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Database: UniProt
Entry: CTTB2_MUSPF
LinkDB: CTTB2_MUSPF
Original site: CTTB2_MUSPF 
ID   CTTB2_MUSPF             Reviewed;        1645 AA.
AC   Q07E15;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669;
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; DP000183; ABI93661.1; -; Genomic_DNA.
DR   RefSeq; XP_004741960.2; XM_004741903.1.
DR   AlphaFoldDB; Q07E15; -.
DR   SMR; Q07E15; -.
DR   Ensembl; ENSMPUT00000007185.1; ENSMPUP00000007067.1; ENSMPUG00000007124.1.
DR   GeneID; 101671972; -.
DR   KEGG; mpuf:101671972; -.
DR   CTD; 83992; -.
DR   eggNOG; ENOG502QWG2; Eukaryota.
DR   GeneTree; ENSGT00940000158293; -.
DR   HOGENOM; CLU_004926_0_0_1; -.
DR   InParanoid; Q07E15; -.
DR   OMA; MCPVEAL; -.
DR   OrthoDB; 5395797at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
DR   CDD; cd14686; bZIP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   PANTHER; PTHR24166:SF27; CORTACTIN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR24166; ROLLING PEBBLES, ISOFORM B; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF09727; CortBP2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 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..1645
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260410"
FT   REPEAT          706..736
FT                   /note="ANK 1"
FT   REPEAT          740..769
FT                   /note="ANK 2"
FT   REPEAT          773..802
FT                   /note="ANK 3"
FT   REPEAT          806..835
FT                   /note="ANK 4"
FT   REPEAT          839..868
FT                   /note="ANK 5"
FT   REPEAT          909..939
FT                   /note="ANK 6"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1551..1645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1613..1638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         495
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1645 AA;  178410 MW;  10FC05FE92A20D44 CRC64;
     MATDGASCEP DFSRAPEDAE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGEKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSTQLA AAESRQKKLE MEKLQLQGLE QEHKQLAARL EEERGKNKHV VLMLVKECKQ
     LSGKVLDEAQ KLEDVLARLE EEKKKTGTLE EQLSAEKRKS TEMEAQMEKQ LSEFDTEREQ
     LRAKLHREEA HTTDLKEEID KMKKMIEQLK RGNDSKPSLS LPRKTKDRRS VSISVGTEGP
     VTRSVACQTD PAVESIDHVK KLPLTVPVKP PTGSPLVSAN TKGNVCPSAA LGRPGIDRQA
     SHGDLIVSSL PTVPPPSASK IEENGPSTGS PSSTPPLPNS TAPPTVQTPT IAPQSHAQAA
     PGHSLHSPCA NAALHPGLNP RIQAARFRFQ GNANDPDQNG NTTQSPPSRD VSPTSRDSLV
     AKQLARNTVT QALSRFTSPP AGAPPRPGAP STGDVGTCPP VGRTSLKTPG VARVDRGNPP
     PIPPKKPGLS QTPSPPHPQL KVIMDSSRAS SAGAKVDNKT MASPPSTLPQ GNRVINEENL
     PKSSSPQLPP KPSIDLTVAP AGCGVSALAT SQVGAWPAET PGLSQPACSE SSLVIPTTIA
     FCSSINPVSA SSCRTGASDS LLVAASGWSP SLTPLLMSGG PAPLAGRPTL LQQAAAQGNV
     TLLSMLLNEE GLDINYSCED GHSALYSAAK NGHTDCVRLL LNAEAQVNAA DKNGFTPLCA
     AAAQGHFKCV ELLIAYNANI NHAADEGQTP LYLACKNGNK ECIKHLLEAG TDRSVKTRDG
     WTPVHAAVDA GNVDSLKLLM YHRAPARRNS LHEEEPESGV FDLDQGEESP EGTSKPVIPA
     DLINHADREG WTAAHIAASK GFKDCLEILC KHRGLEPERR DKCNRTAHDV ATDDCKHLLE
     NLNALKIPVR ISGGESPPGN YGSDDFECEN TICALNIRKQ TSWEDFSKAV SQALTNHFQA
     ISSDGWRSLE DGTFNNTTDS CIGLSTSSVR SVMLGNVPWS TGQSFSQSPW DFMKKNKAEQ
     VTVFLSGPQE GCLSSVTYTS MIPLQMLQNY LRLVEQYHNV IFHGPEGSLQ DYVAHQLALC
     MKHRQMAAGF TCEIVRAKVD AGFSKEQLGD LFISSACLIP VKQSPMNKKV IIVLENLEKC
     SLSELLGDFL APLENRSTES PWILQKGNGT SECYYFHENC FLMGTIAKAC LQGSDLLVQQ
     HFRWVQLRWD GEPMQGLLPR FLRRKVMNKF RGQVPSPCDP VCKTVDWALA VWRQLNSCLA
     RLGTPEALLG PEYFLSCPVV PGHAQATVKW MAKLWNAVIA PRVQEAVLSR ASVRRQPGLG
     LTAARSRPSQ GQQAVVKVAL SILLNKAVLH GCPLQRADLD QHVADFKGGA FPLSIVSSYN
     SCSRKKGESG AWRKVSTSPR KKSGRFSPPS WSKPGPSEEG IKVKAISQLN YNRNASLSKQ
     KSLENDLSLT LNLEQRLSLG SDDEADLVQE LQSMCSSKSE SDISKIADSR DDLRSFDSPG
     NSPAFSATVN PRMPVSPKEV SPFSSHQPTE CSNSQSKMEL GVSRVKSFLP VPRSKVTQCS
     QNTKRSSSSS NTRQIEINNN SKEEI
//
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