ID ARL3_PIG Reviewed; 182 AA.
AC Q52NJ4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=ADP-ribosylation factor-like protein 3;
GN Name=ARL3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y., Xiong Z.Y.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small GTP-binding protein which cycles between an inactive
CC GDP-bound and an active GTP-bound form, and the rate of cycling is
CC regulated by guanine nucleotide exchange factors (GEF) and GTPase-
CC activating proteins (GAP). Required for normal cytokinesis and cilia
CC signaling. Requires assistance from GTPase-activating proteins (GAPs)
CC like RP2 and PDE6D, in order to cycle between inactive GDP-bound and
CC active GTP-bound forms. Required for targeting proteins to the cilium,
CC including myristoylated NPHP3 and prenylated INPP5E. Targets NPHP3 to
CC the ciliary membrane by releasing myristoylated NPHP3 from UNC119B
CC cargo adapter into the cilium (By similarity). Required for PKD1:PKD2
CC complex targeting from the trans-Golgi network to the cilium (By
CC similarity). {ECO:0000250|UniProtKB:P36405,
CC ECO:0000250|UniProtKB:Q9WUL7}.
CC -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2
CC induces hydrolysis of GTP ARL3 in the complex, leading to the release
CC of UNC119 (or UNC119B). Interacts with RP2; interaction is direct and
CC stimulated with the activated GTP-bound form of ARL3. Interacts with
CC SYS1. Interacts with ARL2BP; the GTP-bound form interacts with ARL2BP.
CC Microtubule-associated protein. Does not interact with TBCC (By
CC similarity). Interacts with RP2. Interacts with PDE6D; the interaction
CC occurs specifically with the GTP-bound form of ARL3. Interacts with
CC GGA1; the interaction recruits PKD1:PKD2 complex to trans-Golgi network
CC and is required for ciliary targeting of PKD1:PKD2 complex (By
CC similarity). Interacts with DNAAF9 (By similarity).
CC {ECO:0000250|UniProtKB:P36405, ECO:0000250|UniProtKB:Q9WUL7}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:P36405}. Note=Detected predominantly in
CC the photoreceptor connecting cilium. Centrosome-associated throughout
CC the cell cycle. Not detected to interphase microtubules. Present on the
CC mitotic spindle (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AY996811; AAY17507.1; -; mRNA.
DR RefSeq; NP_001026955.1; NM_001031785.1.
DR AlphaFoldDB; Q52NJ4; -.
DR SMR; Q52NJ4; -.
DR STRING; 9823.ENSSSCP00000073948; -.
DR PaxDb; 9823-ENSSSCP00000011279; -.
DR PeptideAtlas; Q52NJ4; -.
DR Ensembl; ENSSSCT00000054746.3; ENSSSCP00000055492.3; ENSSSCG00000031782.3.
DR Ensembl; ENSSSCT00005029750.1; ENSSSCP00005018110.1; ENSSSCG00005018881.1.
DR Ensembl; ENSSSCT00015026703.1; ENSSSCP00015010450.1; ENSSSCG00015020007.1.
DR Ensembl; ENSSSCT00035109805.1; ENSSSCP00035047724.1; ENSSSCG00035080198.1.
DR Ensembl; ENSSSCT00045031669.1; ENSSSCP00045021928.1; ENSSSCG00045018550.1.
DR Ensembl; ENSSSCT00050062180.1; ENSSSCP00050026707.1; ENSSSCG00050045679.1.
DR Ensembl; ENSSSCT00055007799.1; ENSSSCP00055006164.1; ENSSSCG00055003961.1.
DR Ensembl; ENSSSCT00060034276.1; ENSSSCP00060014678.1; ENSSSCG00060025283.1.
DR Ensembl; ENSSSCT00065006459.1; ENSSSCP00065002872.1; ENSSSCG00065004696.1.
DR Ensembl; ENSSSCT00070022699.1; ENSSSCP00070018769.1; ENSSSCG00070011641.1.
DR GeneID; 595114; -.
DR KEGG; ssc:595114; -.
DR CTD; 403; -.
DR VGNC; VGNC:107366; ARL3.
DR eggNOG; KOG0074; Eukaryota.
DR GeneTree; ENSGT00940000155737; -.
DR InParanoid; Q52NJ4; -.
DR OMA; DGMEWVC; -.
DR OrthoDB; 5349301at2759; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR CDD; cd04155; Arl3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR044612; ARL2/3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR45697; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR45697:SF4; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 3; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell projection; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..182
FT /note="ADP-ribosylation factor-like protein 3"
FT /id="PRO_0000295293"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
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 BINDING 159..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36405"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 182 AA; 20484 MW; 94326391F804B821 CRC64;
MGLLSILRKL KSAPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG FNIKSVQSQG
FKLNVWDIGG QRKIRPYWRN YFENTDILIY VIDSADRKRF EETGQELAEL LEEEKLSCVP
VLIFANKQDL LTAAPASEIA EGLNLHTIRD RVWQIQSCSA LTGEGVQDGM NWVCKNVNAK
KK
//
