GBF1_CAEEL
ID GBF1_CAEEL Reviewed; 1975 AA.
AC G5EGS5; H8ESE7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 homolog {ECO:0000312|WormBase:C24H11.7a};
DE Short=BFA-resistant GEF 1;
GN Name=gbf-1 {ECO:0000312|WormBase:C24H11.7a};
GN Synonyms=phi-34 {ECO:0000312|WormBase:C24H11.7a};
GN ORFNames=C24H11.7 {ECO:0000312|WormBase:C24H11.7a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23840591; DOI=10.1371/journal.pone.0067076;
RA Ackema K.B., Sauder U., Solinger J.A., Spang A.;
RT "The ArfGEF GBF-1 Is Required for ER Structure, Secretion and Endocytic
RT Transport in C. elegans.";
RL PLoS ONE 8:e67076-e67076(2013).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25190516; DOI=10.15252/embj.201489039;
RA Ackema K.B., Hench J., Boeckler S., Wang S.C., Sauder U., Mergentaler H.,
RA Westermann B., Bard F., Frank S., Spang A.;
RT "The small GTPase Arf1 modulates mitochondrial morphology and function.";
RL EMBO J. 33:2659-2675(2014).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26115433; DOI=10.1371/journal.pone.0130778;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a Role in
RT Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 10:e0130778-e0130778(2015).
RN [5]
RP ERRATUM.
RX PubMed=27631731; DOI=10.1371/journal.pone.0163398;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Correction: Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a
RT Role in Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 11:e0163398-e0163398(2016).
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 (By similarity). Also, plays a role in
CC receptor-mediated endocytosis in oocytes and endosomal trafficking
CC (PubMed:23840591). Involved in vesicle retrograde transport from the
CC ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER)
CC (PubMed:23840591). Plays a role in maintaining mitochondrial
CC morphology, network organization and function (PubMed:25190516). May be
CC required for the basolateral cell membrane localization of the serine
CC threonine protein kinase sgk-1 in intestinal cells (PubMed:26115433).
CC {ECO:0000250|UniProtKB:Q92538, ECO:0000269|PubMed:23840591,
CC ECO:0000269|PubMed:25190516, ECO:0000269|PubMed:26115433}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:23840591}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:23840591}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C24H11.7a};
CC IsoId=G5EGS5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C24H11.7b};
CC IsoId=G5EGS5-2; Sequence=VSP_060671;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 larval stage
CC causes cuticle rupture, mostly through the vulva, and results in
CC lethality in 50 to 80% of animals upon reaching adulthood
CC (PubMed:23840591). Most surviving animals that reach adulthood are
CC sterile due to embryonic lethality, and in over 90% of surviving
CC animals there is an accumulation of vacuole-like structures in the body
CC cavity (PubMed:23840591). The few larvae that hatch have severe cuticle
CC formation abnormalities (PubMed:23840591). RNAi-mediated knockdown at
CC the L2 or L3 larval stage, results in reduced lethality in response to
CC oxidative stress induced by paraquat compared to wild-type
CC (PubMed:25190516). RNAi-mediated knockdown at the L2 or L3 larval
CC stage, results in enlarged mitochondria which are interconnected by
CC thin membrane tubes in maturing oocytes (PubMed:25190516). RNAi-
CC mediated knockdown at the L4 larval stage, results in impaired body
CC bend movements, and disorganization of the mitochondrial network and
CC increased connections between mitochondria in body wall muscle cells
CC (PubMed:25190516). RNAi-mediated knockdown at the L3 or L4 larval
CC stage, results in the normal production and fertilization of oocytes,
CC but 60 to 70% of the fertilized oocytes are embryonic lethal
CC (PubMed:23840591). Arrested eggs from these animals have disintegrated
CC egg shells, which results in a mass of cells and membranes in the gonad
CC (PubMed:23840591). While 30% of fertilized oocytes display defects in
CC meiosis, with the extrusion of the second polar body during anaphase II
CC often failing (PubMed:23840591). Furthermore, 30% of fertilized oocytes
CC have cytokinesis defects (PubMed:23840591). RNAi-mediated knockdown at
CC the L3 or L4 larval stage, results in defects in Golgi apparatus
CC organization with small Golgi apparatus foci aggregating in large
CC structures around the nuclear membrane and cell periphery in oocytes,
CC and small vesicles accumulating at the endoplasmic reticulum-Golgi
CC interface (PubMed:23840591). RNAi-mediated knockdown at the L3 or L4
CC larval stage, results in endoplasmic reticulum morphology defects with
CC the absence of endoplasmic reticulum lumen in oocytes
CC (PubMed:23840591). RNAi-mediated knockdown at the L3 or L4 larval
CC stage, results in defective cav-1 transport from the Golgi apparatus to
CC the plasma membrane in oocytes, and an accumulation of the yolk protein
CC vit-2 in intestinal cells and in the body cavity (PubMed:23840591).
