CTTB2_RHIFE
ID CTTB2_RHIFE Reviewed; 1663 AA.
AC Q2IBB2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479;
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 (JAN-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; DP000028; ABC87481.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2IBB2; -.
DR SMR; Q2IBB2; -.
DR Proteomes; UP000472240; 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_0000260415"
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..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 497..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..439
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 539..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1607
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; 180439 MW; F13B0A1129B34DD4 CRC64;
MATDGASCEP DFSRAPEDAA GATAEAAKQD FDVDALSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCANPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQALE LEHKKLAARL EEERGKNKHV VLMLVKECKQ
LSGRVIEEAQ KLEDVMAKLD EEKKKTSALE EELSTEKRRS TDMEAQMEKQ LSEFDTEREQ
LRAKLHREEA HTADLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGP
MTRSVACQTD PVIESTDHVK KLPLTVPVKP STGSPLVSAN AKGNACTSAA LVRPGIDRQA
SHGDLIGSSL PTVPPPSATR VEENGPSTDS APDLTNSTPP VPSSTAPPAM QTPGAAPQSH
SQAPLHSLHS PSANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
NLVAKQLARN TVTQALSRFT GPPAGAPPRH GVPPSGDVGT YPPVGRTNVK TPGVARVDRG
NPPPIPPKKP GLSQAPSPPH PQLKVVMDSS RAPSAGAKVD NKTVASPPSS LPPGNRVINE
ENLPKPTTPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AETPGLNQPA CSERSLVIPT
TIAFCSSINP VSASSCRAGA SDSLLVTASG WSPSLTFLLM SGGPAPLAGR PTLLQQAAAQ
GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLNAEAQV DAADKNGFTP
LCAAAAQGHF KCVELLTAYD ADINHTADGG QTPLYLACKN GNKECIKLLL EAGSDRSVKT
SDGWTPLHAA VDTGNVDSVK LLMYHSAPAR GHFLHEEEPE SGVCGLDGGE GSPEGTAKPV
VPADLINQAD REGWTAAHIA ASKGFKNCLE ILCRHAGLEP DRREKCNRTV HDVATDDCKH
LLENLHAFKI PLRISVGEVQ PDIYCSDDFE CENTICILNI RKQTSWDDFS KAVSQALTNH
FQAISSDGWW SLEDVTCNNT ADSSIGLGAS SVRSVTLGNV PWSVGQSFAQ SPWDFLRKNK
AEQVSVLLSG PQEGCLSSVT YASLIPLQVL QNYLRLVEQY HNVIFHGPEG SLQNYIAHQL
ALCMKHRQIA AGFSCEIVRA QVDASFSKEQ LADLFISSAC LIPVKQSPVN KKIIIILENL
EKSSMSELLG DFLAPLENRS PESPCTFHKG NGTSGCYYFH EHCFLMGTVA KACLQGSDLL
VQQHFRWVQL RWDGEPMQSL LPRFLRRRAV NKFRGQVPSP CDPGCKAVDW AAAVWRQLNS
CLTRLGTPEA LLGPKYFLSC PVIPGHAQVT VKWMCKLWNA VIAPRVQEAI LSRASVERHA
GFAQTTAKKT PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELDQHTADFK GGSFPLSIVS
SYNCCSKKKG ENGTWRKVST SPRKKSGHFS SPTWNKPDLN EEGIRNTTTS QLNCNRNASL
SKQKSLENDL SSTLTLDQKL YLGSDDEADL IKELQSMCSS KSESDISKIA DSRDDLRRFD
SSRNNPTFSA TVNNLRMPVS EKEVSPLSSH QTTECNDSKS KTESGVSRVK SFLPVPQSKA
TLCSQNTKRS SSSSNTRQIE INNNSKEEIW NLHKNEQVEK PNK
