ID A0A3Q2C6W7_CYPVA Unreviewed; 1029 AA.
AC A0A3Q2C6W7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Breakpoint cluster region protein-like {ECO:0000313|Ensembl:ENSCVAP00000000381.1};
GN Name=BCR {ECO:0000313|Ensembl:ENSCVAP00000000381.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000000381.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000000381.1}
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 AlphaFoldDB; A0A3Q2C6W7; -.
DR STRING; 28743.ENSCVAP00000000381; -.
DR Ensembl; ENSCVAT00000015185.1; ENSCVAP00000000381.1; ENSCVAG00000001272.1.
DR GeneTree; ENSGT00940000153491; -.
DR OMA; IKVKISH; -.
DR Proteomes; UP000265020; Unplaced.
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:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08686; C2_ABR; 1.
DR CDD; cd04387; RhoGAP_Bcr; 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; 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; 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; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
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:UP000265020}.
FT DOMAIN 347..450
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 467..624
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 649..778
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 812..1006
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 115518 MW; 135CA426D520E48F CRC64;
MQMERKRSLH SLPGNLATVA GELRARPVYR GRSTESTCGY DAEYEDGEPN QRHSGRANGG
KPPPPPWQPP EFQAYSSVYV GGVMMGEGGS GGGSGVTMKD HSGGDDHLLT WPRRSYSPGS
FEDAGGGGGY TPDCSSNENL TSSEEDFSSG QSSHVSPSPT TGFRRPFREK SRSPSQNSQN
SQHSYDSSSP PTPQSQKRHH RQQGGHVVMS EATIVSVRKT GQIWPPPSSG NSSGSDGHFT
GTPPSYGYDA DRAEEQRRHH DILPYIDDSP SSSPHLSSKS RSSRDTLSSG SLESSKSTEC
DLEKGLEMRK WVLSGILATE EAYLSHLEAL LLVRKAASTI SASQLGVYRA FLDNYELAVE
TAEKCCQANS QFAEISEVRK RGIPLSPSDQ IRWEICTWLT LLYKPVDRVT RSTLVLHDLL
KHTPTSHPDH PLLQDALRIS QNFLSSINEE TTSRRQSVAW KKGENRQLLK DSFMVELVEG
TRKLRHVFLF TDLLLCAKLK KQIGGKNQQY DCKWYIPLTE LTFQGPEETE PLTIPQVPDE
ELDAVKVKIS HLRSEIQREK RANKGSKVID RLRKKLSEQE SLMLLTSPSM PLRLFNKNGK
SYSFLISSDY ERSEWREIIR EQQQKCVKTP SLTSMELQML TSSCLKLQTV HNIPLSLNRE
EDDSSGLYGF LNVIVHSASG LKQSLNLYCT LEVDTFGFFL NKAKTRVYRY TTEPKWNEEF
EIELEGSQTL RLLCYEKSYN RTKLNKEDGD STDRIIGKGQ ILLDPQTLQG KDWQRTVIPM
NGIEVKLSIK FTSREFSLKR MPSEKPMGVF GVKISTVTKR ERSKVPYIVR QCLEEIERRG
MEEVGIYRVS GVATDIQALK TAFDTNNKDV SVMMSEMDVN AIAGTLKLYF RELPEPLFTD
ELYPNFAGGI TLTDSVAKES CMLNLLLSLP EPNLVTFLFL LDHLKRVAEK ESVNKMSLHN
LATVFGPTLL RPAEKDSKIP SNPTQPISMG DSWSLEVMAQ VQVLLYFLQL ETIPTPDSKR
QSILFSTEV
//
