CTTB2_CALJA
ID CTTB2_CALJA Reviewed; 1662 AA.
AC Q2QLF8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
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 (OCT-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; DP000014; ABA90398.1; -; Genomic_DNA.
DR RefSeq; XP_002751825.1; XM_002751779.3.
DR AlphaFoldDB; Q2QLF8; -.
DR SMR; Q2QLF8; -.
DR STRING; 9483.ENSCJAP00000008924; -.
DR GeneID; 100412270; -.
DR KEGG; cjc:100412270; -.
DR CTD; 83992; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR HOGENOM; CLU_004926_0_0_1; -.
DR InParanoid; Q2QLF8; -.
DR OMA; MCPVEAL; -.
DR OrthoDB; 264951at2759; -.
DR TreeFam; TF325130; -.
DR Proteomes; UP000008225; 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..1662
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000226999"
FT REPEAT 708..738
FT /note="ANK 1"
FT REPEAT 742..771
FT /note="ANK 2"
FT REPEAT 775..804
FT /note="ANK 3"
FT REPEAT 808..837
FT /note="ANK 4"
FT REPEAT 841..870
FT /note="ANK 5"
FT REPEAT 911..941
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..275
FT /evidence="ECO:0000255"
FT COMPBIAS 401..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 497
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1662 AA; 181290 MW; 8BEDA031A0BD62C1 CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK PVCTNPLSIL EAVMAHCRKM
QERMSAQLAA AESRQKKLEM EKLQLQALEQ EHKKLAARLE EERGKNKQVV LMLVKECKQL
SGRVIEEAQK LEDIMAKLEE EKKKTNELEE ELSAEKRRSS EMEAQMEKQL SEFDTEREQL
RAKLNREEAH TTDLKEEIDK MKKMIEQLKR GSDSKPSLSL PRKTKDRRLV SISVGTEGTV
MRSVACQTDL VTESADHVKK LPLTMPVKPS TGSPLASANA KGSVCSSAAM ARPGIDRQAS
HGDLIGVSVP AFPPSSANRI EENGPSTGST PDPTSSIPPL PSNAAPSTAQ TPGITPQNSQ
APPMHSLHSP CANASLHPGL NPRIQAARFR FQGNANDPDQ NGNTTQSPPS RDVSPTSRDN
LVAKQLARNT VTQALSRFTG PQAGAPPRPG APPTGDVSTH PSVGRTSVKT HGIARVDRGN
PPPIPPKKPG LSQTPSPPHP QLKVIIDSSR ASNTGAKGDN KTVASPPSSL PQGNRVINEE
NLPKSSSPQL PPKPSIDLTV APAGCAVSAL ATSQVGAWPA ATPGLNQPAC SDSSLIIPTT
IAFCSSINPV SASSCRPGAS DSLLVTASGW SPSLTPLLMS GGPAPLAGRP TLLQQAAAQG
NVTLLSMLLN EEGLDINYSC EDGHSALYSA AKNGHTDCVR LLLSAEAQVN AADKNGFTPL
CAAAAQGHFE CVELLIAYDA NINHAADGGQ TPLYLACKNG NKECIRLLLE AGTDRSVKTT
DGWTPVHAAV DTGNVDSLKL LMYHRVPAHG NSFSEEESES GVFDLDEGEE SPEGKSKPVV
TADFINHANR EGWTAAHIAA SKGFKNCLEI LCRHGGLETE RRDKCNRTVH DVATDDCKHL
LENLNALKIP LRISVGEIEP SNYGSDDFEC ENTICALNIR KQTSWDDFSK AVSQALTNHF
QAISSDGWWS LEDMTCNNTT DSNIGLSARS IRSITLGNVP WSVGQSFVQS PWDFMIKNKA
EHITVLLSGP QEGCLSSVTY ASMIPLKMMQ NYLRLVEQYH NVIFHGPEGS LQDYIVHQLA
LCLKHRQMAA GFSCEIVKAE VDAGFSKKQL LDLFISSACL IPVKQSPVKK KIIIILENLE
KSSLFELLRD FLAPLENRST ESPCTFHKGN GMSECYYFHE NCFLMGTIAK ACLQGSDLLV
QQHFRWVQLR WDGEPMQGLL QRFLRRKVVN KFRGQVPPPC DPVCKIVDWA LSVWRQLNSC
LSRLGTPEAL LGPKYFLSCP VVPGHAQVTV KWMSKLWNGV ITPRVQEAIL SRASVKRQAG
FRQTIAKRHP SQGQQAVVKA ALSILLNKAV LHGCPLPRAE LEQHRADFKG GSFPLSIVSS
YNSCSKKKGE SGAWRKVNTS PRRKSGRFSL PTWNKPDLST EGIKNKTLSQ LNCNRNASLS
KQMSLENDVS LTLNLDQRLS LGSDDEADLV KELQSMCSSK SESDISKIAD SRDDLRMFDS
SGNNPVFSAT INNLRMPVSQ KEVCPLSSHH TTECSNSKSK TELGVSRVKS FLPVPRSKVT
QCSQNTKRSS SSSNTRQIEI NNNSKEENWN LHKNEHLEKP NK
