ARL4A_RAT
ID ARL4A_RAT Reviewed; 200 AA.
AC P61214; P41275;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ADP-ribosylation factor-like protein 4A;
GN Name=Arl4a; Synonyms=Arl4;
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 [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=10980193; DOI=10.1074/jbc.m002470200;
RA Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C.,
RA Patton W.A., Massenburg D., Moss J., Lee F.J.;
RT "ARL4, an ARF-like protein that is developmentally regulated and localized
RT to nuclei and nucleoli.";
RL J. Biol. Chem. 275:37815-37823(2000).
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). GTP-binding protein that does not act as an
CC allosteric activator of the cholera toxin catalytic subunit. Recruits
CC CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CYTH2. Interacts with KPNA2; the interaction is
CC direct. Does not interacts with ARL4A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localization in
CC the nucleolus is dependent by nucleotide binding. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis and liver. Expressed
CC slightly in heart, spleen, lung and kidney.
CC {ECO:0000269|PubMed:10980193}.
CC -!- DEVELOPMENTAL STAGE: Expressed strongly in embryo at 7 dpc. Expressed
CC slightly in embryo at 11, 15 and 17 dpc.
CC -!- PTM: Myristoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; X77235; CAA54452.1; -; mRNA.
DR EMBL; BC088148; AAH88148.1; -; mRNA.
DR PIR; B54022; B54022.
DR RefSeq; NP_062059.1; NM_019186.1.
DR RefSeq; XP_006240113.1; XM_006240051.2.
DR RefSeq; XP_006240114.1; XM_006240052.3.
DR AlphaFoldDB; P61214; -.
DR SMR; P61214; -.
DR STRING; 10116.ENSRNOP00000005800; -.
DR PhosphoSitePlus; P61214; -.
DR PaxDb; P61214; -.
DR Ensembl; ENSRNOT00000108440; ENSRNOP00000084810; ENSRNOG00000069300.
DR Ensembl; ENSRNOT00000118685; ENSRNOP00000089325; ENSRNOG00000069300.
DR GeneID; 29308; -.
DR KEGG; rno:29308; -.
DR UCSC; RGD:2152; rat.
DR CTD; 10124; -.
DR RGD; 2152; Arl4a.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000154546; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61214; -.
DR OMA; FEWIAAN; -.
DR OrthoDB; 1457094at2759; -.
DR PhylomeDB; P61214; -.
DR TreeFam; TF105464; -.
DR PRO; PR:P61214; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004282; Expressed in testis and 20 other tissues.
DR Genevisible; P61214; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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 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 Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..200
FT /note="ADP-ribosylation factor-like protein 4A"
FT /id="PRO_0000207461"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
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 200 AA; 22588 MW; 8D82542D0F5CEA22 CRC64;
MGNGLSDQTS ILSSLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK
VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR
ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE
KLHDMIIKRR KMLRQQKKKR
