ID W5MJS8_LEPOC Unreviewed; 1330 AA.
AC W5MJS8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=BCR activator of RhoGEF and GTPase {ECO:0000313|Ensembl:ENSLOCP00000008637.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008637.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008637.1}
RP IDENTIFICATION.
RG Ensembl;
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; AHAT01005187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000008647.1; ENSLOCP00000008637.1; ENSLOCG00000007102.1.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004164_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG20.
DR Bgee; ENSLOCG00000007102; Expressed in camera-type eye and 11 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: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:0035556; P:intracellular signal transduction; IEA:InterPro.
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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 558..751
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 768..925
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 952..1079
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1113..1307
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 67..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 149805 MW; 219FCD147341531C CRC64;
MVEPVGFVEA WKAQFPESEP PKMELKSVGD IEQELEKCKA SIRRLEMEVN KERFRMIYLQ
TLLAKEKKSY DRQRWGFRRV SHMNEAGGSD QPSSPDPPQP HPHESGEGDR SRPPPVRKAS
SQGEGPEPPP AVEVLYPGEA GEADRFKRHP EDSEVDSASP SKQRGVAPGR RATAGPPPPE
REDSSPREKV GMSVAALRSN FERIKRANSH SSGEGKGGGA EKPFYVNMEY HHERGLVRVN
DREVSDKIST LGSQAMQMER KRSLHSLPGS LAAGAGEYRR PVYRGRSTEA SCGYDAEYED
AELNPRFLKD NLVRANGGRA ERPAADFQPY TSVYVGGMMG DGDGKGVSAR DHGEQDKHLT
WPRRSYSPGS FEDGGGGYTP DCSSNENLTS SEEDFSSGQS SHVSPSPTTY RMFREKSRSP
SQNSQQSFDS SSPPTPQSQK RHKQQVVVSE ATIVGVRKTG QIWPHDGDST PSSRASHDNS
FHGDLDASFS GTPPTYGYDA DRAEEQRRHH DMMPYIDDSP SSSPHLSSKS RGSRDTLSSG
SLESSKSGEL DLEKGLEMRK WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTM
PQIETIFFKV PELYEIHREF YDGLLPRVQQ WSHHQCVGDL FQKLASQLGL YRAFVDNYEI
AVETAEKCCQ ANSQFAEISE NLKVRSTKDS KDQTSKNSLE TLLYKPVDRV TRSTLVLHDL
LKHTPSGHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT VKKGENRQLL KDRFMVELVE
GARKLRHVFL FTDLLLCAKL KKQIGGKSQQ YDCKWYIPLA DLTFQTIDES DSSPIPQLPD
EEIDAMKIKI SQIKNEIQRE KRANKGIKVI ERLKKKLSEQ ESLLLLMSPN MAFRVHNRNG
KSYMFLISSD YERAEWREII REQQKKCFKS FSLTSVELQM LTNSCVKLQT VHNVPLTINK
EDDESPGLYG FLNVIVHSAS GLKQSLNLYC TLEVDSFGYF VNKAKTRVYR DTTEPNWNEE
FEIELEGSQT LRLLCYEKCY NKTKLNKEDG ENTDRIMGKG QIQLDPQSLQ GKDWQRTVIS
MNGIEVKLSM KFTSREFSLK RMPSRKQTGV FGVKIAVVTK RERSKVPYIV RQCVEEIERR
GMEEVGIYRV SGVATDIQAL KAAFDANNKD VSVMMSEMDV NAIAGTLKLY FRELPEPLFT
DELYPNFAGG IALSDSVAKE SCMLNLLLSL PEPNLVTFLF LLDHLKRVAE KEGINKMSLH
NLATVFGPTL LRPSEKDSKI PANPTQPITM SDSWSLEVMS QVQVLLYFLQ LETIPTPDSK
RQSILFSTEV
//
