ARL4A_MOUSE
ID ARL4A_MOUSE Reviewed; 200 AA.
AC P61213; P41275; Q3TGR5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ADP-ribosylation factor-like protein 4A;
GN Name=Arl4a; Synonyms=Arl4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee F.-J.S.;
RT "Cloning and characterization of a mouse ADP-ribosylation factor (ARF)-like
RT 4 gene.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ;
RX PubMed=9761722; DOI=10.1042/bj3350259;
RA Jacobs S., Schuermann A., Becker W., Boeckers T.M., Copeland N.G.,
RA Jenkins N.A., Joost H.-G.;
RT "The mouse ADP-ribosylation factor-like 4 gene: two separate promoters
RT direct specific transcription in tissues and testicular germ cell.";
RL Biochem. J. 335:259-265(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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. {ECO:0000269|PubMed:10980193}.
CC -!- PTM: Myristoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; U76546; AAB18812.1; -; mRNA.
DR EMBL; AK006286; BAB24505.1; -; mRNA.
DR EMBL; AK048606; BAC33388.1; -; mRNA.
DR EMBL; AK168618; BAE40483.1; -; mRNA.
DR EMBL; BC029234; AAH29234.1; -; mRNA.
DR CCDS; CCDS25890.1; -.
DR RefSeq; NP_001034604.1; NM_001039515.1.
DR RefSeq; NP_031513.1; NM_007487.3.
DR AlphaFoldDB; P61213; -.
DR SMR; P61213; -.
DR STRING; 10090.ENSMUSP00000114458; -.
DR PhosphoSitePlus; P61213; -.
DR PaxDb; P61213; -.
DR PRIDE; P61213; -.
DR ProteomicsDB; 265102; -.
DR Antibodypedia; 25147; 202 antibodies from 32 providers.
DR DNASU; 11861; -.
DR Ensembl; ENSMUST00000101472; ENSMUSP00000099013; ENSMUSG00000047446.
DR Ensembl; ENSMUST00000146905; ENSMUSP00000114458; ENSMUSG00000047446.
DR GeneID; 11861; -.
DR KEGG; mmu:11861; -.
DR UCSC; uc007nks.1; mouse.
DR CTD; 10124; -.
DR MGI; MGI:99437; Arl4a.
DR VEuPathDB; HostDB:ENSMUSG00000047446; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000154546; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61213; -.
DR OMA; FEWIAAN; -.
DR OrthoDB; 1457094at2759; -.
DR PhylomeDB; P61213; -.
DR TreeFam; TF105464; -.
DR BioGRID-ORCS; 11861; 0 hits in 74 CRISPR screens.
DR PRO; PR:P61213; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P61213; protein.
DR Bgee; ENSMUSG00000047446; Expressed in seminiferous tubule of testis and 265 other tissues.
DR ExpressionAtlas; P61213; baseline and differential.
DR Genevisible; P61213; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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; TAS:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
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_0000207460"
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
