ID A0A1S3K2V6_LINUN Unreviewed; 807 AA.
AC A0A1S3K2V6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ARF GTPase-activating protein GIT2 isoform X2 {ECO:0000313|RefSeq:XP_013416586.1};
GN Name=LOC106178098 {ECO:0000313|RefSeq:XP_013416586.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013416586.1};
RN [1] {ECO:0000313|RefSeq:XP_013416586.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013416586.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013416586.1; XM_013561132.1.
DR AlphaFoldDB; A0A1S3K2V6; -.
DR EnsemblMetazoa; XM_013561132.1; XP_013416586.1; LOC106178098.
DR GeneID; 106178098; -.
DR OrthoDB; 2877020at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd08833; ArfGap_GIT; 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:SF3; ARF GTPASE-ACTIVATING PROTEIN GIT; 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; 2.
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.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 1..126
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 166..198
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 82..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 356..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 89311 MW; D3DBD939E326687F CRC64;
MSRGKGRTPS EICSDCGAPD PSWASVNRGV LMCDECCSIH RSLGRHISHV KSLKKGNWHP
TLLQMVHQLV SQSTNSIWEH TLLDPTQNKQ GRRKPNPRDQ LHPMKADFIR AKYQFLAFAQ
KPKDEENQSV EDLSKQLHSC VRTGNLETTL RLLSFGANPN YFHQERGNCP IHVAAQSGQA
TQVELVVIYG ADPGAVDSGG KTAADYAKAE GYTDLSNRIV ELQYELTDRL AYYLCGRKPD
HKMGQHFIIP EMADSSLDLS ELAKAAKKQL QGLPNHLFEE LAMDVYDEVD RRENDKIWLG
SQNHNALVSD RQAVPFLPVN PEFSSTRNQG RQKLARFNAR EFATLIIDVL SDAKRRQQGI
TSPVHTPRDR EQVSLANSST KESRGVPKTS SFSDDEPVYD SVASDEDYSS IGGDVASLKD
SDIQNTQKKE GVLEDACRSS GSPTSMISFT ESMASSDQSD GPITSQDYHD LKRALAQSDS
VVHQLMAKNA QLVEEVKRLH SAVQRLTQEN ATLQGQHAIG SSHAVGSAHI LSSPHASASV
PSLSNGYDNV SSLKQQQQLP STQPSPTQPE FDTAVPRRHI GQLSRPQSMF EPRNHHRLPW
QKTYTPFRDD NAIGTGSHRI SEEYSLDERE SPPRQFSREG NASDSDYDNA NKETEDRQRE
STLTPSPDEA EGAVGPCTQD GYEMQEGLPT QEQVVKKTEI ITKKIQELLK NAQEGNHESY
SPCADKILSA VSEMTAIFPQ NVNSDCIGQA LQQLGGGADR LCHECKSLPI KGEDGQLDYA
SKTPQVIQCA FDIAKAAKQL VTLFERA
//
