ID A0A3Q3KS63_9TELE Unreviewed; 783 AA.
AC A0A3Q3KS63;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 18-JUN-2025, entry version 31.
DE SubName: Full=G protein-coupled receptor kinase interacting ArfGAP 1 {ECO:0000313|Ensembl:ENSMAMP00000004178.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000004178.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000004178.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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DR AlphaFoldDB; A0A3Q3KS63; -.
DR FunCoup; A0A3Q3KS63; 935.
DR STRING; 205130.ENSMAMP00000004178; -.
DR Ensembl; ENSMAMT00000004281.2; ENSMAMP00000004178.2; ENSMAMG00000002752.2.
DR GeneTree; ENSGT00940000159604; -.
DR InParanoid; A0A3Q3KS63; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR GO; GO:0098794; C:postsynapse; IEA:TreeGrafter.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0036465; P:synaptic vesicle recycling; IEA:TreeGrafter.
DR FunFam; 1.25.40.20:FF:000013; ARF GTPase-activating protein GIT1 isoform 1; 1.
DR FunFam; 1.10.220.150:FF:000003; ARF GTPase-activating protein GIT2 isoform 1; 1.
DR FunFam; 1.20.5.170:FF:000015; ARF GTPase-activating protein GIT2 isoform 1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR047161; GIT-like.
DR InterPro; IPR032352; GIT1/2_CC.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR PANTHER; PTHR46097:SF1; ARF GTPASE-ACTIVATING PROTEIN GIT1; 1.
DR PANTHER; PTHR46097; G PROTEIN-COUPLED RECEPTOR KINASE INTERACTING ARFGAP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF16559; GIT_CC; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|SMART:SM00105"
FT DOMAIN 264..294
FT /note="GIT Spa2 homology (SHD)"
FT /evidence="ECO:0000259|SMART:SM00555"
FT DOMAIN 328..358
FT /note="GIT Spa2 homology (SHD)"
FT /evidence="ECO:0000259|SMART:SM00555"
FT REGION 354..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..497
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 84910 MW; 0396FBF14B672665 CRC64;
MSRKLQRTEV CADCSAPDPG WTSINRGVLI CDECCSVHRS LGRHISIVKH LRHSGWPPTL
LQMVQTLASN GANSIWEHSL LDPAQVQSGR RKPNPQDKVH PTKSEFIRAK YQMLAFVHKL
PCRDDDGVTT KDLSKQLHSS VRTGSLETCL RLLSLGAQAN FFHPEKGTTP LHVAAKAGQI
LQAELLVVYG ADPGAPDING RSPMDYARQA GHIELAERLV ECQYELTDRL AFYLCGRRPD
HKNGHYIIPQ MADSLDLSEL AKAAKKKLQA LNNRLFEELA MDVYDEVDRR ENDAVWLTTQ
NHSTLVTERS AVPFLPVNPE YSATRNQGRQ KLARFNAREF ATLIIDILSD AKRRQQGKGL
SSPTDPLDLG IDDDQHDYDS VASDEDTDSE LTTQNNNNTQ RSNRAKSMDS SDLSDGPITL
QEYLEVKKAL ASSEAKVQQL MKVNNNLSEE LRRLQKEITR MQTENSVLRG SQQAGGTAGH
GVGGPGGGGG GGGGGGGVHW QGNVMRGVIS GGGLSGFGSG ADPPGLSVPS SVAPHSHLHR
RDRQAFSMYE PGAAPGPTAH GPPALDSLAA RLQPLNTPSV RKGSTGSPAP YGGQHLSGST
EMGRYMVPKP EKHGSGTDSD YDNTQTYDVS LSMGRSSEEE GRGESEDGGG GEAGEPDPTL
PCTEDVILKT EQVTKNIQEL LRAAQEFKHD SFVPCSEKIH SAVTEMASLF PKRPALDAVH
CSLRLLASSA SRLQVECRKA APSEPGAPAV DYQLLTQQVI QCAYDIAKAA KQLVTITTRE
KKQ
//
