ID H2RQR9_TAKRU Unreviewed; 856 AA.
AC H2RQR9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=ABR activator of RhoGEF and GTPase {ECO:0000313|Ensembl:ENSTRUP00000002484.3};
GN Name=ABR {ECO:0000313|Ensembl:ENSTRUP00000002484.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000002484.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000002484.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000002484.3}
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; H2RQR9; -.
DR Ensembl; ENSTRUT00000002496.3; ENSTRUP00000002484.3; ENSTRUG00000001060.3.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004000_1_0_1; -.
DR Proteomes; UP000005226; Chromosome 15.
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 CDD; cd00160; RhoGEF; 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:SF5; ACTIVE BREAKPOINT CLUSTER REGION-RELATED 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:UP000005226}.
FT DOMAIN 85..279
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 296..454
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 479..608
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 642..842
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 97353 MW; E7619D40CBBFB880 CRC64;
MDLDCQDSLA DRDFNYNTDG YEGEGAEDGK SQDGSETLPY IDESPTMSPQ LCAPQGPDGE
AVSPTPPEGL PPGVRAGDIE KGLEMKKLVL SGFLASEEIY INQLEALLLP MRPLKATATT
SQPVLTIQQV DTIFYKIQDI FEIHKEFYDA LLPSIQQWDE NVTVGHLFQK LASQLGVYKA
FVDNYKEALE TAEKCSHANS QFQKISEVSP NTHLPDNSDS WSPSFLPTAL LYKPIDRVTR
STLVLHDLLK HTPKDHPDFP LLQNALRISQ NFLSSINEEI DPRRTAVTTP KGEARQLVKD
GFLVEVSESS RKVRHVFLFT DLLLCAKMKK TAVGRHQQYE CKWYIPLADL TFQTLDDSDS
CHSVQVLPEH EIEEMKIKIS ALKNEIQKEK KGPKGQSRVE RLRKKMNEQE SWLLLHSPTI
PFCIHNKHGK SYLFLLSSDY ERSEWRESIQ KLQKKDLQSC VLSSVELQVL TSSCFKLRTV
HNIPVTSNKD DEETPGLYGF LHVIVHSAQG FRDSANLYCT LEVDSFGYFV SKAKTRVFRD
TTEPQWNEEF EIELEGSQYL RILCYEKCYD KSMLNKDDNE IVDKIMGKGQ VQLDPQTVQS
KNWHMDIIEM NGIKVEFSMK FTSRDLSLKR TPSKKQSGVF GVKINVVTKR ERSKVPYIVR
QCIEEVEKRG IDEVGIYRIS GVATDIQALK TAFDTNTKDI LVMLSDMDIN AIAGTLKLYF
RELPEPLLTD RLYPAFMEGI ALSDPAAKEN CMMHLLRSLP EPNLMTFLTL LEHLKRVAEK
EPINKMSLHN LGTVFGPTLL RPSESESTKG QHITSASDIW SHDVMAQVQV LLYYLQHSPI
SFAELKRNTL YFSTDV
//
