COBL_RAT
ID COBL_RAT Reviewed; 1133 AA.
AC D3ZUI5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein cordon-bleu;
GN Name=Cobl;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH PACSIN1
RP AND WASL, AND INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3.
RX PubMed=21725280; DOI=10.1038/emboj.2011.207;
RA Schwintzer L., Koch N., Ahuja R., Grimm J., Kessels M.M., Qualmann B.;
RT "The functions of the actin nucleator Cobl in cellular morphogenesis
RT critically depend on syndapin I.";
RL EMBO J. 30:3147-3159(2011).
RN [4]
RP FUNCTION, INTERACTION WITH DBNL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23223303; DOI=10.1523/jneurosci.0843-12.2012;
RA Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B.,
RA Kessels M.M.;
RT "The actin nucleator Cobl is crucial for Purkinje cell development and
RT works in close conjunction with the F-actin binding protein Abp1.";
RL J. Neurosci. 32:17842-17856(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-196; SER-219;
RP SER-256; SER-330; SER-333 AND SER-356, AND IDENTIFICATION BY MASS
RP 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: Plays an important role in the reorganization of the actin
CC cytoskeleton. Binds to and sequesters actin monomers (G actin).
CC Nucleates actin polymerization by assembling three actin monomers in
CC cross-filament orientation and thereby promotes growth of actin
CC filaments at the barbed end. Can also mediate actin depolymerization at
CC barbed ends and severing of actin filaments. Promotes formation of cell
CC ruffles. Regulates dendrite branching in Purkinje cells (By
CC similarity). Regulates neuron morphogenesis and increases branching of
CC axons and dendrites. {ECO:0000250, ECO:0000269|PubMed:21725280,
CC ECO:0000269|PubMed:23223303}.
CC -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X (By similarity). Identified in a complex composed of COBL,
CC PACSIN1 and WASL. Interacts with PACSIN1, PACSIN2 and PACSIN3.
CC Interacts (via WH2 domains) with actin monomers. Interacts with both
CC PACSIN1 and DBNL. {ECO:0000250, ECO:0000269|PubMed:21725280,
CC ECO:0000269|PubMed:23223303}.
CC -!- INTERACTION:
CC D3ZUI5; P62161: Calm3; NbExp=2; IntAct=EBI-7003590, EBI-397530;
CC D3ZUI5; Q9Z0W5: Pacsin1; NbExp=6; IntAct=EBI-7003590, EBI-1550185;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle.
CC Cytoplasm. Cytoplasm, cytosol. Note=Recruited to the cell membrane via
CC interaction with PACSIN1. Colocalizes with the actin cytoskeleton.
CC Detected throughout the neuron cell body, as well as in axons and
CC dendrites.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:23223303}.
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DR EMBL; CH474055; EDL76073.1; -; Genomic_DNA.
DR RefSeq; NP_001100706.1; NM_001107236.1.
DR AlphaFoldDB; D3ZUI5; -.
DR SMR; D3ZUI5; -.
DR DIP; DIP-61709N; -.
DR IntAct; D3ZUI5; 3.
DR MINT; D3ZUI5; -.
DR STRING; 10116.ENSRNOP00000063258; -.
DR iPTMnet; D3ZUI5; -.
DR PaxDb; D3ZUI5; -.
DR PeptideAtlas; D3ZUI5; -.
DR PRIDE; D3ZUI5; -.
DR Ensembl; ENSRNOT00000064483; ENSRNOP00000063258; ENSRNOG00000004281.
DR GeneID; 305497; -.
DR KEGG; rno:305497; -.
DR CTD; 23242; -.
DR RGD; 1312002; Cobl.
DR eggNOG; ENOG502QTAY; Eukaryota.
DR GeneTree; ENSGT00530000063608; -.
DR InParanoid; D3ZUI5; -.
DR PhylomeDB; D3ZUI5; -.
DR PRO; PR:D3ZUI5; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000004281; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; D3ZUI5; baseline and differential.
