ARF12_CAEEL
ID ARF12_CAEEL Reviewed; 181 AA.
AC Q10943;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ADP-ribosylation factor 1-like 2;
DE AltName: Full=ADP-ribosylation factor-related protein 1.2;
GN Name=arf-1.2 {ECO:0000312|WormBase:B0336.2};
GN Synonyms=arf-1 {ECO:0000312|WormBase:B0336.2};
GN ORFNames=B0336.2 {ECO:0000312|WormBase:B0336.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15576487; DOI=10.1096/fj.04-2273com;
RA Li Y., Kelly W.G., Logsdon J.M. Jr., Schurko A.M., Harfe B.D.,
RA Hill-Harfe K.L., Kahn R.A.;
RT "Functional genomic analysis of the ADP-ribosylation factor family of
RT GTPases: phylogeny among diverse eukaryotes and function in C. elegans.";
RL FASEB J. 18:1834-1850(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15716356; DOI=10.1091/mbc.e04-08-0726;
RA Poteryaev D., Squirrell J.M., Campbell J.M., White J.G., Spang A.;
RT "Involvement of the actin cytoskeleton and homotypic membrane fusion in ER
RT dynamics in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:2139-2153(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21596567; DOI=10.1016/j.cub.2011.04.025;
RA Singhvi A., Teuliere J., Talavera K., Cordes S., Ou G., Vale R.D.,
RA Prasad B.C., Clark S.G., Garriga G.;
RT "The Arf GAP CNT-2 regulates the apoptotic fate in C. elegans asymmetric
RT neuroblast divisions.";
RL Curr. Biol. 21:948-954(2011).
RN [5]
RP FUNCTION.
RX PubMed=22801495; DOI=10.1038/nature11240;
RA Denning D.P., Hatch V., Horvitz H.R.;
RT "Programmed elimination of cells by caspase-independent cell extrusion in
RT C. elegans.";
RL Nature 488:226-230(2012).
RN [6]
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).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC Involved in endoplasmic reticulum dynamics during embryogenesis
CC (PubMed:15716356). Also required for adult germline function
CC (PubMed:15576487). Plays a role in cell shedding during embryogenesis
CC probably by promoting the endocytosis of cell adhesion molecules
CC (PubMed:22801495). During neurogenesis, involved in cell autonomous Q.p
CC neuroblast asymmetric divisions that generate one precursor cell and
CC one apoptotic cell, probably by controlling endocytosis
CC (PubMed:21596567). Plays a role in maintaining mitochondrial morphology
CC (PubMed:25190516). {ECO:0000269|PubMed:15576487,
CC ECO:0000269|PubMed:15716356, ECO:0000269|PubMed:21596567,
CC ECO:0000269|PubMed:25190516, ECO:0000305|PubMed:22801495}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis, intestine, spermatheca,
CC uterus, gonadal sheath, vulva cells, pharynx muscle, body wall muscle,
CC head neurons, ventral nerve cord. {ECO:0000269|PubMed:15576487}.
CC -!- DEVELOPMENTAL STAGE: First detected in very young embryos with as
CC little as 48-64 cells. {ECO:0000269|PubMed:15576487}.
CC -!- DISRUPTION PHENOTYPE: Death during embryogenesis (PubMed:15716356).
CC Some muscle differentiation occurs although it is poorly organized and
CC little elongation or morphogenesis is evident (PubMed:15716356). Extra
CC A/PVM neurons are produced from the precursor Q.pp, which is normally
CC fated to die, acquiring the fate of its sister Q.pa (PubMed:21596567).
CC Q.pa and Q.pp have almost similar size caused by a loss of Q.p
CC asymmetric cell division (PubMed:21596567). In oocytes, plasma membrane
CC localization of rme-2 is impaired resulting in the loss of vit-2 uptake
CC which accumulates in the pseudocoelom (PubMed:21596567). RNAi-mediated
CC knockdown results in a hyper-connected mitochondrial network in body
CC wall muscle cells (PubMed:25190516). {ECO:0000269|PubMed:15716356,
CC ECO:0000269|PubMed:21596567, ECO:0000269|PubMed:25190516}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD61516.1; -; Genomic_DNA.
DR PIR; T15341; T15341.
DR RefSeq; NP_498235.1; NM_065834.3.
DR AlphaFoldDB; Q10943; -.
DR SMR; Q10943; -.
DR BioGRID; 41027; 18.
DR DIP; DIP-24528N; -.
DR IntAct; Q10943; 3.
DR STRING; 6239.B0336.2.1; -.
DR EPD; Q10943; -.
DR PaxDb; Q10943; -.
DR PeptideAtlas; Q10943; -.
DR PRIDE; Q10943; -.
DR EnsemblMetazoa; B0336.2.1; B0336.2.1; WBGene00000182.
DR EnsemblMetazoa; B0336.2.2; B0336.2.2; WBGene00000182.
DR UCSC; B0336.2.1; c. elegans.
DR WormBase; B0336.2; CE00696; WBGene00000182; arf-1.2.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; Q10943; -.
DR OMA; VEYRNIQ; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; Q10943; -.
DR Reactome; R-CEL-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q10943; -.
DR PRO; PR:Q10943; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000182; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0048599; P:oocyte development; IMP:WormBase.
DR GO; GO:1904748; P:regulation of apoptotic process involved in development; IGI:UniProtKB.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IGI:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 2: Evidence at transcript level;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1-like 2"
FT /id="PRO_0000207405"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 181 AA; 20522 MW; 98FD0886AD9A2459 CRC64;
MGNVFGSLFK GLFGKREMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV GEAREELMRM LAEDELRDAV
LLVFANKQDL PQAMNAAEVT DKLGLHSLRN RSWYIQATCA TSGDGLYEGL DWLSNQLKNR
S
