GBF1_CRIGR
ID GBF1_CRIGR Reviewed; 1856 AA.
AC Q9R1D7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1;
DE Short=BFA-resistant GEF 1;
GN Name=GBF1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=10402461; DOI=10.1083/jcb.146.1.71;
RA Claude A., Zhao B.-P., Kuziemsky C.E., Dahan S., Berger S.J., Yan J.-P.,
RA Armold A.D., Sullivan E.M., Melancon P.;
RT "GBF1. A novel Golgi-associated bfa-resistant guanine nucleotide exchange
RT factor that displays specificity for ADP-ribosylation factor 5.";
RL J. Cell Biol. 146:71-84(1999).
RN [2]
RP SUBUNIT, AND MUTAGENESIS OF LYS-91; GLU-130 AND ASP-541.
RX PubMed=17640864; DOI=10.1074/jbc.m705525200;
RA Ramaen O., Joubert A., Simister P., Belgareh-Touze N.,
RA Olivares-Sanchez M.C., Zeeh J.C., Chantalat S., Golinelli-Cohen M.P.,
RA Jackson C.L., Biou V., Cherfils J.;
RT "Interactions between conserved domains within homodimers in the BIG1,
RT BIG2, and GBF1 Arf guanine nucleotide exchange factors.";
RL J. Biol. Chem. 282:28834-28842(2007).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF MET-830.
RX PubMed=19182783; DOI=10.1038/nchembio.144;
RA Saenz J.B., Sun W.J., Chang J.W., Li J., Bursulaya B., Gray N.S.,
RA Haslam D.B.;
RT "Golgicide A reveals essential roles for GBF1 in Golgi assembly and
RT function.";
RL Nat. Chem. Biol. 5:157-165(2009).
CC -!- FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the
CC Arf family of small GTPases involved in trafficking in the early
CC secretory pathway; its GEF activity initiates the coating of nascent
CC vesicles via the localized generation of activated ARFs through
CC replacement of GDP with GTP. Recruitment to cis-Golgi membranes
CC requires membrane association of Arf-GDP and can be regulated by ARF1,
CC ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat
CC complex to cellular membranes such as the endoplasmic reticulum exit
CC sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC)
CC and cis-Golgi compartments implicating ARF1 activation. Involved in
CC COPI vesicle-dependent retrograde transport from the ERGIC and cis-
CC Golgi compartments to the endoplasmic reticulum (ER). Involved in the
CC trans-Golgi network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and
CC the AP-1 adaptor protein complex related to chlathrin-dependent
CC transport; the function requires its GEF activity (probably at least in
CC part on ARF4 and ARF5). Has GEF activity towards ARF1 (By similarity).
CC Has in vitro GEF activity towards ARF5 (PubMed:10402461). Involved in
CC the processing of PSAP. Required for the assembly of the Golgi
CC apparatus (PubMed:19182783). The AMPK-phosphorylated form is involved
CC in Golgi disassembly during mitotis and under stress conditions. May be
CC involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid
CC droplets. In neutrophils, involved in G protein-coupled receptor
CC (GPCR)-mediated chemotaxis und superoxide production. Proposed to be
CC recruited by phosphatidylinositol-phosphates generated upon GPCR
CC stimulation to the leading edge where it recruits and activates ARF1,
CC and is involved in recruitment of GIT2 and the NADPH oxidase complex
CC (By similarity). Plays a role in maintaining mitochondrial morphology
CC (By similarity). {ECO:0000250|UniProtKB:Q92538,
CC ECO:0000269|PubMed:10402461, ECO:0000269|PubMed:19182783}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A (BFA) (By similarity).
CC Inhibited by golgicide A (GCA) (PubMed:19182783).
CC {ECO:0000250|UniProtKB:Q92538, ECO:0000269|PubMed:19182783}.
CC -!- SUBUNIT: Can form homodimers and probably homotetramers
CC (PubMed:17640864). Interacts with COPG1; the interaction is independent
CC on ARF1 activation. Interacts with ARF1, ARF3, ARF4 and ARF5. Interacts
CC with RAB1B (GTP-bound form); required for GBF1 membrane association.
