CTTB2_LOXAF
ID CTTB2_LOXAF Reviewed; 1661 AA.
AC Q108T9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785;
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 (JUL-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; DP000087; ABG66653.1; -; Genomic_DNA.
DR AlphaFoldDB; Q108T9; -.
DR SMR; Q108T9; -.
DR STRING; 9785.ENSLAFP00000004829; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR HOGENOM; CLU_004926_0_0_1; -.
DR InParanoid; Q108T9; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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..1661
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000250462"
FT REPEAT 707..737
FT /note="ANK 1"
FT REPEAT 741..770
FT /note="ANK 2"
FT REPEAT 774..803
FT /note="ANK 3"
FT REPEAT 807..836
FT /note="ANK 4"
FT REPEAT 840..869
FT /note="ANK 5"
FT REPEAT 910..940
FT /note="ANK 6"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..280
FT /evidence="ECO:0000255"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..430
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 584..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1661
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 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1661 AA; 181265 MW; 4E81BDF7E308E2D8 CRC64;
MATDGASCEP DFSRASEDAA EATAEATAEA AKKEFDVDTL SKSELRMLLS VMEGELEARD
LVIEALRARR KEVFIQERYG RFNLNDPFLA LQRDYEAGAR EKEKKPVCTN PLSILEAVMA
HCRKMQERMS TQLAAAESRQ KKLEMEKLQL QALEQEHKKL AARLEEERGK NKHVVLMLVK
ECKQLSGKVI EEAQKVEEVM AQLEEEKKRT NELEEELSTE KRRSTEMEAQ MEKQLSEFDT
EREQLRAKLN REEAHTTDLK EEIDKMKKMI EQLKRGNDSK PSLSLPRKVK DRRLVSVSVG
TEGPVTRSVA CQTDLVVEST DHVKKLPLTV PVKPSAGSPL VSASAKGNVV RPSVDRQASH
GDLILSSVPT VPPPSVNKTE ENGPSTGSTP DLPSSTPPLP NNTAPPAVQP PSIASQNYSQ
ASSLHSLHSP CANASLHPGV NPRIQAVRFR FQGNANDQDQ NGNTTQSPPS RDVSPTSRDN
LVAKQLARNT VTQALSRFTG PQVGASARPG APTTGDISTH PPVGRTSLKT SGVARVDRGN
PPPIPPKKPG LSQTPSPPHP QLKVIMDSSR ASNAGAKVDK TVASPPTSLP QGNRVINEEN
LPKSSSPQLP PKPSIDLTVA PAGCAVSALA TSQVGAWRAE TPGLNQPACS DSSLVIPTTI
AFCSSINPVS ASSCRPGASD SLLVTASGWS PSLTPLLMSG GPAPLAGRPT LLQQAAAQGN
VTLLSMLLNE EGLDINYSCE DGHSALYSAA KNGHTDCVRL LLNAEAQVNA ADKNGFTPLC
AAAAQGHDKC VELLIAYRAN INHAADGGQT PLYLACKNGN KECIKLLLEA GTDRSVKTRD
GWTPVHAAVD TGNVDSLKLL MYHRAPACGD RLNEEEPESD VFDLDGGGER PEGTVKPVVP
ADLINHADRE GWTAAHIAAS KGFKNCLEIL CQHGGLEPER NDKCNRTVHD VATDDCKHLL
ENLNALKIPL RISMSETQRD SFGSDDFECE NTIWALTIRR QTSWDDFSKG VIQALTNHFQ
AISSDGWWSL EDVTFNNTTE SSIGLGASSV LSIMLGSVSW SPGQSFAQSP WDFLKKNKAE
QVTVLLSGPQ EGCLSSVTYA SMIPLPMLQN YLRLVEQYHN VIFHGPEGSL QDYIAHQLAL
CMKHRQMAVG FSCEIVRAEV DAAFCKEQLV DLFIRNACLI PVKQSPGNKK VIVILENLEK
SSLSELLGDF LAPLENRSTE SPCTFQKGNG TSECYYFHEN CFLMGTIAKA CLQGSDLLVQ
QHFRWVQLRW DGEPMQGLLQ RFLRRKAVNK FRGKLSSPRD PVCKTVDWAL SVWRQLNSCL
ARLGTPEALL GPKYFLSCPV VPGHAQATVK WMSKLWNAVI APRVQEAILS KASVKRQPGL
GQTNAKKHPS QGQQAVVKAA LSILLNKAVL HGCPLPRAEL DQYIAEFKGG SFPLSIVSSY
SSCGKKKGEN GAWRKVSTSP RKKSGRFPSP TWSKPDLSDE GIKNKTVSQL NCNRNASLSR
QKCLENDLSL TLNLDQRLSL GSDDEADLVK ELQSMCSSKS ESDISKIADS RDDLRRFDSS
RNSPAFSATV NNPRMPVSQK EVSPLSSHQT TECSNSKLKT ELGVSRVKSF LPVPRSKVAQ
CSQNTRRSSS SSNTRQIEIN NNSKDEIWNL RKNEQVEKPN K
