CTTB2_HORSE
ID CTTB2_HORSE Reviewed; 1665 AA.
AC Q2QLA2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
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; DP000020; ABB89807.1; -; Genomic_DNA.
DR RefSeq; NP_001107617.1; NM_001114145.1.
DR AlphaFoldDB; Q2QLA2; -.
DR SMR; Q2QLA2; -.
DR STRING; 9796.ENSECAP00000022668; -.
DR PaxDb; Q2QLA2; -.
DR GeneID; 100071265; -.
DR KEGG; ecb:100071265; -.
DR CTD; 83992; -.
DR InParanoid; Q2QLA2; -.
DR OrthoDB; 264951at2759; -.
DR Proteomes; UP000002281; 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 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; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1665
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000227001"
FT REPEAT 710..740
FT /note="ANK 1"
FT REPEAT 744..773
FT /note="ANK 2"
FT REPEAT 777..806
FT /note="ANK 3"
FT REPEAT 810..839
FT /note="ANK 4"
FT REPEAT 843..872
FT /note="ANK 5"
FT REPEAT 914..944
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..276
FT /evidence="ECO:0000255"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
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; 181385 MW; 1A0E6F32D986C340 CRC64;
MATDGASCEP DFSRSPEDAA GATAEAAKKE FDVDTLSKSE LLMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLASRL EEERGKNKHV VLMLVKECKQ
LSSKVIEEAQ KLEEVMAKLE EEKKKTSALE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLHREEA HTTDLKEEID KMKKMIEQLK RGNDNKPSLS LPRKTKDRRL VSISVGTEGP
MTRSVACQTD PVIESSDHVK KLPLTMPVKP STGSPLVSAN AKGNVCTNAA LVRPGIDRQA
SHGDLIGSSL PTVPPPSANR IEENGPSTGS TADLTSSTPP LPNNAAPPTV QTPGVAPQSY
SQASPMHSLH SPCANASLHP GLNPRIQAAR FRFQGNANDP DQNGNTTQSP PSRDVSPTSR
ENLVAKQLAR NTVTQALSRF TSPQAGAPPR PGVSPTGDVG TYPPVGRTSL KTPGVARVDR
GNPPPIPPKK PGLSQTPSPP HPQLKVIMDS SRASNAGAKV DNKTVASPPS SLPQGNRVIN
EENLPKSSSP QLPPKPSIDL TVAPAGCAVS ALATSQVGAW PAETPGLNQP ACSESSLVIP
TTIAFSSSIN PVSASSCRAG ASDSLLVTAS GWSPSLTPLL MSGGPAPLAG RPTLLQQAAA
QGNVTLLSML LNEEGLDINY SCEDGHSALY SAAKNGHTDC VRLLLNAEAQ VDAADKNGFT
PLCAAAAQGH FKCVQLLIAY DANINHAADG GQTPLYLACK NGNKECIKLL LEAGSDRSIK
TRDGWTPVHA AVDTGNVDSL KLLMYHRAPA HGSSLHKEEP ESSIFDLDRQ GEESPEGTFK
PVVPADLINQ ADREGWTAAH IAASKGFKNC LEILCRHGGL EPERRDKCSR TAHDVATDDC
KHLLENLNAL KIPLRISVGE IQPGNYGSDD FECENTICAL NIRKQTSWDD FSKAVTQALT
NHFQAISSDG WWSLEDMKFN NTTDSSIGLG ASSVRSITLG NVPWSAGQSF TQSPWDFMRK
NKAEQITVLL SGPQEGCLSS VTYTSMIPLQ MLQNYLRLVE QYHNVIFHGP EGSLQDYIAH
QLALCMKHRQ MAAGFSCEIV RAEVDAGFSK EQLVDLFISS ACLIPVKQSP VKKKIIIILE
NLERSSLSEL LGDFLAPLEN RCPESPCTFQ KGNGTAECYY FHENCFLMGT IAKACLQGSD
LLVQQHFRWV QLRWDGEPMQ GLLQRFLRRK VVNKFRGQVP SPCDPVCKTV DWALAVWRQL
NSCLARLGTP EALLGPKYFL SCPVIPGHAQ ATVKWMSKLW NAVIAPRVQD AILSRASVKR
QPGLGQTIAK KHPSQGQQAV VKAALSILLN KAVLHGCPLP RAELDQHTAD FKGGSFPLSL
VSSYNSCSKK KGESGAWRKV STSPRKKSSR FSSPTWNKPD LSEEGIKNKT ISQLNCNRNA
SLSKQKSFEN DLSLTLSLDQ RFSLGSDDEA DLVKELQSMC SSKSESDISK IADSRDDLRR
FDSPGNNPAF SATVNNPRMP VSQKEVSPLS SHQTTECSNS QSKTELGVSR VKSFLPVPRS
KVTPCSQNTK RSSSSSNTRQ IEINNNSKEE IWNLRKNEQV EKPNK
