ID B7Z4Q0_HUMAN Unreviewed; 444 AA.
AC B7Z4Q0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3 {ECO:0000256|ARBA:ARBA00039243};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAH12636.1};
RN [1] {ECO:0000313|EMBL:BAH12636.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:BAH12636.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of
CC coatomer from Golgi-derived membranes to allow fusion with target
CC membranes. {ECO:0000256|ARBA:ARBA00037105}.
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; AK297635; BAH12636.1; -; mRNA.
DR AlphaFoldDB; B7Z4Q0; -.
DR PeptideAtlas; B7Z4Q0; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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:SF1; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 3; 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 2: Evidence at transcript level;
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}; 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 10..87
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48970 MW; 1FC0362C6B9CFB3A CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
YIRSTELDSN WSWFQLRCMQ VGGNASAVSD TAWASAIAEP SSLTSRPVET TLENNEGGQE
QGPSVEGLNV PTKATLEVSS IIKKKPNQAK KGLGAKKGSL GAQKLANTCF NEIEKQAQAA
DKMKEQEDLA KVVSKEESIV SSLRLAYKDL EIQMKKDEKM NISGKKNVDS DRLGMGFGNC
RSVISHSVTS DMQTIEQESP IMAKPRKKYN DDSDDSYFTS SSRYFDEPVE LRSSSFSSWD
DSSDSYWKKE TSKDTETVLK TTGYSDRPTA RRKPDYEPVE NTDEAQKKFG NVKAISSDMY
FGRQSQADYE TRARLERLSA SSSISSADLF EEPRKQPAGN YSLSSVLPNA PDMAQFKQGV
RSVAGKLSVF ANGVVTSIQD RYGS
//
