ID   ARFG2_XENTR             Reviewed;         526 AA.
AC   Q28CM8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 2;
DE            Short=ARF GAP 2;
DE   AltName: Full=GTPase-activating protein ZNF289;
DE   AltName: Full=Zinc finger protein 289;
GN   Name=arfgap2; Synonyms=znf289; ORFNames=TEgg043a17.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC       (ARF1). Implicated in coatomer-mediated protein transport between the
CC       Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound
CC       GTP may lead to dissociation of coatomer from Golgi-derived membranes
CC       to allow fusion with target membranes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the coatomer complex. Interacts with the C-
CC       terminal appendage domain of COPG1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Also found on peripheral punctate structures
CC       likely to be endoplasmic reticulum-Golgi intermediate compartment.
CC       {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR926298; CAJ81762.1; -; mRNA.
DR   EMBL; BC122890; AAI22891.1; -; mRNA.
DR   AlphaFoldDB; Q28CM8; -.
DR   SMR; Q28CM8; -.
DR   STRING; 8364.ENSXETP00000011114; -.
DR   PaxDb; Q28CM8; -.
DR   eggNOG; KOG0706; Eukaryota.
DR   InParanoid; Q28CM8; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000005097; Expressed in gastrula and 27 other tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048205; P:COPI coating of Golgi vesicle; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW   GTPase activation; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..526
FT                   /note="ADP-ribosylation factor GTPase-activating protein 2"
FT                   /id="PRO_0000278472"
FT   DOMAIN          11..127
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   ZN_FING         26..49
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          97..526
FT                   /note="Required for interaction with coatomer"
FT                   /evidence="ECO:0000250"
FT   REGION          159..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          247..314
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        386..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  57224 MW;  378B3442F2BF4D4A CRC64;
     MAAEPTKAEI QAVFKRLRAA PTNKSCFDCG AKNPSWASIP YGVFLCIDCS GVHRSLGVHL
     SFIRSTELDS NWSWFQLRCM QVGGNASANA FFHQHGATTS DTNAKYNSRS AQMYREKIRQ
     LANAAMSKHG TDLWIDGMNC ALVQPAEKKE SDFFAEMTQP SSSWEATPAS EPTSTTVTTV
     TRTISSPETA DSASAECGPS VDILSTSPKA AVEVKPSLIG KKKVNTAKKG LGAKKGLGAQ
     KVSSQSFSEI ERRAQVAEKL REQQAAELKK EAEESLVSSM RLAYQELQID RKQEEKKLQN
     LEGKKREQAE RLGMGLAARS SISHSLLSEM HVIEQETPVA NKSSRSQLDL LEDASFTSGP
     PKYKDNPFSL GDGFSSRWET ESSSWGSADK AEEEREVTIS SIQPARDRPA NRRKPEGAPA
     PESNEARMKF ASAKAISSDM FFGRENDAEY EARSRLQQLS SSNSISSADL FGDPNAVNLS
     GGVSLGNVMP AADITHFKQG VKSVAGKMAV LANGVMNSLQ DRYSSY