CC RNAi-mediated knockdown at the L3 or L4 larval stage also results in
CC defects in the endosomal pathway with reduced expression of the early
CC endosomal protein rab-5 in the intestine (PubMed:23840591). RNAi-
CC mediated knockdown results in the mis-localization of the serine
CC threonine protein kinase sgk-1 in intestinal cells (PubMed:26115433).
CC {ECO:0000269|PubMed:23840591, ECO:0000269|PubMed:25190516,
CC ECO:0000269|PubMed:26115433}.
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DR EMBL; BX284603; CAB03915.3; -; Genomic_DNA.
DR EMBL; BX284603; CCG28191.1; -; Genomic_DNA.
DR RefSeq; NP_001255139.1; NM_001268210.1.
DR RefSeq; NP_001255140.1; NM_001268211.1.
DR AlphaFoldDB; G5EGS5; -.
DR SMR; G5EGS5; -.
DR STRING; 6239.C24H11.7a; -.
DR EPD; G5EGS5; -.
DR PaxDb; G5EGS5; -.
DR PeptideAtlas; G5EGS5; -.
DR EnsemblMetazoa; C24H11.7a.1; C24H11.7a.1; WBGene00007703. [G5EGS5-1]
DR EnsemblMetazoa; C24H11.7b.1; C24H11.7b.1; WBGene00007703. [G5EGS5-2]
DR WormBase; C24H11.7a; CE44078; WBGene00007703; gbf-1. [G5EGS5-1]
DR WormBase; C24H11.7b; CE47290; WBGene00007703; gbf-1. [G5EGS5-2]
DR eggNOG; KOG0928; Eukaryota.
DR GeneTree; ENSGT00940000168092; -.
DR HOGENOM; CLU_001204_2_0_1; -.
DR InParanoid; G5EGS5; -.
DR OMA; AITHCRF; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; G5EGS5; -.
DR Reactome; R-CEL-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:G5EGS5; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00007703; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EGS5; baseline and differential.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:WormBase.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:WormBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:WormBase.
DR GO; GO:0016197; P:endosomal transport; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0046903; P:secretion; IMP:WormBase.
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 3: Inferred from homology;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus;
KW Reference proteome; Transport.
