CTTB2_MUNRE
ID CTTB2_MUNRE Reviewed; 1642 AA.
AC Q07DW4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-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 Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000195; ABJ08878.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07DW4; -.
DR SMR; Q07DW4; -.
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..1642
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260409"
FT REPEAT 702..732
FT /note="ANK 1"
FT REPEAT 736..765
FT /note="ANK 2"
FT REPEAT 769..798
FT /note="ANK 3"
FT REPEAT 802..831
FT /note="ANK 4"
FT REPEAT 835..864
FT /note="ANK 5"
FT REPEAT 904..934
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 366..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 381..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1642 AA; 178011 MW; 47EDC664FFACBF50 CRC64;
MATDGASCEP DFSRAPEDAA GAPAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGASDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKHV VLMLVKECKQ
LSGKVLEEAQ KLEEVMAKLE EEKKKTSALE EELATEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLHREEA HTADLKEEID KMKKMIEQLK RGTDSKPGLS LPRKTKDRRS ISISVATEGP
MTRSVACQTD LVMESAEPVK KLPLTVPVKP AAGSPPVAAG AKGNACASAA AVRPGVERQV
SHGDLIGASL PAAPPPSANR IEENGPSTGS TADLTSSPTP VPSTVSPASG HTPAPPPHSL
HSPCANAPLH PGLNPRIQAA RFRFQGSNAN DPDQNGNTTQ SPPSRDVSPT SRDNLVAKQL
ARNTVTQALS RFTSPPAGAP PRPGAPPTGD VGTYPPVGRT SLKTPGGARV DRGNPPPIPP
KKPGLSQTPS PPHPQLKVIM DSSRASSTGI KADNKTVASP PSTLPQGSRV MNEENLSKSS
SPQLPPKPSI DLTVAPAGCA VSALATSQVG AWPAETPGLN QSACSERSLV IPTTTASSSS
IHPVNASSRR AGASDSLLVT ASGWSPSLTP LLMSGGPAPL AGRPTLLQQA AAQGNVTLLS
MLLNEEGLDI NYSCEDGHSA LYSAAKNGHT DCVRLLLNAE AQVNVADTNG FTPLCAAAAQ
GHFKCVELLI AYDANINHAA DGGQTPLYLA CKNGNKECIK LLLEAGTDRS VKTRDGWTPI
HAAVDTGNVD SLKLLMYHRA PAHGNKLREE PGLAIFDLDQ EEERHEGTSK PVVPADLINH
ADSEGWTAAH IAASKGFKNC LEVLCRHGGL EPERRDKCNR TAHDVATDDC KHLLENLNAL
KIPLRISVGE IEPGNYGADD FECENTICAL NIRKQTSWDD FSKAVSQALT NHFQAISSDG
WWSLEDMTFN STTDSSIGLS ASSVRSITLG TVPWSAGQSF AQSPWDFVRT NKAEQVTVLL
SGPQEGCLSS VTYASMIPLQ MLQNYLRLVE QYHNVIFHGP EGSLQDYIAH QLALCLKHRQ
MAAGFPCEIV RAEVDADFSK EQLVDLFISN ACLIPVKQSP ANKKIIVILE NLEKSSLSEL
LGDFLGPLEN HSTESPCTFQ KGNGTSECYY FHENCFLMGT IAKACLQGSD LLVQQHFRWV
QLRWDGEPMQ GLLRRFLRRK VVNKFRGQVP SPCDPVCKTV DWALAVWRQL NSCLARLGTP
EALLGPKYFL SCPVIPGHAQ ATVKWMSKLW NAVIAPRVQE AILSRASVKR QPGLGQTTKN
PSQGQQAVVR AALSILLNKA VLHGCPLQRA ELDQHTADFK GGSFPLSIVS SYGSCNKKKE
SGAWRKVSTS PRKKSGRFSS PTWNKPDLSE EGIKSNTILQ LNCNRNASLS NQKSLENDLS
LTLDLDQRLS LGSDDEADLV KELQSMCASK SESDISKIAD SRDDLRRFDS SGNNPVFSAT
VNNPRMPVSQ KEVSPLSSHQ TTECSNSKSK TELGVSRVKS FLPVPRSKAT QCSQNTKRSS
SSSNTRQIEI NNNSRDLEPT QK