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   03-AUG-2022, entry version 189.
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}.
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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; 61.
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; P49703; -.
DR   PeptideAtlas; P49703; -.
DR   PRIDE; P49703; -.
DR   ProteomicsDB; 56052; -.
DR   Antibodypedia; 29560; 120 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   CTD; 379; -.
DR   DisGeNET; 379; -.
DR   GeneCards; ARL4D; -.
DR   HGNC; HGNC:656; ARL4D.
DR   HPA; ENSG00000175906; Tissue enhanced (retina).
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; PSFQCLH; -.
DR   OrthoDB; 1457094at2759; -.
DR   PhylomeDB; P49703; -.
DR   TreeFam; TF105464; -.
DR   PathwayCommons; P49703; -.
DR   SignaLink; P49703; -.
DR   BioGRID-ORCS; 379; 135 hits in 1069 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 182 other tissues.
DR   Genevisible; P49703; HS.
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; IBA:GO_Central.
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; -; 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   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