ARFG2_BOVIN
ID ARFG2_BOVIN Reviewed; 520 AA.
AC A1L520;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 2;
DE Short=ARF GAP 2;
DE AltName: Full=Zinc finger protein 289;
GN Name=ARFGAP2; Synonyms=ZNF289;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:ABM06074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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).
CC {ECO:0000250|UniProtKB:Q8N6H7}.
CC -!- SUBUNIT: Interacts with the coatomer complex. Interacts with C-terminal
CC appendage domain of COPG1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N6H7}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q8N6H7}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8N6H7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8N6H7}. Note=Also found on peripheral punctate
CC structures likely to be endoplasmic reticulum-Golgi intermediate
CC compartment. {ECO:0000250|UniProtKB:Q8N6H7}.
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DR EMBL; BT029807; ABM06074.1; -; mRNA.
DR RefSeq; NP_001073696.1; NM_001080227.1.
DR AlphaFoldDB; A1L520; -.
DR SMR; A1L520; -.
DR STRING; 9913.ENSBTAP00000012592; -.
DR PaxDb; A1L520; -.
DR PeptideAtlas; A1L520; -.
DR PRIDE; A1L520; -.
DR GeneID; 505438; -.
DR KEGG; bta:505438; -.
DR CTD; 84364; -.
DR eggNOG; KOG0706; Eukaryota.
DR InParanoid; A1L520; -.
DR OrthoDB; 1155557at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 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..520
FT /note="ADP-ribosylation factor GTPase-activating protein 2"
FT /id="PRO_0000314051"
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..520
FT /note="Required for interaction with coatomer"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT REGION 159..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 242..307
FT /evidence="ECO:0000255"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 431
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 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
SQ SEQUENCE 520 AA; 56758 MW; C43E5AB83976AA46 CRC64;
MAAEPNKTEI QTFFKRLRAI PTNKACFDCG AKNPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS TWSWFQLRCM QVGGNANATA FFRQHGCTAN DANTKYNSRA AQMYREKIRQ
LGSAALARHG TDLWTDSVST APSHSPEKKE SDFFLEHTQP PAWNAPVTDL SETQQPAPSA
ESSGLAQPEH GPNMDLLGTS PKASLEPKTS LIGKKKPAAA KKGLGAKKGL GAQKVSSQSF
SEIERQAQVA EKLREQQVAD AKKQAEESMV ASMRLAYQEL QIDRKKEEKK LQNLEGKKRE
QAERLGMGLV SRSSVSHSVL SEMQVIEQET PVSAKSSRSQ LDLFDDVGTF ASGPPKYKDN
PFSLGESFGS RWDTDTAWGM DRMEEKEPEV TVSSIRPVSE RVTNRREVES RSSGLESSEA
RQKFAGAKAI SSDMFFGREV DTEYEARSRL QQLSGSSAIS SSDLFGDVDG AHGAGSVSLG
NVLPTADIAQ FKQGVKSVAG KMAVLANGVM NSLQDRYGSY
