ABR_XENLA
ID ABR_XENLA Reviewed; 862 AA.
AC Q8AVG0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Active breakpoint cluster region-related protein;
GN Name=abr;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein with a unique structure having two opposing
CC regulatory activities toward small GTP-binding proteins. The C-terminus
CC is a GTPase-activating protein domain which stimulates GTP hydrolysis
CC by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP
CC hydrolysis of RAC1 or CDC42, leading to down-regulation of the active
CC GTP-bound form. The central Dbl homology (DH) domain functions as
CC guanine nucleotide exchange factor (GEF) that modulates the GTPases
CC CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1
CC from the GDP-bound to the GTP-bound form.
CC {ECO:0000250|UniProtKB:Q12979}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q5SSL4}. Synapse
CC {ECO:0000250|UniProtKB:A0A0G2JTR4}.
CC -!- DOMAIN: The central Dbl homology (DH) domain functions as guanine
CC nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA
CC and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-
CC bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which
CC stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a
CC unique structure having two opposing regulatory activities toward small
CC GTP-binding proteins. {ECO:0000250|UniProtKB:Q12979}.
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DR EMBL; BC042307; AAH42307.1; -; mRNA.
DR RefSeq; NP_001080209.1; NM_001086740.1.
DR AlphaFoldDB; Q8AVG0; -.
DR SMR; Q8AVG0; -.
DR DNASU; 379901; -.
DR GeneID; 379901; -.
DR KEGG; xla:379901; -.
DR CTD; 379901; -.
DR Xenbase; XB-GENE-5797121; abr.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 379901; Expressed in brain and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13366; PH_ABR; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR037865; ABR_PH.
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; PTHR23182; 1.
DR Pfam; PF00168; C2; 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; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 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 2: Evidence at transcript level;
KW Cell projection; GTPase activation; Guanine-nucleotide releasing factor;
KW Reference proteome; Synapse.
FT CHAIN 1..862
FT /note="Active breakpoint cluster region-related protein"
FT /id="PRO_0000355540"
FT DOMAIN 93..286
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 303..462
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 488..616
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 650..848
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 29..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 98616 MW; EC2AC4DB8F1E49FA CRC64;
MEPVSHQDMP RLSWIDTLYS NFNYGTDGYD AEGNEEHKNS REGSETMPYI DESPTMSPQL
SARSQDSVDG VSPTPTEVLL PGGESESDKG LLMRKLVLSG VLASEEIYIN QLEALLLPMK
PLKATASTSQ PVLTLQQIND IFYKIEDIYQ MHKDFYDKLC PIVQQWDNKT TVGHLFQKLA
TQLGVYKAFV DNYKFALETA EKCSQCNVQF FKISEDLKVK GPKDSKEQPQ SVTMEALLYK
PIDRVTRSTL VLHDLLKHTP TDHPDYPLLQ DALRISQNFL SSINEDIDPR RTAVTTPKGE
PRQLVKDGFL VELSENSRKL RHLFLFTDLL LCAKLKKTTV GKHQQYDCKW YIPLADLVFP
SLEESEPIHQ LHATPDYEIE EMKAKISVLK SEIQKEKKSN KGSSRAIERL KKKMFEYESW
LLLYSPTIPF RIHNKNGKSY LFLLSSDYER SEWREAIQKL QKKDLQALAL SPFELQVLTA
SCFKLRTVHN VPIISHKDDD ESPGLYGFLH VIVKSAKGFS HSSNFYCTLE VDSFGYFVSK
AKTRVFRDTS EPEWNEEFEI ELEGSQCLRI LCYETCYDKS KLNKDNNEIV DKIMGKGQIQ
LDPQGVQSKN WHDDVIEMNG IKVEFSMKFS SRDMSLKRTP SKKQTGVFGV KISVVTKRER
SKVPYIVRQC IEEVEKRGIE EVGIYRISGV ATDIQALKAA FDANSKDILM MLSDMDINAI
AGTLKLYFRE LPEPLLTDRL YLAFMEGIAL SDPAAKENCM MHLLRSLPDP NLITFLFLLH
HLKKVAENEP INKMSLHNLA TVFGPTLLRP SEVEIKGHMN LASDIWSHDV MAQVQVLLYY
LQHPPISFSE LKRSTLYYST DV
