ID A0A2I3HFX1_NOMLE Unreviewed; 493 AA.
AC A0A2I3HFX1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 2 {ECO:0000256|ARBA:ARBA00039244};
DE AltName: Full=Zinc finger protein 289 {ECO:0000256|ARBA:ARBA00043100};
GN Name=ARFGAP2 {ECO:0000313|Ensembl:ENSNLEP00000042407.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000042407.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000042407.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000042407.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}.
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DR EMBL; ADFV01115836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003279007.1; XM_003278959.3.
DR AlphaFoldDB; A0A2I3HFX1; -.
DR Ensembl; ENSNLET00000049593.1; ENSNLEP00000042407.1; ENSNLEG00000014290.2.
DR GeneTree; ENSGT00940000155568; -.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd09029; ArfGap_ArfGap2; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR PANTHER; PTHR45686:SF10; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}; Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 11..117
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 128..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 141..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 53509 MW; F4D00D0FB4E48BA7 CRC64;
MAAEPNKTEI QTLFKRLRAV PTNKACFDCG AKNPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS NWNWFQLRCM QVGGNANATA FFRQHGCTAN DANTKYNSRA AQMYREKIRQ
LGSAALARHG TDPPAWDAPA TEPSGTQQPA LSTESSGLTQ PEHGPNTDLL GTSPKASLEL
KSSIIGKKKP AAAKKGLGAK KGLGAQKVSS QSFSEIERQA QVAEKLREQQ AADAKKQAEE
SMVASMRLAY QELQIDRKKE EKKLQNLEGK KREQAERLGM GLVSRSSVSH SVLSEMQVIE
QETPVSAKSS RSQLDVFDDV GTFASGPPKY KDNPFSLGES FGSRWDTDAA WGMDRVEEKE
PEVTISSIRP ISERATNRRE VESRSSGLES SEARQKFAGA KAISSDMFFG REVDAEYEAR
SRLQQLSGSS AISSSDLFGD MDGAHGAGSV SLGNVLPTAD IAQFKQGVKS VAGKMAVLAN
GVMNSLQDRY GSY
//