ARFG2_RAT
ID ARFG2_RAT Reviewed; 520 AA.
AC Q3MID3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=Zfp289, Znf289;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-236; SER-239;
RP SER-339 AND SER-431, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1). May regulate coatomer-mediated protein transport from the Golgi
CC complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may
CC lead to dissociation of coatomer from Golgi-derived membranes to allow
CC 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}.
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DR EMBL; BC101917; AAI01918.1; -; mRNA.
DR RefSeq; NP_001028879.1; NM_001033707.1.
DR PDB; 5NZS; EM; 10.10 A; P=1-520.
DR PDBsum; 5NZS; -.
DR AlphaFoldDB; Q3MID3; -.
DR SMR; Q3MID3; -.
DR IntAct; Q3MID3; 1.
DR STRING; 10116.ENSRNOP00000053988; -.
DR iPTMnet; Q3MID3; -.
DR PhosphoSitePlus; Q3MID3; -.
DR jPOST; Q3MID3; -.
DR PaxDb; Q3MID3; -.
DR PRIDE; Q3MID3; -.
DR Ensembl; ENSRNOT00000057161; ENSRNOP00000053988; ENSRNOG00000014429.
DR GeneID; 362162; -.
DR KEGG; rno:362162; -.
DR UCSC; RGD:1306177; rat.
DR CTD; 84364; -.
DR RGD; 1306177; Arfgap2.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000155568; -.
DR HOGENOM; CLU_023062_6_2_1; -.
DR InParanoid; Q3MID3; -.
DR OMA; QNVGESI; -.
DR OrthoDB; 1155557at2759; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR PRO; PR:Q3MID3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014429; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q3MID3; RN.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; ER-Golgi transport;
KW Golgi apparatus; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW 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_0000278471"
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"
FT REGION 163..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..307
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 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6H7"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 56556 MW; 4F1E74D2593F1EA0 CRC64;
MAAGPSKSEI QTLFKRLRAI PTNKACFDCG AKSPSWASIT YGVFLCIDCS GVHRSLGVHL
SFIRSTELDS NWSWLQLRCM QVGGNANATA FFRQHGCLAN DANTKYNSRA AQMYREKIRQ
LGSTALARHG TDLWIDNMNS APSHSPEKKD SDFFTEHTQA PAWDTAATDP SGTQQPALPS
ESSSLAQPEP GPNTDLLGTS PQASLELKSS IIGKKKPAAA KKGLGAKKGL GAQKVSNQSF
TEIERQAQVA EKLREQQAAD AKKQAEESMV ASMRLAYQEL QIDRKKEEKK LQNLEGKKRE
QAERLGMGLV SRSSISHSVL SEMQMIEQET PLSAKSSRSQ LDLFDDVGTF ASGPPKYKDN
PFSLGETFGS RWDSDAAWGM DRVEEKEPEV TISSIRPISE RTTSRREVES RISGLESSEA
RQKFAGAKAI SSDMFFGREV DSEYEARSRL QQLSGSSAIS SSDLFGDVDG AHGGGTVSLG
NVLPTADIAQ FKQGVKSVAG KMAVLANGVM NSLQDRYGSY