FT CHAIN 1..1975
FT /note="Golgi-specific brefeldin A-resistance guanine
FT nucleotide exchange factor 1 homolog"
FT /id="PRO_0000450677"
FT DOMAIN 624..812
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 216..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1490
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060671"
SQ SEQUENCE 1975 AA; 219532 MW; FC2976D59506BE79 CRC64;
MATNGVYIVM GEANCVVALL NKARRQYQLS QVPTLEDTDP LLRNFTDLKE VLNEVADLAD
MNPQTYLSPF LDVIKAQNTN GPITEAALAA VAKFLNYGLI DASSIKAANA VESIAYAVVH
TKFIGGKSTG SDECVLFKIL QVLRSLLLSP PGILLSNEAV CDMMQSCFRI VFEQNLSLLL
RKAAESTLAD MTQLIFTRLP TFVEDTRHPY IRQLVNPTEK RQKRKKKRQL SVHIETKAKE
PENVPTEMTK LIGEAAETAE TDGAANLGYD VVLTTDPPVD TVTHPDPPIE EIIKLAEPIS
AGDEADSESE GGGGEEHHER PPVRAHAGLQ REIVSDEEEI DTEQTVGGEE KMPYGLPCCR
ELLRFLITMT NPVDRHNTES MVILGLNLLI VALEAIADFL PNYDILMPLI KNELCRNLLQ
LLDTNRLPVL AATNRCCFLL FESMRMHMKF QLESYLKKLQ SIVLTEEKQH ENGGGGTEQK
EMALESLVQL WRIPGLVTEM YLNFDCDLYC GNIFEDLTKL LVENSFPTVG GHTASLLSLD
ALLVVIETIE QNCEDRENGR GEVAKEQEHK DLKKLGLPVL SGYDLAKKMA ISTGGKASPM
PVSSSIVLRS NRHAPSTELP SMSQIIEQKK RKRLIAEGTE LFNQSPKKGI AFLREKGILG
HDEQSLVQWL RTNPQLDKKA IADYICNRKH AEVLNAFVKS FPFENTRLDV ALRMFLETFR
LPGESAEIAL VMQHFSEEWF RANNEPFFHV DAAFTLSYAI IMLNVDQHNP QAKRSQPPMT
VDCFRRNLSG TNDSRDFDPE MLADMYQAIK TEEIVMPAEQ KGTVKEDYMW KVLLRRGETA
EGSFYHAPTG WNDHDLFAVC WGPAVAALSY VFDKSEHEQI LQKALTGYRK CAKIAAYYGM
KEVFDNLCIH LCKFTTLTSM RDGGAGGGAD EDVDLSAAAL LSHSSSPEAV ALAFGENHKA
QLATRTLFYL VHENGNILRE GWRNLFEALL QLFRARLLPA ELTEVEDYVD EKGWVNIQRV
HQKELPHTRN DSGLLSWFGL GGGASEADRR KPTQEQLSSM KLASQVISEC RPSQIVADSK
YLTSTSLAEL LSSIAANSAQ IVEQAEPQQK TASLSGEDED ALVFYLELIV AITLENKDRL
PLVWPHVRRH LEWLLSPRFG RCPVLVERAV VGLLRVANRN LFRDNTVSDD VLHSLSMLLR
LSPKALFIFS RQIAFGLYEL IRANAANVHK KEHWAVLFAL LEAAGAAVLP DDYVMMTTTE
KQQQSLRVGG DQQQQRMAYS DVEGASGRGG GAHEERAYTS EGEERRRGGY DSNSDLESRV
DSAGSLLGAQ KQPADWIHLD HKDAAKATEE ALTALGANVV SSKKNFRQFG SLVLRNGLGR
HEPAAFLKVC ECLAFLLRDA VHVTPDNFES SLQCLRTMVE ASLDGGVYAA GPLSGDAQNR
LRSNVTDEKA VKKHHHHHHG HKKKELCTDV TEDADESRNE EQQLIGNYQQ MSLHLLDLCS
QLHSQTPAIF AKWAQGASPA ASDLATVAFI WTDIWRPLLQ AIGRLSCDCR RGVRAAALTH
LQRAFLPANM ATLGAAEWQS CFGEVLFPLL TKLLEPFSQM DPIGMEDTRV RTLQIVAKTL
LNHLSALSAL DSFPDLWMLL LDYMEQYLRV DSCGNLNEAV PESLKNMLLV MDSTGIFAAT
PRLYDVTVER LNKFMPELIK DTIPNPPRPG QQQSEASEPK KEHASGLEPP PPSSNSTAAT
STSDPSIATA QSSISTASSV VGPLVTCPED AGISAPIPIQ HPLTEVIVHS GPTSPIGSPP
QTEPPASSPP QHQHSEHQQY EQYRQQQAAA AQQYQQYNQN YPQQQQQQQQ QYAYSPEHAA
YYQQQYAHQQ QQYAEHYANQ YQHYQQQQQQ QQQHPVNPTS PSVHGQYSVA NPLPLPAHPA
YHPIVAPSVN SAFTHVYTPP QNNAPALAPS APTTTSADSP YFTPIPYNPS QQEKP
