ARFG2_PONAB
ID ARFG2_PONAB Reviewed; 521 AA.
AC Q5RAT7; Q5R6A6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- SEQUENCE CAUTION:
CC Sequence=CAH92710.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR858925; CAH91123.1; -; mRNA.
DR EMBL; CR860588; CAH92710.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001125657.1; NM_001132185.1.
DR AlphaFoldDB; Q5RAT7; -.
DR SMR; Q5RAT7; -.
DR STRING; 9601.ENSPPYP00000003801; -.
DR GeneID; 100172577; -.
DR KEGG; pon:100172577; -.
DR CTD; 84364; -.
DR eggNOG; KOG0706; Eukaryota.
DR InParanoid; Q5RAT7; -.
DR OrthoDB; 1155557at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated 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 Acetylation; Coiled coil; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT CHAIN 2..521
FT /note="ADP-ribosylation factor GTPase-activating protein 2"
FT /id="PRO_0000278470"
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..521
FT /note="Required for interaction with coatomer"
FT /evidence="ECO:0000250"
FT COILED 242..308
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT CONFLICT 38
FT /note="S -> R (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="N -> S (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="Q -> R (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> V (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> T (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="N -> S (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="M -> I (in Ref. 1; CAH92710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 57301 MW; 4DE003F1C19F3B87 CRC64;
MAAEPNKTEI QTLFKRLRAV PTNKACFDCG AKNPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS NWNWFQLRCM QVGGNANATA FFRQHGCTAN DANTKYNSRA AQMYREKIRQ
LGSAALARHG TDLWIDNMSS AVPNHSPEKK DSDFFTEHTQ PPAWDAPPLS LQGPSSQPRL
QRAVAWHSRS MAPTQTCLAP HPKPHWNWKS SIIGKKKPAA AKKGLGAKKG LGAQKVSSQS
FSEIERQAQV AEKLREQQAA DAKKQAEESM VASMRLAYQE LQIDRKKEEK KLQNLEGKKR
EQAERLGMGL VSRSSVSHSV LSEMQVIEQE TPVSAKSSRS QLDLFDDVGT FASGPPKYKD
NPFSLGESFG SRWDTDAAWG MDRVEEKEPE VTISSIRPIS ERATNRREVE NRSSGLESSE
ARQKFAGAKA ISSDMFFGRE VDAEYEARSR LQQLSGSSAI SSSDLFGDMD GAHGAGSVSL
GNVLPTADIA QFKQGVKSVA GKMAVLANGV MNSLQDRYGS Y
