ID F1Q9E9_DANRE Unreviewed; 1341 AA.
AC F1Q9E9; A0A8M1RL18;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=BCR activator of RhoGEF and GTPase {ECO:0000313|Ensembl:ENSDARP00000092056};
DE SubName: Full=Breakpoint cluster region protein {ECO:0000313|RefSeq:XP_002665983.2};
GN Name=bcr {ECO:0000313|Ensembl:ENSDARP00000092056,
GN ECO:0000313|RefSeq:XP_002665983.2,
GN ECO:0000313|ZFIN:ZDB-GENE-040724-43};
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 {ECO:0000313|Ensembl:ENSDARP00000092056};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000092056}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000092056};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000092056, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000092056};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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 [3] {ECO:0000313|RefSeq:XP_002665983.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002665983.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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DR EMBL; AL844518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002665983.2; XM_002665937.5.
DR STRING; 7955.ENSDARP00000092056; -.
DR PaxDb; 7955-ENSDARP00000092056; -.
DR Ensembl; ENSDART00000101282; ENSDARP00000092056; ENSDARG00000079286.
DR Ensembl; ENSDART00000101282.5; ENSDARP00000092056.4; ENSDARG00000079286.4.
DR GeneID; 568320; -.
DR KEGG; dre:568320; -.
DR AGR; ZFIN:ZDB-GENE-040724-43; -.
DR CTD; 613; -.
DR ZFIN; ZDB-GENE-040724-43; bcr.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_004164_0_0_1; -.
DR OrthoDB; 2916231at2759; -.
DR PhylomeDB; F1Q9E9; -.
DR TreeFam; TF105082; -.
DR Proteomes; UP000000437; Chromosome 21.
DR Bgee; ENSDARG00000079286; Expressed in retina and 16 other cell types or tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd08686; C2_ABR; 1.
DR CDD; cd04387; RhoGAP_Bcr; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 4.10.280.30; Bcr-Abl oncoprotein oligomerisation domain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
DR InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182:SF3; BREAKPOINT CLUSTER REGION PROTEIN; 1.
DR PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR Pfam; PF09036; Bcr-Abl_Oligo; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF19057; PH_19; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF69036; Bcr-Abl oncoprotein oligomerization domain; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1Q9E9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 569..762
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 779..936
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 963..1089
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1124..1318
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 70..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 151092 MW; 99D85D2FBD7F7245 CRC64;
MVEPVGFIEA WKAQFPESEP PKMELRSVGG IEQELEKCKA SIRRLEMEVN KERFRMIYLQ
TLLAKERKSY DRQRWGFRKP PHMTEGDPQA VGADSQHLHA QEHGQPERSR FQPVGETRAK
PRPPPARKSA SHGDGLELQS SFEAHQPGPV SEADGLSPST QRGGVSPRRP HPPPDKELPS
DPSQKDKASM GLGVAALRSN FERIKRANSH SASDGKSGQE KPFYTNVEFH HDRGLVKVND
REVSDKISSL GNQAMQMERK RSLHSLPGNL ATVAGDLRAR PVYRGRSTES TCGYDAEYED
GEPSPRYSAA RPNGAKPPPP PWQPSDFQPY TSVYVGGMMP GEGGDGRVPM REHGGSDDHL
LTWPRRSYSP GSYEDVGGGG GGYTPDCSSN ENLTSSEEDF SSGQSSHVSP SPTTAYRRPI
REKSRSPSQN SQNSQHSFDS SSPPTPQTQK RHRQQHVVVS EATIVGVRKT GQIWPHDGES
VASSRASHDN SYHGDLDGPF TGTPPTYGYD ADRAEEQRRH HDILPYIDDS PSSSPHLSSK
SRSSRDTLSS GSIESSKSAE LDLEKGLEMR KRVLSGILAS EETYLSHLEA LLLPMKPLKA
AATTSQPVLT VQQIETIFFK VPELYEIHKE FYDSLLPRVQ QWSHHQRVGD LFQKQASQLG
LYRAFVDNYE LAVETAEKCC QANTQFAEIS ESLKVRSTKE CKDLTAKYSL ETLLYKPVDR
VTRSTLVLHD LLKHTPSSHP DYPLLQDALR ISQNFLSSIN EESTPRRQSM TVKKGENRQL
LKDGFMVELV EGARKLRHVF LFTDLLLCAK LKKLIGGKSQ QYDSKWYIPL SDLTFQTAEE
SEPLPIPQAP DEELDAIKIK ISSLRSEIQR ERRANKGSKV MERLKKKLSE QESLFLLNSP
NMPLRVHNRN GKSYMFLISS DYERAEWKEV IREQQKKCFK TFNLSSMELQ MLTNSCVKLQ
TVHQLPLTVN KEEDESTGLY GFLNVIVHSA SGLKQSLNLY CTLEVDSFGI FVNKAKTRVY
RYTTEPKWNE EFEIELEGSH TLRLLCYEKS YNKAKVNKED GESTDRIMGK GQMPLDPQML
QGKDWQRTVI PMNGIEVKIS MKFTSREFSL KRMPSRKPMG VFGVNISTVT KRERSKVPYI
VRQCLEEIER RGMEEVGIYR VSGVATDIQA LKTAFDTNNK DVSVMMSEMD VNAIAGTLKL
YFRELPEPLF TDELYPNFAG GIALSDSVAK ESCMLNLLLS LPEPNLVTFL FLLDHLKRIA
EKECVNKMSL HNLATVFGPT LLRPAEKDSK IPTNPTQPIT MGDSWSLEVM SQVQVLLYFL
QLETIPTPDS KRQSILFSTE V
//
