ID   CTTB2_SHEEP             Reviewed;        1641 AA.
AC   Q09YI1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=CTTNBP2; Synonyms=CORTBP2;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
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; DP000179; ABI75299.1; -; Genomic_DNA.
DR   RefSeq; NP_001182240.1; NM_001195311.1.
DR   AlphaFoldDB; Q09YI1; -.
DR   SMR; Q09YI1; -.
DR   STRING; 9940.ENSOARP00000010942; -.
DR   Ensembl; ENSOART00000011100; ENSOARP00000010942; ENSOARG00000010183.
DR   GeneID; 100126575; -.
DR   KEGG; oas:100126575; -.
DR   CTD; 83992; -.
DR   eggNOG; ENOG502QWG2; Eukaryota.
DR   HOGENOM; CLU_004926_0_0_1; -.
DR   OMA; MCPVEAL; -.
DR   OrthoDB; 264951at2759; -.
DR   Proteomes; UP000002356; Chromosome 4.
DR   Bgee; ENSOARG00000010183; Expressed in mitral valve and 51 other tissues.
DR   ExpressionAtlas; Q09YI1; baseline.
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..1641
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000260414"
FT   REPEAT          702..732
FT                   /note="ANK 1"
FT   REPEAT          736..765
FT                   /note="ANK 2"
FT   REPEAT          769..798
FT                   /note="ANK 3"
FT   REPEAT          802..831
FT                   /note="ANK 4"
FT   REPEAT          835..864
FT                   /note="ANK 5"
FT   REPEAT          903..933
FT                   /note="ANK 6"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1544..1641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        371..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..510
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..550
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1452..1468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1550..1595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1605..1641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         491
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ   SEQUENCE   1641 AA;  178220 MW;  C2C1A5C3CE6F216C CRC64;
     MATDGASCEP DFSRAPEDAA GAPAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGASDKEK KPVCTNPLSI LEAVMAHCRK
     MQERMSTQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKHV VLMLVKECKQ
     LSGKVLEEAQ KLEEVMAKLE EEKKKTSALE EELATEKRRS AEMEAQMEKQ LSEFDTEREQ
     LRAKLHREEA HTTDLKEEID KMKKMIEQLK RGNDSKPSLS LPRKTKDRRL VSISVATEGP
     MTRSVACQTD LVTETAEPLK KLPLTVPVKP AAGSPLVSAS AKGNACASAA SVRPGIERQV
     SHGDLIGSSL PTVPPPSTDR IEENGPSTGS TPDLTSSPTA LPSTVSPASG HTPTPPPHSL
     HSPCANAPLH PGLNPRIQAA RFRFQGSNAN DPDQNGNTTQ SPPSRDVSPT SRDTLVAKQL
     ARNTVTQALS RFTSPPAGAP PRPGAPPTGD VGTYPPVGRT SLKTPGGARV DRGNPPPIPP
     KKPGLSQTPS PPHPQLKVIM DSSRASSTGI KADNKTVASS PSSLPQGNRV INEENLSKSS
     SPQLPPKPSI DLTVAPAGCA VSALATSQVG AWPAETPGLN QPACSESSLV IPTTTAFRSS
     INPVSASSRR AGASDSLLVT ASGWSPSLTP LLMSGGPAPL AGRPTLLQQA AAQGNVTLLS
     MLLNEEGLDI NYSCEDGHSA LYSAAKNGHT DCVRLLLNAE AQVNAADKNG FTPLCAAAAQ
     GHFKCVELLI AYDANINHAA DGGQTPLYLA CKNGNKECIK LLLEAGTDRS VKTRDGWTPI
     HAAVDTGNVD SLKLLMYHGA PAHGNKLQEE PGLAIFDLDQ EEHHEGTSKP VVPADLINHA
     DSEGWTAAHI AASKGFKNCL EVLCRHGGLE PERRDKCNRT AHDVATDDCK HLLENLNALK
     IPLRISVGEI EPGNYGADDF ECENTICALN IRKQTSWDDF SKAVSQALTN HFQAISSDGW
     WSLEDMTFNS TTDSSIGLSA SSVRSITLGS VPWSAGQSFT QSPWDFMRTN KAEQVTVLLS
     GPQEGCLSSV TYASMIPLQM LQNYLRLVEQ YHNVIFHGPE GSLQDYIAHQ LALCLKHRQM
     AAGFPCEIVR AEVDADFSKE QLVDLFISSA CLIPVKQSPA NKKIIIILEN LEKSSLSELL
     GDFLGPLENH STESPCTFQK GNGMSECYYF HENCFLMGTI AKACLQGSDL LVQQHFRWVQ
     LRWDSEPMQG LLQRFLRRKV VNKFRGQVPS PCDPVCKTVD WALAVWRQLN SCLARLGTPE
     ALLGPKYFLS CPVIPGHAQA TVKWMSKLWN AVIAPRVQEA ILSRASVKRQ PGLGQTTKNP
     SQGQQAVVRA ALSILLNKAV LHGCPLQRAE LDQHTADFKG GSFPLSIVSS YSSCSKKRES
     GAWRKVSTSP RKKSGRFSSP TWNKPDLSEE GIKSNTILQL NCNRNASLSN QKSLENDLSL
     TLNLDQRLSL GSDDEADLVK ELQSMCSSKS ESDISKIADS RDDLRRFDSS GNNPVFSATV
     NNPRMPVSQK EVSPLSSHQM TERSNSKSKT ESGVSRVKSF LPVPRSKVTQ CSQNTKRSSS
     SSNTRQIEIN NNSRDLEPTQ K