ID A0A2R9A567_PANPA Unreviewed; 755 AA.
AC A0A2R9A567;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE SubName: Full=GIT ArfGAP 1 {ECO:0000313|Ensembl:ENSPPAP00000012438.1};
GN Name=GIT1 {ECO:0000313|Ensembl:ENSPPAP00000012438.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000012438.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000012438.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000012438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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DR EMBL; AJFE02040574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9A567; -.
DR STRING; 9597.ENSPPAP00000012438; -.
DR Ensembl; ENSPPAT00000035103.1; ENSPPAP00000012438.1; ENSPPAG00000029400.1.
DR GeneTree; ENSGT00940000159604; -.
DR Proteomes; UP000240080; Chromosome 17.
DR Bgee; ENSPPAG00000029400; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0061743; P:motor learning; IEA:Ensembl.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IEA:Ensembl.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
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; 1.20.120.330:FF:000002; 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 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.
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|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; 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:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 7..117
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 159..191
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 348..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 83616 MW; 6003174C196ED5AD CRC64;
MQLSPKGPRM DPGWASISRG VLVCDECCSV HRSLGRHISI VKHLRHSAWP PTLLQMVHTL
ASNGANSIWE HSLLDPAQVQ SGRRKANPQD KVHPIKSEFI RAKYQMLAFV HKLPCRDDDG
VTAKDLSKQL HSSVRTGNLE TCLRLLSLGA QANFFHPEKG TTPLHVAAKA GQTLQAELLV
VYGADPGSPD VNGRTPIDYA RQAGHHELAE RLVECQYELT DRLAFYLCGR KPGESLLSSQ
FPSPSALSLD LSELAKAAKK KLQALSNRLF EELAMDVYDE VDRRENDAVW LATQNHSTLV
TERSAVPFLP VNPEYSATRN QGRQKLARFN AREFATLIID ILSEAKRRQQ GKSLSSPTDN
LELSLRSQSD LDDQHDYDSV ASDEDTDQEP LRSTGATRSN RARSMDSSDL SDGAVTLQEY
LELKKALATS EAKVQQLMKV NSSLSDELRR LQREIHKLQA ENLQLRQPPG PVPTPPLPTE
RAEHTPMAPG GSTHRRDRQA FSMYEPGSAL KPFGAPPGDE LTTRLQPFHS TELEDDAIYS
VHVPAGLYRI RKGVSASAVP FTPSSPLLSC SQEGSRHTSK LSRHGSGADS DYENTQSGDP
LLGLEGKRFL ELGKEEDFHP ELESLDGDLD PGLPSTEDVI LKTEQVTKNI QELLRAAQEF
KHDSFVPCSE KIHLAVTEMA SLFPKRPALE PVRSSLRLLN ASAYRLQSEC RKTVPPEPGA
PVDFQLLTQQ VIQCAYDIAK AAKQLVTITT REKKQ
//