DR Genevisible; D3ZUI5; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0044294; C:dendritic growth cone; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:1990357; C:terminal web; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0051639; P:actin filament network formation; ISO:RGD.
DR GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
DR GO; GO:0033504; P:floor plate development; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0030903; P:notochord development; ISO:RGD.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:RGD.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0001757; P:somite specification; ISO:RGD.
DR InterPro; IPR039895; COBL-like.
DR InterPro; IPR019025; Cordon-bleu_ubiquitin_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR47008; PTHR47008; 2.
DR Pfam; PF09469; Cobl; 1.
DR Pfam; PF02205; WH2; 3.
DR SMART; SM00246; WH2; 3.
DR PROSITE; PS51082; WH2; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1133
FT /note="Protein cordon-bleu"
FT /id="PRO_0000422092"
FT DOMAIN 981..1001
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1021..1041
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1109..1129
FT /note="WH2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..312
FT /note="KKRRAP 1"
FT MOTIF 340..345
FT /note="KKRRAP 2"
FT COMPBIAS 267..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5NBX1"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
SQ SEQUENCE 1133 AA; 122267 MW; A1DFF048013B5403 CRC64;
MKARAPPPPG KPAAQNVHSE QKLPHDATLG SQQSLVHLKE ALHNSTLDIT VVLPSGLEKQ
SVVSGSRAVM DLLVELCLQN HLNPSHHVLE IWSSETQQPL SFKPNTLIGS LNAHTVFLKE
KVPEEKGKPG LTKAPEKSVR LVVNYLRTQK AVMRVSPEVP LQNILPVICA KCEVSPDHVV
LLRDNIAGEE LELSKSLNEL GIKELYAWDN RREMLRKSSL GNDETDKEKK KFLGFFKVNK
RSNSKAEHLG LSGADSDEDP SKSASGGDLN GCVTTPNSPS LHSRSLTLGP SLSLGNISGM
SMKSDMKKRR APPPPSPGLL GQDKVSEKAS LSSQADLQKK KRRAPAPPPP QPPPPSPVVP
NRKEDKEENR KSTVGMEENY ETDTSSLTSS VNGVSNHSLQ EAIIPDSGVD DIPVTFIGEV
SDEPFDSGLF FSGSNNAAAL NQGGIASQRS HLPPYQTEQS QPFIRTNRKE PDPSLPSQDY
RKRNQPILAN TSENENPVGI DPRVTSFVSK PSTDDPKAKD KDKMCGSGPS EKTQTGHRVN
SLPVNPRVGE DENSNSALPP WSHHGQASGG SYGLKYGLTT YKIVPPKPEM RCYDRDVSLS
TGAIKIDELG NLMSPHMNGS RTISKPSAVA ETEAPPIGKV KEFWRRNSME KYLNGPAECT
VKKAPSTTIT ATSEKPQRDE TKAGFTLTTP EQQPASQEYG APPEEDRSRP HSAVSCPVKV
PAPNPTDITF LKPQRRTSSQ YVASAIAKKM GPPKVHADVV RPHKKTAEQG HEEAKLARPP
PAWKDSAVPN LCSEAGQCEH GTNQGSVRLP SNPGGQLPAD HPKVEVNSTY GKSATHNSPA
AVHRNSYFLP GRSSQRDRVS VGQSCGFHEK QTISNQKMNS TSNPSQALDK AHPAPLLLTE
ARDSGRILVN GSAQTPGNCE PPHSQKESTL TSYIILQTEE KPSPLSADGQ NSDDALPSSI
FGPKKKFKPV VQRPLPKDIS LHSALMEAIH TSGGRDKLRK TAEQASEGRP KKPSYVEAES
ERSALLAAIR GHSGTLSLRK VSSLASEELQ SFRDAALMAP GVDKPQQEDR GLPPPPALPP
PSTPASQVPS ASIPVSRFSI GTLSNPVNAR QALMDAIRSG TGAARLRKVP LLV
