CTTB2_NOMLE
ID CTTB2_NOMLE Reviewed; 1663 AA.
AC Q07DX4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853;
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; DP000194; ABJ08868.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07DX4; -.
DR SMR; Q07DX4; -.
DR STRING; 61853.ENSNLEP00000014299; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR InParanoid; Q07DX4; -.
DR Proteomes; UP000001073; 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..1663
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260407"
FT REPEAT 709..739
FT /note="ANK 1"
FT REPEAT 743..772
FT /note="ANK 2"
FT REPEAT 776..805
FT /note="ANK 3"
FT REPEAT 809..838
FT /note="ANK 4"
FT REPEAT 842..871
FT /note="ANK 5"
FT REPEAT 912..942
FT /note="ANK 6"
FT REGION 1..23
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 352..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 498
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1663 AA; 181147 MW; D699B03DA9FF4ED7 CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRREVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCKK
MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
LSGKVIEEAQ KLEDIMAKLE EEKKKTNELE EELSTEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRCL VSISVGTEGT
VTRSVACQTD LVTESADHMK KLPLTMPVKP STGSPLVSAN AKGSVCTSAT MARPGIDRQP
SHGDLIGASV PAFPPPSANR IEENGPSTGS TPDPTSSTPP LPSNAAPPTT QTPGIAPQNS
QAPPIHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
NLVAKQLARN TVTQALSRFT SPQAGAPSRP GAPPTGDVGT HPPVGRTSLK THGVARVDRG
NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTAAKVD NKTVASPPSS LPQGNRVINE
ENLPKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQV NAADKNGFTP
LCAAAAQGHF ECVELLIAYD ANINHAADGG QTPLYLACKN GNKECIKLLL EAGTNRSVKT
TDGWTPVHAA VDTGNVDSLK LLMYHRILAR GNSFNEEGSE SSVFDLDGGE ESPEGISKPV
VPADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLEP ERRDKCNRTV HDVATDDCKH
LLENLNALKI PLRISVGEIE PSNYGSDDLE CENTICALNI RKQTSWDDFS KAVSQALINH
FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGQSFTQ SPWDFMRKNK
AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
ALCLKHRQMT AGFSCEIVRA EVDAGFSKEQ LLDLFISSAC LIPVKQSPSK KKIIIILENL
EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFKGQAPSP CDPVCKIVDW ALSVWRQLNS
CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VIAPRVQEAI LSRASVKRQP
GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELDQHTADFR GGSFPLSIVS
SYNSCNKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGMKNKTIS QLNCNRNASL
SKQKSLENDL SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDIRMFD
SSGNNRVLSA TINNLRMPVS QKEVSPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
TQCSQNTKRS SSSSNTRQIE INNNSKEENW NLHKNEHLEK PNK