CC Interacts with GGA1, GGA2 and GGA3. Interacts with USO1. Interacts (via
CC SEC7 domain) with PNPLA2 (via C-terminus); the interaction is direct.
CC Can form homodimers and probably homotetramers. Interacts with COPG1;
CC the interaction is independent on ARF1 activation. Interacts with ARF1,
CC ARF3, ARF4 and ARF5. Interacts with RAB1B (GTP-bound form); required
CC for GBF1 membrane association. Interacts with GGA1, GGA2 and GGA3.
CC Interacts with USO1. Interacts (via SEC7 domain) with PNPLA2 (via C-
CC terminus); the interaction is direct. Interacts with ARMH3 (By
CC similarity). {ECO:0000250|UniProtKB:Q92538,
CC ECO:0000269|PubMed:17640864, ECO:0000305|PubMed:17640864}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:Q92538}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:Q92538}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92538}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q92538}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92538}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q92538}. Membrane; Peripheral membrane protein
CC {ECO:0000305}. Note=Cycles rapidly on and off early Golgi membranes.
CC Stabilized on membranes when complexed with ARF1-GDP and is released
CC from both ARF1 and membranes after it catalyzes GDP displacement and
CC ARF1 binds GTP. Continuous cycles of recruitment and dissociation of
CC GBF1 to membranes are required for sustained ARF activation and COP I
CC recruitment (By similarity). {ECO:0000250|UniProtKB:Q92538}.
CC -!- DOMAIN: The DCB (dimerization and cyclophiln-binding) and HUS (homology
CC upstream of Sec7) domains are necessary for dimerization. The DCB
CC domain is proposed to support constitutive homodimerization; the HUS
CC domain interacts with the DCB domain which may occur intramolecular or
CC intermolecular. {ECO:0000269|PubMed:17640864,
CC ECO:0000305|PubMed:17640864}.
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DR EMBL; AF127523; AAD45661.1; -; mRNA.
DR RefSeq; NP_001233615.1; NM_001246686.1.
DR AlphaFoldDB; Q9R1D7; -.
DR SMR; Q9R1D7; -.
DR STRING; 10029.NP_001233615.1; -.
DR PRIDE; Q9R1D7; -.
DR GeneID; 100689421; -.
DR KEGG; cge:100689421; -.
DR CTD; 8729; -.
DR eggNOG; KOG0928; Eukaryota.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Guanine-nucleotide releasing factor;
KW Lipid droplet; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Transport.
FT CHAIN 1..1856
FT /note="Golgi-specific brefeldin A-resistance guanine
FT nucleotide exchange factor 1"
FT /id="PRO_0000120209"
FT DOMAIN 690..880
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 1..378
FT /note="Interaction with RAB1B"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT REGION 1..211
FT /note="DCB (dimerization and cyclophiln-binding); DCB:DCB
FT domain and DCB:HUS domain interaction"
FT /evidence="ECO:0000269|PubMed:17640864"
FT REGION 215..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..548
FT /note="HUS (homology upstream of Sec7); DCB:HUS domain
FT interaction"
FT /evidence="ECO:0000269|PubMed:17640864"
FT REGION 601..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1370
FT /note="Phosphatidylinositol-phosphate binding; required for
FT translocation to the leading edge and for ARF1 activation
FT upon GPCR signaling"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT REGION 1284..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1314
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1335
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MOD_RES 1781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92538"
FT MUTAGEN 91
FT /note="K->A: Disrupts DCB:DCB domain interaction; decreases
FT DCB:HUS domain interaction."
FT /evidence="ECO:0000269|PubMed:17640864"
FT MUTAGEN 130
FT /note="E->A: Disrupts DCB:DCB domain and DCB:HUS domain
FT interaction."
FT /evidence="ECO:0000269|PubMed:17640864"
FT MUTAGEN 541
FT /note="D->A: Disrupts DCB:HUS domain interaction."
FT /evidence="ECO:0000269|PubMed:17640864"
FT MUTAGEN 830
FT /note="M->L: Confers GCA tolerance."
