ARL16_HUMAN
ID ARL16_HUMAN Reviewed; 197 AA.
AC Q0P5N6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ADP-ribosylation factor-like protein 16 {ECO:0000305};
GN Name=ARL16 {ECO:0000312|HGNC:HGNC:27902};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH DDX58, AND MUTAGENESIS OF
RP THR-37.
RX PubMed=21233210; DOI=10.1074/jbc.m110.206896;
RA Yang Y.K., Qu H., Gao D., Di W., Chen H.W., Guo X., Zhai Z.H., Chen D.Y.;
RT "ARF-like protein 16 (ARL16) inhibits RIG-I by binding with its C-terminal
RT domain in a GTP-dependent manner.";
RL J. Biol. Chem. 286:10568-10580(2011).
CC -!- FUNCTION: May suppress the RNA sensing activity of DDX58 in a GTP-
CC dependent. {ECO:0000269|PubMed:21233210}.
CC -!- SUBUNIT: Interacts with DDX58; this interaction is GTP-dependent and
CC induced upon viral infection; this interaction suppresses the RNA
CC sensing activity of DDX58. {ECO:0000269|PubMed:21233210}.
CC -!- INTERACTION:
CC Q0P5N6; P49418: AMPH; NbExp=7; IntAct=EBI-10186132, EBI-7121510;
CC Q0P5N6; Q92870-2: APBB2; NbExp=3; IntAct=EBI-10186132, EBI-21535880;
CC Q0P5N6; P05067: APP; NbExp=3; IntAct=EBI-10186132, EBI-77613;
CC Q0P5N6; P05067-2: APP; NbExp=3; IntAct=EBI-10186132, EBI-17264467;
CC Q0P5N6; P54253: ATXN1; NbExp=6; IntAct=EBI-10186132, EBI-930964;
CC Q0P5N6; Q05D60: DEUP1; NbExp=3; IntAct=EBI-10186132, EBI-748597;
CC Q0P5N6; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-10186132, EBI-12143817;
CC Q0P5N6; Q08379: GOLGA2; NbExp=7; IntAct=EBI-10186132, EBI-618309;
CC Q0P5N6; P42858: HTT; NbExp=18; IntAct=EBI-10186132, EBI-466029;
CC Q0P5N6; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10186132, EBI-748974;
CC Q0P5N6; O43924: PDE6D; NbExp=13; IntAct=EBI-10186132, EBI-712685;
CC Q0P5N6; Q7Z412: PEX26; NbExp=3; IntAct=EBI-10186132, EBI-752057;
CC Q0P5N6; D3DTS7: PMP22; NbExp=3; IntAct=EBI-10186132, EBI-25882629;
CC Q0P5N6; O60260-5: PRKN; NbExp=6; IntAct=EBI-10186132, EBI-21251460;
CC Q0P5N6; P49810: PSEN2; NbExp=3; IntAct=EBI-10186132, EBI-2010251;
CC Q0P5N6; Q04864-2: REL; NbExp=3; IntAct=EBI-10186132, EBI-10829018;
CC Q0P5N6; P37840: SNCA; NbExp=3; IntAct=EBI-10186132, EBI-985879;
CC Q0P5N6; P00441: SOD1; NbExp=3; IntAct=EBI-10186132, EBI-990792;
CC Q0P5N6; Q13148: TARDBP; NbExp=6; IntAct=EBI-10186132, EBI-372899;
CC Q0P5N6; Q99081-3: TCF12; NbExp=3; IntAct=EBI-10186132, EBI-11952764;
CC Q0P5N6; P15884-3: TCF4; NbExp=3; IntAct=EBI-10186132, EBI-13636688;
CC Q0P5N6; O95292: VAPB; NbExp=3; IntAct=EBI-10186132, EBI-1188298;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21233210}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; BC105078; AAI05079.1; -; mRNA.
DR EMBL; BC105076; AAI05077.1; -; mRNA.
DR RefSeq; NP_001035114.1; NM_001040025.2.
DR RefSeq; NP_001316537.1; NM_001329608.1.
DR AlphaFoldDB; Q0P5N6; -.
DR SMR; Q0P5N6; -.
DR BioGRID; 130847; 15.
DR IntAct; Q0P5N6; 22.
DR MINT; Q0P5N6; -.
DR STRING; 9606.ENSP00000380635; -.
DR iPTMnet; Q0P5N6; -.
DR PhosphoSitePlus; Q0P5N6; -.
DR BioMuta; ARL16; -.
DR DMDM; 119361248; -.
DR EPD; Q0P5N6; -.
DR MassIVE; Q0P5N6; -.
DR PaxDb; Q0P5N6; -.
DR PeptideAtlas; Q0P5N6; -.
DR PRIDE; Q0P5N6; -.
DR ProteomicsDB; 58764; -.
DR DNASU; 339231; -.
DR GeneID; 339231; -.
DR KEGG; hsa:339231; -.
DR UCSC; uc002kbf.4; human.
DR CTD; 339231; -.
DR DisGeNET; 339231; -.
DR GeneCards; ARL16; -.
DR HGNC; HGNC:27902; ARL16.
DR MIM; 619117; gene.
DR neXtProt; NX_Q0P5N6; -.
DR PharmGKB; PA142672583; -.
DR VEuPathDB; HostDB:ENSG00000214087; -.
DR eggNOG; KOG0072; Eukaryota.
DR InParanoid; Q0P5N6; -.
DR OMA; CICLGPK; -.
DR OrthoDB; 1383112at2759; -.
DR PhylomeDB; Q0P5N6; -.
DR TreeFam; TF323823; -.
DR PathwayCommons; Q0P5N6; -.
DR SignaLink; Q0P5N6; -.
DR BioGRID-ORCS; 339231; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; ARL16; human.
DR GenomeRNAi; 339231; -.
DR Pharos; Q0P5N6; Tdark.
DR PRO; PR:Q0P5N6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q0P5N6; protein.
DR Genevisible; Q0P5N6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..197
FT /note="ADP-ribosylation factor-like protein 16"
FT /id="PRO_0000264630"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VARIANT 10
FT /note="S -> R (in dbSNP:rs8066889)"
FT /id="VAR_059129"
FT MUTAGEN 37
FT /note="T->N: Loss of the inhibition of DDX58-mediated
FT antiviral response activity. Loss of GTP binding activity.
FT Loss of interaction with DDX58."
FT /evidence="ECO:0000269|PubMed:21233210"
SQ SEQUENCE 197 AA; 20936 MW; 678AE0CFE6159E7F CRC64;
MRVAGGRALS RGAELRVPGG AKHGMCLLLG ATGVGKTLLV KRLQEVSSRD GKGDLGEPPP
TRPTVGTNLT DIVAQRKITI RELGGCMGPI WSSYYGNCRS LLFVMDASDP TQLSASCVQL
LGLLSAEQLA EASVLILFNK IDLPCYMSTE EMKSLIRLPD IIACAKQNIT TAEISAREGT
GLAGVLAWLQ ATHRAND
