GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1

GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Magnify GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1Enlarged view of image
3D view in GLMol or JMol

gray dot

Download Coordinates

gray dot

Topology in Golgi apparatus membrane
TopologyGolgi lumenal side
cytoplasmic side
GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 » BFA-resistant GEF 1;
Hydrophobic Thickness 30.4 ± 3.9 Å
Tilt Angle 6 ± 16°
ΔGtransfer -17.2 kcal/mol
ΔGfold -9.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology In
TM Segments 1634-1654 (1631-1654)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 400-551, Guanine nucleotide exchange factor in Golgi transport N-terminal

AA: 699-884, PDBID: 2R09, Subunit A, Seq Identity:43%, Sec7 domain

UniProt annotation for GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP. Recruitment to cis-Golgi membranes requires membrane association of Arf-GDP and can be regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat complex to the endoplasmic reticulum exit sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi compartments which implicates ARF1 activation. Involved in COPI vesicle-dependent retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmatic reticulum (ER) (PubMed:16926190, PubMed:17956946, PubMed:18003980, PubMed:12047556, PubMed:12808027, PubMed:19039328, PubMed:24213530). Involved in the trans-Golgi network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1 adaptor protein complex related to chlathrin-dependent transport; the function requires its GEF activity (probably at least in part on ARF4 and ARF5) (PubMed:23386609). Has GEF activity towards ARF1 (PubMed:15616190). Has in vitro GEF activity towards ARF5 (By similarity). Involved in the processing of PSAP (PubMed:17666033). Required for the assembly of the Golgi apparatus (PubMed:12808027, PubMed:18003980). The AMPK-phosphorylated form is involved in Golgi disassembly during mitotis and under stress conditions (PubMed:18063581, PubMed:23418352). May be involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid droplets; however, this function is under debate (PubMed:19461073, PubMed:22185782). In neutrophils, involved in G protein-coupled receptor (GPCR)-mediated chemotaxis und superoxide production. Proposed to be recruited by phosphatidylinositol-phosphates generated upon GPCR stimulation to the leading edge where it recruits and activates ARF1, and is involved in recruitment of GIT2 and the NADPH oxidase complex (PubMed:22573891).
UniProt features for GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
CHAIN 1 1859 Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1.

DOMAIN 692 882 SEC7.

REGION 1 380 Interaction with RAB1B.

REGION 1 211 DCB; DCB:DCB domain and DCB:HUS domain interaction.

REGION 530 550 HUS; DCB:HUS domain interaction.

REGION 886 1370 Phosphatidylinositol-phosphate binding; required for translocation to the leading edge and for ARF1 activation upon GPCR signaling.

Amino Acid Sequence for GBF1_HUMAN » Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
MVDKNIYIIQ GEINIVVGAI KRNARWSTHT PLDEERDPLL HSFGHLKEVL NSITELSEIE PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP THEGTAEGME NMADAVTHAR FVGTDPASDE VVLMKILQVL RTLLLTPVGA HLTNESVCEI MQSCFRICFE MRLSELLRKS AEHTLVDMVQ LLFTRLPQFK EEPKNYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM TKVTPGSELP TPNGTTLSSN LTGGMPFIDV PTPISSASSE AASAVVSPST DSGLEFSSQT TSKEDLTDLE QPGSPGYSTA TEPGSSELGV PEQPDLQEGT HVEKSQSASV ESIPEVLEEC TSPADHSDSA SVHDMDYVNP RGVRFTQSSQ KEGTALVPYG LPCIRELFRF LISLTNPHDR HNSEVMIHMG LHLLTVALES APVAQCQTLL GLIKDEMCRH LFQLLSIERL NLYAASLRVC FLLFESMREH LKFQMEMYIK KLMEIITVEN PKMPYEMKEM ALEAIVQLWR IPSFVTELYI NYDCDYYCSN LFEELTKLLS KNAFPVSGQL YTTHLLSLDA LLTVIDSTEA HCQAKVLNSL TQQEKKETAR PSCEIVDGTR EASNTERTAS DGKAVGMASD IPGLHLPGGG RLPPEHGKSG CSDLEEAVDS GADKKFARKP PRFSCLLPDP RELIEIKNKK KLLITGTEQF NQKPKKGIQF LQEKGLLTIP MDNTEVAQWL RENPRLDKKM IGEFVSDRKN IDLLESFVST FSFQGLRLDE ALRLYLEAFR LPGEAPVIQR LLEAFTERWM NCNGSPFANS DACFSLAYAV IMLNTDQHNH NVRKQNAPMT LEEFRKNLKG VNGGKDFEQD ILEDMYHAIK NEEIVMPEEQ TGLVRENYVW NVLLHRGATP EGIFLRVPTA SYDLDLFTMT WGPTIAALSY VFDKSLEETI IQKAISGFRK CAMISAHYGL SDVFDNLIIS LCKFTALSSE SIENLPSVFG SNPKAHIAAK TVFHLAHRHG DILREGWKNI MEAMLQLFRA QLLPKAMIEV EDFVDPNGKI SLQREETPSN RGESTVLSFV SWLTLSGPEQ SSVRGPSTEN QEAKRVALEC IKQCDPEKMI TESKFLQLES LQELMKALVS VTPDEETYDE EDAAFCLEML LRIVLENRDR VGCVWQTVRD HLYHLCVQAQ DFCFLVERAV VGLLRLAIRL LRREEISAQV LLSLRILLLM KPSVLSRVSH QVAYGLHELL KTNAANIHSG DDWATLFTLL ECIGSGVKPP AALQATARAD APDAGAQSDS ELPSYHQNDV SLDRGYTSDS EVYTDHGRPG KIHRSATDAD VVNSGWLVVG KDDVDNSKPG PSRPGPSPLI NQYSLTVGLD LGPHDTKSLL KCVESLSFIV RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQEKRGKSH KYDSKGNRFK KKSKEGSMLR RPRTSSQHAS RGGQSDDDED EGVPASYHTV SLQVSQDLLD LMHTLHTRAA SIYSSWAEEQ RHLETGGQKI EADSRTLWAH CWCPLLQGIA CLCCDARRQV RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL LENISPADVG GMEETRMRAS TLLSKVFLQH LSPLLSLSTF AALWLTILDF MDKYMHAGSS DLLSEAIPES LKNMLLVMDT AEIFHSADAR GGGPSALWEI TWERIDCFLP HLRDELFKQT VIQDPMPMEP QGQKPLASAH LTSAAGDTRT PGHPPPPEIP SELGACDFEK PESPRAASSS SPGSPVASSP SRLSPTPDGP PPLAQPPLIL QPLASPLQVG VPPMTLPIIL NPALIEATSP VPLLATPRPT DPIPTSEVN