FT /evidence="ECO:0000269|PubMed:19182783"
SQ SEQUENCE 1856 AA; 206192 MW; 46E8962C0E08EDBF CRC64;
MVDKNIYIIQ GEINIVVGAI KRNARWSTHI PLDEERDPLL HSFSHLKEVL NSVTELSEIE
PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP THEGTAEGME NMADAVTHAR
FVGTDPASDE VVLMKILQVL RTLLLTPVGT HLTNESVCEI MQSCFRICFE MRLSELLRKS
AEHTLVDMVQ LLFTRLPQFK EEPKSYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM
TRVTPGSELP APNGATLSCN LTSGMPFIDV PSSISSASSE AASAVVSPCT DSGLELSSQT
TSKEDLTDLE QAGSPRESTT TESGSNEIGV SDQLDPQEGS HVEKAQSASV ESIPEVLEEC
TSPPDHSASV HDMDYVNPRG VRFTQSSQKE GTALVPYGLP CIRELFRFLI SLTNPHDRHN
SEGMIHMGLH LLTVALESAP VAQCQTLLGL IKDEMCRHLF QLLSVERLNL YAASLRVCFL
LFESMREHLK FQLEMYMKKL MEIITVENPK MPYEMKEMAL EAIVQLWRIP SFVTELYINY
DCDYYCANLF EDLTKLLSKN AFPVSGQLYT THLLSLDALL TVIDSTEAHC QAKVLNTLTQ
QEKKETSRPS YEAVDSTQEA NSTERATIDG KATGMASDAL GLHLQSGGWL SAEHGKPRCN
DVEEAGDSGA DKKFTRKPPR FSCLLPDPRE LIEIKNKKKL LITGTEQFNQ KPKKGIQFLQ
EKGLLTIPMD NTEVAQWLRE NPRLDKKMIG EFVSDRKNID LLESFVSTFS FQGLRLDEAL
RLYLEAFRLP GEAPVIHRLL EAFTEHWRSC NGSPFANSDA CFALAYAVIM LNTDQHNHNV
RKQNVPMTLE EFRKNLKGVN GGKDFEQDIL EDMYHAIKNE EIVMPEEQTG LVRENYVWSV
LLHRGATPEG IFLRVPPGSY DLDLFTMTWG PTIAALSYVF DKSIEETIIQ KAISGFRKCA
MISAHYGLSD VFDNLIISLC KFTALSSESI ENLPTVFGSN PKAHIAAKTV FHLAHRHGDI
LREGWKNIME AVLQLFRAQL LPQAMVEVED FVDPNGKISL QREEMPSNRG ESSVLSFVSW
LTLSGPEQSS VRGPSTENQE AKRVALDCIK QCDPEKMITE SKFLQLESLQ ELMKALVSVT
ADEETYDEED AAFCLEMLLR IVLENRDRVG CVWQTVRDHL YHLCVQAQDF CFLVERAVVG
LLRLAIRLLR REEISGQVLL SLRILLLMKP SVLSRVSHQV AYGLHELLKT NAANIHSGDD
WATLFTLLEC IGSGVKPPDA LQATARADAP DAGAQSDSEL PSYHQNDVSL DRGYTSDSEV
YTDHGRPGKI HRSATDADMV NSGWLVVGKD DIDNSKAGAG LSRPSPSPLV NQYSLTVGLD
LGPHDTKSLL KCVESLSFIV RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQDKRGKSH
KYDSKGNRFK KKPKEGSVLR RPRTSSQHGT RGGHSDEEED EGVPASYHTV SLQVSQDLLD
LMHTLHTRAA SIYSSWAEEQ RHLESGGRKI EADSRTLWAH CWCPLLQGIA CLCCDARRQV
RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL LENISPADVG GMEETRMRAS
TLLSKVFLQH LSPLLSLSTF AALWLTILDF MDKYMHAGSS DLLSEAIPES LKNMLLVMDT
AEIFHSADAR GGSPSALWEI TWERIDCFLP HLRDELFKQT VIQDPMPTEP HSQNALASTH
LTPAAGDPGH LPSPEIPSEV GACDSEKPEG TRATSSSSPG SPVASSPSRL SPSPEGPPPL
AQPPLILQPL TSPLQVGVPP MALPIILNPA LIEATSPVPL LSTPRPTDPI PTSEVN
