ARL4D_MOUSE
ID ARL4D_MOUSE Reviewed; 201 AA.
AC Q99PE9; Q9CQB1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ADP-ribosylation factor-like protein 4D;
DE AltName: Full=ADP-ribosylation factor-like protein 4L;
DE AltName: Full=ADP-ribosylation factor-like protein 5;
GN Name=Arl4d; Synonyms=Arf4l, Arl5;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=12414990; DOI=10.1242/jcs.00123;
RA Lin C.-Y., Li C.-C., Huang P.-H., Lee F.-J.S.;
RT "A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei
RT and nucleoli, interacts with heterochromatin protein 1.";
RL J. Cell Sci. 115:4433-4445(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
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; the interaction is direct and ARL4D GTP-
CC dependent. Does not interact with ARL4D (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:12414990}. Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AF312686; AAG53667.1; -; mRNA.
DR EMBL; AK004126; BAB23183.1; -; mRNA.
DR EMBL; AK013320; BAB28789.1; -; mRNA.
DR EMBL; AL590994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34064.1; -; Genomic_DNA.
DR EMBL; BC016113; AAH16113.1; -; mRNA.
DR CCDS; CCDS36336.1; -.
DR RefSeq; NP_079680.1; NM_025404.3.
DR AlphaFoldDB; Q99PE9; -.
DR SMR; Q99PE9; -.
DR BioGRID; 219856; 3.
DR MINT; Q99PE9; -.
DR STRING; 10090.ENSMUSP00000035918; -.
DR PhosphoSitePlus; Q99PE9; -.
DR PaxDb; Q99PE9; -.
DR PRIDE; Q99PE9; -.
DR ProteomicsDB; 265104; -.
DR Antibodypedia; 29560; 120 antibodies from 27 providers.
DR DNASU; 80981; -.
DR Ensembl; ENSMUST00000039388; ENSMUSP00000035918; ENSMUSG00000034936.
DR GeneID; 80981; -.
DR KEGG; mmu:80981; -.
DR UCSC; uc007lpq.2; mouse.
DR CTD; 379; -.
DR MGI; MGI:1933155; Arl4d.
DR VEuPathDB; HostDB:ENSMUSG00000034936; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000161341; -.
DR HOGENOM; CLU_040729_9_2_1; -.
DR InParanoid; Q99PE9; -.
DR OMA; PSFQCLH; -.
DR OrthoDB; 1457094at2759; -.
DR PhylomeDB; Q99PE9; -.
DR TreeFam; TF105464; -.
DR BioGRID-ORCS; 80981; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Arl4d; mouse.
DR PRO; PR:Q99PE9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PE9; protein.
DR Bgee; ENSMUSG00000034936; Expressed in decidua and 228 other tissues.
DR Genevisible; Q99PE9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 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 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..201
FT /note="ADP-ribosylation factor-like protein 4D"
FT /id="PRO_0000207465"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
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"
FT CONFLICT 7
FT /note="E -> D (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> I (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="RM -> KV (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="G -> A (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="P -> Q (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="H -> R (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> G (in Ref. 1; AAG53667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22270 MW; A6462A22B3AD451A CRC64;
MGNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI
RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDSAETERLE EARMELHRIS
KASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQPGL
EHLYEMILKR KKAPRSSKKR R
