ABR_XENTR
ID ABR_XENTR Reviewed; 862 AA.
AC A4II46; Q0V9W3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Active breakpoint cluster region-related protein;
GN Name=abr;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4II46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4II46-2; Sequence=VSP_035907;
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; BC121371; AAI21372.1; -; mRNA.
DR EMBL; BC135846; AAI35847.1; -; mRNA.
DR RefSeq; NP_001072313.1; NM_001078845.1. [A4II46-2]
DR RefSeq; XP_012812700.1; XM_012957246.2. [A4II46-1]
DR AlphaFoldDB; A4II46; -.
DR SMR; A4II46; -.
DR STRING; 8364.ENSXETP00000051209; -.
DR PRIDE; A4II46; -.
DR DNASU; 779766; -.
DR GeneID; 779766; -.
DR KEGG; xtr:779766; -.
DR CTD; 29; -.
DR Xenbase; XB-GENE-5797083; abr.
DR InParanoid; A4II46; -.
DR OrthoDB; 762492at2759; -.
DR Reactome; R-XTR-193648; NRAGE signals death through JNK.
DR Reactome; R-XTR-416482; G alpha (12/13) signalling events.
DR Reactome; R-XTR-9013026; RHOB GTPase cycle.
DR Reactome; R-XTR-9013106; RHOC GTPase cycle.
DR Reactome; R-XTR-9013148; CDC42 GTPase cycle.
DR Reactome; R-XTR-9013149; RAC1 GTPase cycle.
DR Reactome; R-XTR-9013404; RAC2 GTPase cycle.
DR Reactome; R-XTR-9013423; RAC3 GTPase cycle.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
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: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: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; PF00169; PH; 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 Alternative splicing; Cell projection; GTPase activation;
KW Guanine-nucleotide releasing factor; Reference proteome; Synapse.
FT CHAIN 1..862
FT /note="Active breakpoint cluster region-related protein"
FT /id="PRO_0000355541"
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 30..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"
FT VAR_SEQ 1..21
FT /note="MEPVSHQGMPRLSWIDTLYSN -> MTPRHKPYASSLAALIEGTQRPFLFLV
FT TD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035907"
SQ SEQUENCE 862 AA; 98563 MW; C63164DC19ABB66E CRC64;
MEPVSHQGMP RLSWIDTLYS NFNYGTDGYD AEGNEEHKSS REGSETMPYI DESPTMSPQL
SARSQDSVDG VSPTPTEVLL PGGESESDKG LLMRKLVLSG VLASEEIYIN QLEALLLPMK
PLKATASTSQ PVLTLQQIND IFYKIEDIYQ MHKDFYDKLC PIVLQFDNKT TVGHLFQKLA
SQLGVYKAFV DNYKFALETA EKCSQCNVQF FKISEDLKVK GPKDSKEQPQ SVTMEALLYK
PIDRVTRSTL VLHDLLKHTP TDHPDYPLLQ DALRISQNFL SSINEDIDPR RTAVTTPKGE
PRQLVKDGFL VELSENSRKL RHLFLFTDLL LCAKLKKTTV GKHQQYDCKW YIPLADLVFP
SPEESEPIPQ LHATPDHEIE EMKAKISVLK SEIQKERKSN KGSSRTIERL KKKMFEYESW
LLLYSPTIPF RIHNKNGKSY FFLLSSDYER SEWREAIQKL QKKDLQALAL SPFELQVLTA
SCFKLRTVHN VPIISHKDDD ESPGLYGFLH VIVKSAKGFS HSSNLYCTLE VDSFGYFVSK
AKTRVFRDTT EPEWNEEFEI ELEGSQCLRI LCYEKCYDKS KLNKDNNEIV DKIMGKGQIQ
LDPQVVQSKN WHDDVIEMNG IKVEFSMKFS SRDMSLKRTP SKKQTGVFGV KISVVTKRER
SKVPYIVRQC IEEVEKRGIE EVGIYRISGV ATDIQALKAS FDANSKDILM MLSDMDINAI
AGTLKLYFRE LPEPLLTDRL YLAFMEGIAL SDPAAKENCM MHLLRSLPDP NLMTFLFLLQ
HLKRVAEKEP INKMSLHNLA TVFGPTLLRP SEVESKGHMN LASDIWSHDV MAQVQVLLYY
LQHPPISFSE LKRSTLYYST DV
