CTTB2_SAIBB
ID CTTB2_SAIBB Reviewed; 1659 AA.
AC Q09YG9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432;
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; DP000180; ABI75311.1; -; Genomic_DNA.
DR RefSeq; XP_003921100.1; XM_003921051.2.
DR AlphaFoldDB; Q09YG9; -.
DR SMR; Q09YG9; -.
DR STRING; 39432.ENSSBOP00000032993; -.
DR Ensembl; ENSSBOT00000049894; ENSSBOP00000032986; ENSSBOG00000032674.
DR GeneID; 101036139; -.
DR KEGG; sbq:101036139; -.
DR CTD; 83992; -.
DR GeneTree; ENSGT00940000158293; -.
DR OMA; MCPVEAL; -.
DR OrthoDB; 264951at2759; -.
DR Proteomes; UP000233220; 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; 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..1659
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260416"
FT REPEAT 705..735
FT /note="ANK 1"
FT REPEAT 739..768
FT /note="ANK 2"
FT REPEAT 772..801
FT /note="ANK 3"
FT REPEAT 805..834
FT /note="ANK 4"
FT REPEAT 838..867
FT /note="ANK 5"
FT REPEAT 908..938
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 389..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 494
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1659 AA; 180557 MW; EF7DBCFF0B4B2C25 CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCRK
MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELSAEKQRS TEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
VTRSVACQTD LVTESADHVK KLPLTMPVKP STGSPLASAN AKGSAAMARP GIDRQTSHGD
LIGVSVPAFP PSSANRIEEN GPSTGLTPDP TSSTPPLPGN AAPPTAQTPG ITPQNSQAPP
MHSLHSPCAN ASLHPGLNPR IQAARFRFQG NANDPDQNGN TTQSPPSRDV SPTSRDNLVA
KQLARNTVTQ ALSRFTGPQA GAPPRPGAPP TGDVSTHHSV GRTGVKTHGV ARVDRGNPPP
IPPKKPGLSQ TPSPPHPQLK VIIDSSRASN TGAKGDNKTV ASPPSSLPQG NRVINEENLP
KSSSPQLPPK PSIDLTVAPA GCTVSALATS QVGAWPAATP GLNQPACSGS SLAIPTTIAF
CSSINPVSAS SCRPGASDSL LVTASGWSPS LTPLLMSGGP APLAGRPTLL QQAAAQGNVT
LLLMLLNEEG LDINYSCEDG HSALYSAAKN GHTDCVRLLL SAEAQVNAAD KNGFTPLCAA
AAQGHFECVE LLIAYDANIN HAADGGQTPL YLACKNGNKE CIKLLLEAGT DRNVKTTDGW
TPVHAAVDTG NVDSLKLLMY HRVPAHGNSF SEEESESGVF DLDGGGESPE GKSKPVVTAD
FINHANREGW TAAHIAASKG FKNCLEILCR HGGLETERRD KCNRTVHDVA TDDCKHLLEN
LNALKIPLRI SVGEIEPSNY GSDDFECENT ICTLNIRKQT SWDDFSKAVS QALTNHFQAI
SSDGWWSLED VTCNNSTDSN IGLSSRSIRS ITLGNVPWSV GQSFLQSPWD FMMKNKAEHI
TVLLSGPQEG CLSSVTYASM IPLQMMQNYL RLVEQYHNVI FHGPEGSLQD YIVRQLALCL
KHRQMAAGFS CEIVRAEVDA GFSKKQLLDL FISSACLIPV KQSPVKKKII IILENLEKSS
LSELLRDFLA PLENRSAESP CTFQKGNGMS ECYYFHENCF LMGTIAKACL QGSDLLVQQH
FRWVQLRWDG EPMQGLLQRF LRRKVVNKFR GQVPPPCDPV CKIVDWALSV WRQLNSCLAR
LGTPEALLGP KYFLSCPVVP GHAQVTVKWM SKLWNGVITP RVQEAILSRA SVKRQPGLGQ
TTAKRHPSQG QQAVVKAALS ILLNKAVLHG CPLPRAELEQ HRADFKGGSF PLSIVASYNS
CSKKKGESGA WRKVNTSPRR KSGRFSLPTW NKPDLSTEGI KSKTLSQLNC NRNASLSKQK
SLENDVSLTL NLDQRLSLGS DDEADLVKEL QSMCSSKSES DISKIADSRD DLRMFDSAGN
NPVFSAAINN LRMPVSQKEV CPLSSHQTTE CSNSKSKTEL GVSRVKSFLP VPRSKVTQCS
QNTKRNSSSS NTRQIEINNN SKEENWNLHK NEHLEKPNK
