ID ARL4D_HUMAN Reviewed; 201 AA. AC P49703; B2RC59; D3DX43; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=ADP-ribosylation factor-like protein 4D; DE AltName: Full=ADP-ribosylation factor-like protein 4L; GN Name=ARL4D; Synonyms=ARF4L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-91. RC TISSUE=Retina; RX PubMed=7590735; DOI=10.1006/geno.1995.1115; RA Smith S.A., Holik P.R., Stevens J., Melis R., White R., Albertsen H.; RT "Isolation and mapping of a gene encoding a novel human ADP-ribosylation RT factor on chromosome 17q12-q21."; RL Genomics 28:113-115(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=7581362; DOI=10.1093/hmg/4.8.1259; RA Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., RA Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., RA Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S., RA Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., RA Shattuck-Eidens D., Kamb A.; RT "Comparison of the positional cloning methods used to isolate the BRCA1 RT gene."; RL Hum. Mol. Genet. 4:1259-1266(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Tuda N., Shichijo S., Itoh K.; RT "Two brain-related proteins are a tumor-rejection antigen recognized by RT HLA-A2-restriction."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [7] RP LACK OF INTERACTION WITH ARL4D. RX PubMed=10831612; DOI=10.1083/jcb.149.5.1087; RA Bhamidipati A., Lewis S.A., Cowan N.J.; RT "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of RT tubulin-folding cofactor D with native tubulin."; RL J. Cell Biol. 149:1087-1096(2000). RN [8] RP FUNCTION, INTERACTION WITH CYTH2, AND SUBCELLULAR LOCATION. RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007; RA Hofmann I., Thompson A., Sanderson C.M., Munro S.; RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6 RT exchange factors to the plasma membrane."; RL Curr. Biol. 17:711-716(2007). 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 {ECO:0000269|PubMed:17398095}. CC -!- SUBUNIT: Interacts with CYTH2; the interaction is direct and ARL4D GTP- CC dependent. Does not interact with ARL4D. {ECO:0000269|PubMed:17398095}. CC -!- INTERACTION: CC P49703; Q68D86: CCDC102B; NbExp=4; IntAct=EBI-711726, EBI-10171570; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cell membrane CC {ECO:0000269|PubMed:17398095}. Nucleus {ECO:0000269|PubMed:17398095}. CC Cytoplasm {ECO:0000269|PubMed:17398095}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L38490; AAA57126.1; -; mRNA. DR EMBL; U25771; AAA93229.1; -; mRNA. DR EMBL; AB060692; BAB91080.1; -; mRNA. DR EMBL; AK314951; BAG37456.1; -; mRNA. DR EMBL; CH471178; EAW51681.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51682.1; -; Genomic_DNA. DR EMBL; BC000043; AAH00043.1; -; mRNA. DR CCDS; CCDS11463.1; -. DR PIR; A57646; A57646. DR RefSeq; NP_001652.2; NM_001661.3. DR RefSeq; XP_011523084.1; XM_011524782.2. DR AlphaFoldDB; P49703; -. DR SMR; P49703; -. DR BioGRID; 106874; 150. DR IntAct; P49703; 20. DR MINT; P49703; -. DR STRING; 9606.ENSP00000322628; -. DR iPTMnet; P49703; -. DR PhosphoSitePlus; P49703; -. DR BioMuta; ARL4D; -. DR DMDM; 116241256; -. DR EPD; P49703; -. DR jPOST; P49703; -. DR MassIVE; P49703; -. DR PaxDb; 9606-ENSP00000322628; -. DR PeptideAtlas; P49703; -. DR Antibodypedia; 29560; 135 antibodies from 27 providers. DR DNASU; 379; -. DR Ensembl; ENST00000320033.5; ENSP00000322628.2; ENSG00000175906.5. DR GeneID; 379; -. DR KEGG; hsa:379; -. DR MANE-Select; ENST00000320033.5; ENSP00000322628.2; NM_001661.4; NP_001652.2. DR UCSC; uc002idt.4; human. DR AGR; HGNC:656; -. DR CTD; 379; -. DR DisGeNET; 379; -. DR GeneCards; ARL4D; -. DR HGNC; HGNC:656; ARL4D. DR HPA; ENSG00000175906; Low tissue specificity. DR MIM; 600732; gene. DR neXtProt; NX_P49703; -. DR OpenTargets; ENSG00000175906; -. DR PharmGKB; PA24938; -. DR VEuPathDB; HostDB:ENSG00000175906; -. DR eggNOG; KOG0070; Eukaryota. DR GeneTree; ENSGT00940000161341; -. DR HOGENOM; CLU_040729_9_2_1; -. DR InParanoid; P49703; -. DR OMA; YTLHHVQ; -. DR OrthoDB; 5349301at2759; -. DR PhylomeDB; P49703; -. DR TreeFam; TF105464; -. DR PathwayCommons; P49703; -. DR SignaLink; P49703; -. DR BioGRID-ORCS; 379; 138 hits in 1146 CRISPR screens. DR ChiTaRS; ARL4D; human. DR GeneWiki; ARL4D; -. DR GenomeRNAi; 379; -. DR Pharos; P49703; Tbio. DR PRO; PR:P49703; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P49703; Protein. DR Bgee; ENSG00000175906; Expressed in pharyngeal mucosa and 184 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0009306; P:protein secretion; TAS:ProtInc. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. 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:SF137; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 4D; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. DR Genevisible; P49703; HS. PE 1: Evidence at protein 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_0000207464" 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 VARIANT 91 FT /note="T -> N (in dbSNP:rs1059968)" FT /evidence="ECO:0000269|PubMed:7590735" FT /id="VAR_028205" SQ SEQUENCE 201 AA; 22156 MW; 18766BCF56A8127D CRC64; MGNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDAAEAERLE EAKVELHRIS RASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQQGL ERLYEMILKR KKAARGGKKR R //