COBL_DANRE
ID COBL_DANRE Reviewed; 1343 AA.
AC E7F568; I1X3U9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Protein cordon-bleu;
GN Name=cobl;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-1327, FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH PACSIN1, AND DEVELOPMENTAL STAGE.
RX PubMed=23203810; DOI=10.1242/jcs.111674;
RA Schuler S., Hauptmann J., Perner B., Kessels M.M., Englert C., Qualmann B.;
RT "Ciliated sensory hair cell formation and function require the F-BAR
RT protein syndapin I and the WH2 domain-based actin nucleator Cobl.";
RL J. Cell Sci. 126:196-208(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=21129373; DOI=10.1016/j.ydbio.2010.11.023;
RA Ravanelli A.M., Klingensmith J.;
RT "The actin nucleator Cordon-bleu is required for development of motile
RT cilia in zebrafish.";
RL Dev. Biol. 350:101-111(2011).
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 neuron morphogenesis and increases branching of
CC axons and dendrites (By similarity). Required for normal embryonic
CC development, including normal development of laterality, normal body
CC size and shape, as well as normal brain, heart and kidney development.
CC Required for normal development of stereocilia and kinocilia in sensory
CC hair cells of neuromasts in the posterior lateral line organ, and thus
CC also for balance keeping and normal swimming behavior. {ECO:0000250,
CC ECO:0000269|PubMed:21129373, ECO:0000269|PubMed:23203810}.
CC -!- SUBUNIT: Interacts with pacsin1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle
CC {ECO:0000250}. Cytoplasm. Cytoplasm, cytosol. Note=Detected throughout
CC the neuron cell body, as well as in axons and dendrites (By
CC similarity). Colocalizes with the actin cytoskeleton. Recruited to the
CC cell membrane via interaction with pacsin1. Detected at the apical
CC surface of cells at the basis of forming cilia, but not in the cilia
CC themselves. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Detected in early zygote. Detected in neural keel
CC and in Kupffer's vesicle at the eight somite stage. Detected in
CC developing pronephric tubules, the otic vesicle and nasal placodes at
CC 24 hpf. At 24 to 72 hpf, detected in ciliated epithelium cells of the
CC neural tube, nasal pits and pronephric tubules. Detected in embryonic
CC neuronal tissues, including forebrain, hindbrain, spinal cord and
CC retina. {ECO:0000269|PubMed:21129373, ECO:0000269|PubMed:23203810}.
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DR EMBL; BX537113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JQ776648; AFI74363.1; -; mRNA.
DR AlphaFoldDB; E7F568; -.
DR SMR; E7F568; -.
DR STRING; 7955.ENSDARP00000018030; -.
DR PaxDb; E7F568; -.
DR ZFIN; ZDB-GENE-091020-11; cobl.
DR eggNOG; ENOG502QTAY; Eukaryota.
DR InParanoid; E7F568; -.
DR TreeFam; TF333490; -.
DR PRO; PR:E7F568; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IEA:InterPro.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0003146; P:heart jogging; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR InterPro; IPR039895; COBL-like.
DR InterPro; IPR019025; Cordon-bleu_ubiquitin_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR21557; PTHR21557; 1.
DR Pfam; PF09469; Cobl; 1.
DR Pfam; PF02205; WH2; 2.
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; Reference proteome; Repeat.
FT CHAIN 1..1343
FT /note="Protein cordon-bleu"
FT /id="PRO_0000422093"
FT DOMAIN 1167..1187
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1207..1227
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1297..1317
FT /note="WH2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..310
FT /note="KKRRAP 1"
FT MOTIF 338..343
FT /note="KKRRAP 2"
FT COMPBIAS 16..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 50
FT /note="C -> S (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Y -> N (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..239
FT /note="Missing (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="T -> I (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="S -> A (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="Missing (in Ref. 2; AFI74363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1343 AA; 145731 MW; F553F55B31BC92CE CRC64;
MNLGDATTRP PVGRRMKAQA PPPPRPPQPA PRRIFRNAVP DGGGSSGGDC KENMLRSYVD
LHISLPTGYQ TTINVDGRKA LMDLLVDLCS QYHLNPAYHT LELLSPDAQP VSFKPNALLG
ALDVSCALIK ERVLEDRVIR KPPPKVPEKT VRLVVNYHRS QKAVVRVNPL APLQTLVPVI
CQKCEFDPAH VLLFKDNINH QQLDLDKSLS DLGIRELYVL DQTLVLQPKM ASTPALNYSA
ESLRSNSLSG SEKKGLLGFL KFNRRKSKGM SVVASGPCVE ARPSTLGQSQ SVMNISKMSP
KVELKKRRAP APPPAPTQTL PPTSQISLGS PSSHNLLKKR KAPAPPPTPP PSTPEPDIST
YVPTATVQEH YIPASVERTP RASTPADDSD LSHSIEDSEP ARSICSSSSG DDAAAVGSSS
SSLAEEPVTH RADVIAPFTT STPEPEPKPE YEPELKKEAS PRSTPELEPG PRPEVPAAED
LEVEMELKME ETENNRHSGI AWLHSAHESV LERRVQQEVE TVSVASSESF ADHGYAASED
MAEESGPVSP SERMQSVSPM DIMSLNSDST LPVKQSKESS SDSDEGCATW GSRQSSGHIQ
DGQKSIKRQN GYEEDPEITA QIHLTLADLD ANLADLNHSD GASVFVDDEI PVSIVDMDIP
VTAIDEVLDD DQCSASECES VLLRSTQSIS SKPCTPCGVI QNKNNNACLT EEKHRSPFPD
IEKQLQTATL TVIDKPTIQS PTSKKPSQDA KITDNMEQKT TFNSEAKSKS ETVELTSQKD
TVLQKSQSFV RPDVQSVQKE RTSSTRVLPT QGKITLSSFS RFGMKTFTVI PPKPAVSQTK
PAGSLVTGAI KIDEQGNMVT QRQISSGPEK NNTPSVDTTR ADKTPLVKAK AFWSTTEKQE
KLTTAKTEPI VNNGDTDVFK ASAVTGSFKL SPPEETHKEV IIVERKPISG VASKPSFSEN
HAEKRDLSFL IPSRRTSSQY VASVIAKNNK NSSIPKTKID TTPAPLSISG VQNPVNQLLN
NEVKPTSIHK PAVTVKPTEN PVPSFRPKCL QSYVAEKPTS SERISTLHGG DKTKSLDSQP
LSIKIQPFPH VSAHIKSFSE EATSINNFPD TSSARQTPTD TTHPPLAKKP ELHKSEIPSE
PNQGNVFGPV KKFKPVIFKP VQQETSIHSS LMEAIQSGEG IERLRKVSDL PTSCTVKKPS
YNDPENERSA LLSAIRASST SAKLKKTKSV ASKELEQLRK VEEDRNVHTE VISPRPTSPD
FVPPLPPSFS PPPPPPPPLA PAKPPVVLPP GGNPEAAREA LLEAIRSGSG AQQLRKVPVT
QTRRQVNGRL GTIQATSPLS YGH
