ARL1_BOVIN
ID ARL1_BOVIN Reviewed; 181 AA.
AC Q2YDM1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ADP-ribosylation factor-like protein 1;
GN Name=ARL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTP-binding protein. Can activate phospholipase D with very
CC low efficiency. Important for normal function of the Golgi apparatus
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The GTP-bound form interacts with GOLGA1, GOLGA4 and RGPD8.
CC The GTP-bound form directly interacts with ARFIP2; this interaction
CC leads to an increase in the amount of bound GTP at steady state level.
CC Binds to SCOC, preferentially in its GTP-bound form. May interact with
CC UNC119 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P40616}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P40616}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; BC110156; AAI10157.1; -; mRNA.
DR RefSeq; NP_001039694.1; NM_001046229.2.
DR AlphaFoldDB; Q2YDM1; -.
DR SMR; Q2YDM1; -.
DR STRING; 9913.ENSBTAP00000015767; -.
DR PaxDb; Q2YDM1; -.
DR PRIDE; Q2YDM1; -.
DR Ensembl; ENSBTAT00000015767; ENSBTAP00000015767; ENSBTAG00000011883.
DR GeneID; 517345; -.
DR KEGG; bta:517345; -.
DR CTD; 400; -.
DR VEuPathDB; HostDB:ENSBTAG00000011883; -.
DR VGNC; VGNC:26135; ARL1.
DR eggNOG; KOG0072; Eukaryota.
DR GeneTree; ENSGT00940000155118; -.
DR HOGENOM; CLU_040729_9_4_1; -.
DR InParanoid; Q2YDM1; -.
DR OMA; QEGMDWL; -.
DR OrthoDB; 1271528at2759; -.
DR TreeFam; TF105461; -.
DR Reactome; R-BTA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011883; Expressed in saliva-secreting gland and 108 other tissues.
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; ISS:UniProtKB.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
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 Gene3D; 3.40.50.300; -; 1.
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 Golgi apparatus; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW 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_0000245352"
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 45..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 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P40616"
SQ SEQUENCE 181 AA; 20428 MW; BB2736C8ED632FF2 CRC64;
MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN
LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI
LVVFANKQDM EQAMTPSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR
Q
