CTTB2_RAT
ID CTTB2_RAT Reviewed; 1649 AA.
AC Q2IBD4; O88864;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=Cttnbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9813110; DOI=10.1046/j.1365-2443.1998.00216.x;
RA Ohoka Y., Takai Y.;
RT "Isolation and characterization of cortactin isoforms and a novel
RT cortactin-binding protein, CBP90.";
RL Genes Cells 3:603-612(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=12917688; DOI=10.1038/nature01858;
RA Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA Haussler D., Green P., Miller W., Green E.D.;
RT "Comparative analyses of multi-species sequences from targeted genomic
RT regions.";
RL Nature 424:788-793(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH CTTN, AND SUBCELLULAR LOCATION.
RX PubMed=22262902; DOI=10.1523/jneurosci.4405-11.2012;
RA Chen Y.K., Hsueh Y.P.;
RT "Cortactin-binding protein 2 modulates the mobility of cortactin and
RT regulates dendritic spine formation and maintenance.";
RL J. Neurosci. 32:1043-1055(2012).
RN [6]
RP INTERACTION WITH STRN; STRN4 AND MOB4.
RX PubMed=23015759; DOI=10.1091/mbc.e12-05-0365;
RA Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.;
RT "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic
RT distribution of the striatin-PP2A complex.";
RL Mol. Biol. Cell 23:4383-4392(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, and thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000269|PubMed:22262902}.
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:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000269|PubMed:22262902}. Note=Remains
CC associated with dendritic spines even after glutamate stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CTTNBP2-L;
CC IsoId=Q2IBD4-1; Sequence=Displayed;
CC Name=2; Synonyms=CTTNBP2-S;
CC IsoId=Q2IBD4-2; Sequence=VSP_046479, VSP_046480;
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DR EMBL; AF053768; AAC35911.1; -; mRNA.
DR EMBL; DP000027; AAR16316.1; -; Genomic_DNA.
DR EMBL; AC087251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473959; EDM15128.1; -; Genomic_DNA.
DR RefSeq; NP_001107873.1; NM_001114401.1. [Q2IBD4-1]
DR AlphaFoldDB; Q2IBD4; -.
DR SMR; Q2IBD4; -.
DR BioGRID; 251850; 1.
DR IntAct; Q2IBD4; 1.
DR MINT; Q2IBD4; -.
DR STRING; 10116.ENSRNOP00000011135; -.
DR CarbonylDB; Q2IBD4; -.
DR iPTMnet; Q2IBD4; -.
DR PhosphoSitePlus; Q2IBD4; -.
DR jPOST; Q2IBD4; -.
DR PaxDb; Q2IBD4; -.
DR PRIDE; Q2IBD4; -.
DR Ensembl; ENSRNOT00000087167; ENSRNOP00000072761; ENSRNOG00000061845. [Q2IBD4-1]
DR GeneID; 282587; -.
DR KEGG; rno:282587; -.
DR UCSC; RGD:628691; rat. [Q2IBD4-1]
DR CTD; 83992; -.
DR RGD; 628691; Cttnbp2.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR GeneTree; ENSGT00940000158293; -.
DR HOGENOM; CLU_004926_0_0_1; -.
DR InParanoid; Q2IBD4; -.
DR OMA; MCPVEAL; -.
DR OrthoDB; 264951at2759; -.
DR PhylomeDB; Q2IBD4; -.
DR TreeFam; TF325130; -.
DR PRO; PR:Q2IBD4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000061845; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q2IBD4; RN.
