ABR_BOVIN
ID ABR_BOVIN Reviewed; 859 AA.
AC A6QNS3; Q29RJ4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Active breakpoint cluster region-related protein;
GN Name=ABR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Hereford; TISSUE=Fetal cerebellum, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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 (By similarity). Functions as
CC an important negative regulator of neuronal RAC1 activity (By
CC similarity). Regulates macrophage functions such as CSF1-directed
CC motility and phagocytosis through the modulation of RAC1 activity (By
CC similarity). {ECO:0000250|UniProtKB:Q12979,
CC ECO:0000250|UniProtKB:Q5SSL4}.
CC -!- SUBUNIT: Interacts with DLG4. {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=A6QNS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6QNS3-2; Sequence=VSP_035900, VSP_035901, VSP_035902;
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; BC114145; AAI14146.1; -; mRNA.
DR EMBL; BC148971; AAI48972.1; -; mRNA.
DR RefSeq; NP_001039669.2; NM_001046204.2. [A6QNS3-1]
DR AlphaFoldDB; A6QNS3; -.
DR SMR; A6QNS3; -.
DR STRING; 9913.ENSBTAP00000011083; -.
DR PaxDb; A6QNS3; -.
DR PRIDE; A6QNS3; -.
DR Ensembl; ENSBTAT00000011083; ENSBTAP00000011083; ENSBTAG00000008424. [A6QNS3-1]
DR Ensembl; ENSBTAT00000035191; ENSBTAP00000035069; ENSBTAG00000008424. [A6QNS3-2]
DR GeneID; 515556; -.
DR KEGG; bta:515556; -.
DR CTD; 29; -.
DR VEuPathDB; HostDB:ENSBTAG00000008424; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004000_1_0_1; -.
DR InParanoid; A6QNS3; -.
DR OMA; RILCYEN; -.
DR OrthoDB; 762492at2759; -.
DR TreeFam; TF105082; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008424; Expressed in prefrontal cortex and 105 other tissues.
DR ExpressionAtlas; A6QNS3; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; 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; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..859
FT /note="Active breakpoint cluster region-related protein"
FT /id="PRO_0000355538"
FT DOMAIN 91..284
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 301..459
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 484..613
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 647..845
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 27..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSL4"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035900"
FT VAR_SEQ 219..233
FT /note="GPKDSRDSHTSVTME -> MEILLIIRFCCNCTY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035901"
FT VAR_SEQ 326..689
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035902"
SQ SEQUENCE 859 AA; 97612 MW; 84797AC01471015B CRC64;
MEPLSHRGLP RLSWIDTLYS NFSYGADDYD AEGNEEQKGP PEGSETMPYI DESPTMSPQL
SARSQGGGDS ISPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL
KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ
LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSRDSHTSV TMEALLYKPI
DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR
QLVKDGFLVE VSEGSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP
EESEASPQVH PFPDHELEDM KMKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL
NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF
KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT
RVFRDTTEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP
QTVETKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QSGVFGVKIS VVTKRERSKV
PYIVRQCVEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT
LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK
RVAEKEPVNK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH
PPISFAELKR NTLYFSTDV
