLGC NPGPSQPACS ESSHAIPTAI ACSSSINPVS
ASSCAPWASH SLLVAASGWP PSLTPLLTSC GPVSLGGRPT RLHQAAAQGN VTLLSVLLNE
EGLDINHACE DGSSALYSAA KNGHTDCVRL LLNANAQVDD ADKNGFTPLC SAAAQGHVKC
AELLIAYHAD INHAAEGGQT PLYLACKNGN NECIKLLLEA GTDRSITTSD GWTPVHAAVD
SGNVDSLTLL MYYGGPESEN SGSKDQTGLG SREESRGAMP VISADLINQA DKEGWTAAHI
AASKGLKNCL EILCGHGRLE AERKDKCDRT AHDVATDDCK HLLENLNALK ISVRISVGEK
QPAVCGSDDF EAENTICALN IRKQTSWDDF SKAVSQAVTN HFQAISSDGW KRLEDLTFNN
ATESSVGLSV SSILSVKLGS VTWSTGQSFS QPPWDFLQKN KVEHVTVFLS GPQEGCLSSV
TYASMIPLQM LQNYLRLVEQ YHNVVFHGPE GSLQDYIAHQ IALCLKHKQT AAGFPCEIVK
AEVDTNFSKE QLVELFINSA CLIPVKQPPV SKKVIVILEN LEKASLSELL GDFLAPLENR
SSENPYTFQK GNGVANSYYF HENCFLVGTI AKSCLQGSDL LVQQHFRWVQ LRWDGEPIHG
LLQRFLRRKV MNKFRGKVPS PCDPVCKIID WILTVWHQLN SCLSRLGTPE ALIGPRYFLS
CPVVPGHAHV TVKWMSKLWN AVIAPKVQEA ILSRASVKRP AVRPSPSQGQ QAVVKAALSI
LLNKAILHGC PLPRAELDQY MAEFRSGCFP LSMVSSYSGS HRKKGESGSW RKVNTSPRKK
SGLSSSQTWT KQEATKDGVR NDTGHQNGNS IASLVKQKSL ENGHPQVLHL DQRLSLGSDD
EVDLVRELQS MCSSKSESDI SKIADSKDDF RMFGSSRTDP DPEFSPTMSD RSLPSSEKEV
CPLSSNPTLE CSNNTPKPES GVSRVKSFLP VPRNKVAQCS PNPKRSNSSS SSNTRQREIN
NNLKEEFWVL RKNIQ
