RASA3_BOVIN
ID RASA3_BOVIN Reviewed; 834 AA.
AC Q28013;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ras GTPase-activating protein 3;
DE AltName: Full=GAP1(IP4BP);
DE AltName: Full=Ins P4-binding protein;
GN Name=RASA3;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=8530488; DOI=10.1074/jbc.270.51.30557;
RA Yamamoto T., Matsui T., Nakafuku M., Iwamatsu A., Kaibuchi K.;
RT "A novel GTPase-activating protein for R-Ras.";
RL J. Biol. Chem. 270:30557-30561(1995).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind
CC inositol tetrakisphosphate (IP4).
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DR EMBL; U30857; AAC48500.1; -; mRNA.
DR AlphaFoldDB; Q28013; -.
DR SMR; Q28013; -.
DR STRING; 9913.ENSBTAP00000026598; -.
DR PaxDb; Q28013; -.
DR PRIDE; Q28013; -.
DR eggNOG; KOG2059; Eukaryota.
DR InParanoid; Q28013; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13371; PH_GAP1_mammal-like; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR037774; RASA3_PH.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 2.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 2: Evidence at transcript level;
KW Acetylation; GTPase activation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT CHAIN 2..834
FT /note="Ras GTPase-activating protein 3"
FT /id="PRO_0000056641"
FT DOMAIN 1..112
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 123..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 330..524
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 576..677
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 679..715
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT REGION 806..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60790"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60790"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14644"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60790"
SQ SEQUENCE 834 AA; 95386 MW; AB996368A27174BA CRC64;
MAVEEEGLRV FQSVKIKIGE AKNLPTYPGP NKMRDCYCTV NLDQEEVFRT KVVEKSLCPF
YGEDFYCEIP RSFRHLSFYI FDRDVFRRDS IIGKVAIKKE DLQKYHNRDT WFQLQHVDAD
SEVQGKVHLE LRLSEVITDS GVVCHKLATR ILECQGLPIV NGQCDPYATV TLAGPCRSEA
KKTKVKKKTN NPQFDEVFYF EVTRPCSYSR KSHFDFEDED VDKLEIRVDL WNASNLKFGD
EFLGELRVPL KVLRQSSPHE AWYFLQPRDN GSKSLKPGDL GSLRLNVVYT EDHVFSSDYY
SPLRDLLLKS ADVEPVSASA AHILGEVCRE KQEAAIPLVR LFLHYGRVVP FISAIASAEV
RRTQDPNTIF RGNSLTSKCI DETMKLAGMQ YLHVTLKPTI EEICQSHKSC EIDPVRLKDG
ESLESNMENL RQFVDRVFSV ITKSGVSCPT VMCDIFFSLR EAAAKRFQDD LDVRYTAVSS
FIFLRFFAPA ILSPNLFQLT PHHTDPQTSR TLTLVSKTIQ TLGSLSKSKS ASFKESYMAA
FYEFFNEQKY ADAVKNFLDL ISSSGRRDPK SVQQPILLKE GFMIKRAQGR KRFGMKNFKK
RWFRLTNHEF TYQKSKGDPP LYSIPIENIL AVEPLEEESF KMKNMFQVIQ PERALYIQAN
NCVEAKAWID ILTKVSQCNQ KRLAVYHPSA YLNGHWLCCR ASSDTAAGCS PCTGGLPANI
QLDIDGDRET ERIYSLSSSY MSKLETMQEA CGSRSVYDGP EQEEYSTFII DDPQETYKTL
KQVVAGVGAL EQEHAQYKRD KFRRTKYGSQ EHPIGDKSFQ SYIRQQSETP AHSM