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 GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
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 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Coiled coil; Cytoplasm;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1649
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000422173"
FT REPEAT 699..729
FT /note="ANK 1"
FT REPEAT 733..762
FT /note="ANK 2"
FT REPEAT 766..795
FT /note="ANK 3"
FT REPEAT 799..828
FT /note="ANK 4"
FT REPEAT 832..861
FT /note="ANK 5"
FT REPEAT 901..931
FT /note="ANK 6"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..275
FT /evidence="ECO:0000255"
FT COMPBIAS 330..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..476
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 576..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1649
FT /note="Basic and acidic 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 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 626..630
FT /note="VGAWP -> AGHPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9813110"
FT /id="VSP_046479"
FT VAR_SEQ 631..1649
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9813110"
FT /id="VSP_046480"
FT CONFLICT 163
FT /note="R -> K (in Ref. 1; AAC35911)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="K -> Q (in Ref. 1; AAC35911)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> F (in Ref. 1; AAC35911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1649 AA; 178768 MW; 12C85BF86EB2634B CRC64;
MATDSASCEP DLSRAPGDAE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK PVCTNPLSIL EAVMAHCRKM
QERMSAQLAA AESRQKKLEM EKLQLQALEQ EHKKLAAHLE EERGKNKHVV LMLVKECKQL
SGKVVEEAQK LEEVMVKLEE EKKKTSELED QLSAEKQRSA GMEAQLEKQL FEFDTEREQL
RAKLTREEAH TTDLKEEIDK MKKMMEQMKK GNDGKPGLSL PRKTKDKRLA SISVATEGPV
TRSVACQTDV VTESTDPVKK LPLSVPIKPS TGSPLVSTNT KGNVGPSALL IRPGIDRQAS
HSDLGPSPPT ALPSSASRIE ENGPSAGNAP DLSNSTPSTP SGTAPAAAQT LGAAPQNHSQ
APPVHSLHSP CANTHPGLNP RIQAARFRFQ GNANDPDQNG NNTQSPPSRD VSPTSRDNLV
AKQLARNTVT QALSRFTSPQ AGASSRLGAS PGGDAGTCPP VGRTGLKTPG AARVDRGNPP
PIPPKKPGLS QTPSPPHPQL RASNAGAKVD NKIVASPPST LPQGTKVVNE ENVPKSSSPQ
LPPKPSIDLT VASAGCPVSA LATSQVGAWP AETPGLNQPA CTDSSLVIPT TVAFRSSINP
VSASSRSPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ GNVTLLSMLL
NEEGLDINYC CEDSHSALYS AAKNGHTDCV RLLLNAEARV DAADKNGFTP LCVAAAQGHF
ECIELLTAYN ANINHSAAGG QTPLYLACKT GNKECIKLLL EAGTDRSIKT RDGWTPIHAA
VDTGNVDSLK LLMYHRVPAP GNSLSAEEPK SGLFSLNGGE SPPGSSKPVV PADLINHADK
EGWTAAHIAA SKGFKNCLEI LCRHGGLEPE RRDKCNRTVH DVATDDCKHL LENLNALKIP
LRISVGEIQP SNDGSDDFEC EHTICTLNIR KQTSWEDFSK AVSQALTNHF QAISSDGCWG
LEDGTLNNTT DSCIGLGTSS IQSIMLGSIP WSTGQSFSQS PWDFMKKKKV EQVTVLLSGP
QEGCLSSVTY TSMIPLQMLQ NYLRLVEQYH NVIFHGPEGS LQDYIANQLA LCMKHRQMAA
GFPCEIVRAE VDSGFSKEQL VDVFISNACL IPVKQFPVKK KIIVILENLE KSSLSELLGD
FLAPLENRST ESPCTFQKGN GTSECYYFHE NCFLLGTLAK ACLQGSDLLV QQHFRWVQLR
WDCEPSQGLL QRFLRRKAVS KFRGQLPAPC DPVCKIVDWV ISVWRQLNSC LARLGTPEAL
LGPKYFLSCP VVPGHAQATV KWMSKLWNAI IAPRVQEAIL SRAAMNKQPG ARQTASKKHP
SQGQQAVVRA ALSILLNKAI LHGCPLPRTE LDQQIADFKG GSFPLSIVSS YSKKKGESAA
WRKVNTSPRK KPGHFSSPMW NKPDLKHEGM RNKSVPHLNI NRSSSLSKQQ SLENDLSMTL
TLDHRLSLGS DDEADLVKEL QSMCSSKSES DISKIADSRE DLRTFDSSRT NPVTSAPVNL
RMPVPQKEAS PLSSHQTTEC SNSKSKTELG VSRVKSFLPV PRSKVAQCSQ NTKRSSSSSS
NTRQLEINNN SKEENWNVDK HEHVEKRNK
