ID ARL1_RAT Reviewed; 181 AA.
AC P61212; P41276;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=ADP-ribosylation factor-like protein 1;
GN Name=Arl1; Synonyms=Arf7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RX PubMed=8195219; DOI=10.1016/s0021-9258(17)40735-6;
RA Schuermann A., Breiner M., Becker W., Huppertz C., Kaninulainen H.,
RA Kentrup H., Joost H.-G.;
RT "Cloning of two novel ADP-ribosylation factor-like proteins and
RT characterization of their differential expression in 3T3-L1 cells.";
RL J. Biol. Chem. 269:15683-15688(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Lowe S.L., Hong W.J.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP FUNCTION, AND MUTAGENESIS OF GLY-2; THR-31 AND GLN-71.
RX PubMed=11792819; DOI=10.1242/jcs.114.24.4543;
RA Lu L., Horstmann H., Ng C., Hong W.;
RT "Regulation of Golgi structure and function by ARF-like protein 1 (Arl1).";
RL J. Cell Sci. 114:4543-4555(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA1 AND GOLGA4.
RX PubMed=12972563; DOI=10.1091/mbc.e03-01-0864;
RA Lu L., Hong W.;
RT "Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97
RT and Golgin-245/p230 onto the Golgi.";
RL Mol. Biol. Cell 14:3767-3781(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 16-180 IN COMPLEX WITH GDPNP;
RP MAGNESIUM AND GOLGA4.
RX PubMed=14718928; DOI=10.1038/nsmb714;
RA Wu M., Lu L., Hong W., Song H.;
RT "Structural basis for recruitment of GRIP domain golgin-245 by small GTPase
RT Arl1.";
RL Nat. Struct. Mol. Biol. 11:86-94(2004).
CC -!- FUNCTION: GTP-binding protein. Can activate phospholipase D with very
CC low efficiency (By similarity). Important for normal function of the
CC Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:11792819,
CC ECO:0000269|PubMed:12972563}.
CC -!- SUBUNIT: The GTP-bound form interacts with RGPD8 (By similarity). The
CC GTP-bound form directly interacts with ARFIP2; this interaction leads
CC to an increase in the amount of bound GTP at steady state level (By
CC similarity). Binds to SCOC, preferentially in its GTP-bound form. May
CC interact with UNC119 (By similarity). The GTP-bound form interacts with
CC GOLGA1 and GOLGA4. {ECO:0000250, ECO:0000269|PubMed:12972563,
CC ECO:0000269|PubMed:14718928}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12972563}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12972563}; Cytoplasmic side
CC {ECO:0000269|PubMed:12972563}. Membrane {ECO:0000250|UniProtKB:P40616};
CC Lipid-anchor {ECO:0000250|UniProtKB:P40616}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; X76920; CAA54245.1; -; mRNA.
DR EMBL; U12402; AAA20668.1; -; mRNA.
DR EMBL; BC061553; AAH61553.1; -; mRNA.
DR PIR; A54022; A54022.
DR RefSeq; NP_071780.1; NM_022385.3.
DR PDB; 1R4A; X-ray; 2.30 A; A/B/C/D=16-180.
DR PDBsum; 1R4A; -.
DR AlphaFoldDB; P61212; -.
DR SMR; P61212; -.
DR IntAct; P61212; 2.
DR STRING; 10116.ENSRNOP00000007623; -.
DR iPTMnet; P61212; -.
DR PhosphoSitePlus; P61212; -.
DR jPOST; P61212; -.
DR PaxDb; 10116-ENSRNOP00000007623; -.
DR PeptideAtlas; P61212; -.
DR GeneID; 64187; -.
DR KEGG; rno:64187; -.
DR UCSC; RGD:621326; rat.
DR AGR; RGD:621326; -.
DR CTD; 400; -.
DR RGD; 621326; Arl1.
DR VEuPathDB; HostDB:ENSRNOG00000005763; -.
DR eggNOG; KOG0072; Eukaryota.
DR HOGENOM; CLU_040729_9_4_1; -.
DR InParanoid; P61212; -.
DR OrthoDB; 5474610at2759; -.
DR PhylomeDB; P61212; -.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR EvolutionaryTrace; P61212; -.
DR PRO; PR:P61212; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005763; Expressed in stomach and 20 other cell types or tissues.
DR Genevisible; P61212; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0008047; F:enzyme activator activity; 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:1990583; F:phospholipase D activator activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; IMP:RGD.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0009404; P:toxin metabolic process; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04151; Arl1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR PANTHER; PTHR11711:SF41; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 1; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; GTP-binding; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40616"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor-like protein 1"
FT /id="PRO_0000207452"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14718928"
FT BINDING 45..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14718928"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14718928"
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 BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P40616"
FT MUTAGEN 2
FT /note="G->A: Abolishes association with the Golgi
FT apparatus."
FT /evidence="ECO:0000269|PubMed:11792819"
FT MUTAGEN 31
FT /note="T->N: Accumulation of GDP-bound form."
FT /evidence="ECO:0000269|PubMed:11792819"
FT MUTAGEN 71
FT /note="Q->L: Accumulation of GTP-bound form."
FT /evidence="ECO:0000269|PubMed:11792819"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1R4A"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1R4A"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1R4A"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1R4A"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1R4A"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1R4A"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1R4A"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:1R4A"
SQ SEQUENCE 181 AA; 20412 MW; 3DFC4CC8ED632FEB CRC64;
MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN
LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI
LVVFANKQDM EQAMTPSEMA NALGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR
Q
//
