ARL1_HUMAN
ID ARL1_HUMAN Reviewed; 181 AA.
AC P40616; B4DWW1; P80417; Q53XB1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=ADP-ribosylation factor-like protein 1;
GN Name=ARL1;
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] (ISOFORM 1).
RC TISSUE=Umbilical vein endothelial cell;
RA Rosenwald A.G., Kahn R.A.;
RL Submitted (JAN-1995) to UniProtKB.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7814376; DOI=10.1074/jbc.270.1.21;
RA Zhang G.-F., Patton W.A., Lee F.-J.S., Liyange M., Han J.-S., Rhee S.G.,
RA Moss J., Vaughan M.;
RT "Different ARF domains are required for the activation of cholera toxin and
RT phospholipase D.";
RL J. Biol. Chem. 270:21-24(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9624189; DOI=10.1074/jbc.273.25.15872;
RA Hong J.-X., Lee F.-J.S., Patton W.A., Lin C.Y., Moss J., Vaughan M.;
RT "Phospholipid- and GTP-dependent activation of cholera toxin and
RT phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1).";
RL J. Biol. Chem. 273:15872-15876(1998).
RN [11]
RP INTERACTION WITH ARFIP2; GOLGA4; RGPD8; SCOC AND UNC119, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLN-71.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, INTERACTION WITH ARFIP1 AND ARFIP2, MUTAGENESIS OF THR-31, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21239483; DOI=10.1074/jbc.m110.201442;
RA Man Z., Kondo Y., Koga H., Umino H., Nakayama K., Shin H.W.;
RT "Arfaptins are localized to the trans-Golgi by interaction with Arl1, but
RT not Arfs.";
RL J. Biol. Chem. 286:11569-11578(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH ARFIP1.
RX PubMed=22981988; DOI=10.1016/j.devcel.2012.07.019;
RA Gehart H., Goginashvili A., Beck R., Morvan J., Erbs E., Formentini I.,
RA De Matteis M.A., Schwab Y., Wieland F.T., Ricci R.;
RT "The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at
RT the trans-Golgi network.";
RL Dev. Cell 23:756-768(2012).
RN [15]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-181 IN COMPLEX WITH MAGNESIUM;
RP GTP AND GOLGA4.
RX PubMed=14580338; DOI=10.1016/s1097-2765(03)00356-3;
RA Panic B., Perisic O., Veprintsev D.B., Williams R.L., Munro S.;
RT "Structural basis for Arl1-dependent targeting of homodimeric GRIP domains
RT to the Golgi apparatus.";
RL Mol. Cell 12:863-874(2003).
RN [18] {ECO:0007744|PDB:5J5C}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 16-181, INTERACTION WITH ARFGEF1,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27436755; DOI=10.1093/jmcb/mjw033;
RA Wang R., Wang Z., Wang K., Zhang T., Ding J.;
RT "Structural basis for targeting BIG1 to Golgi apparatus through interaction
RT of its DCB domain with Arl1.";
RL J. Mol. Cell Biol. 8:459-461(2016).
RN [19] {ECO:0007744|PDB:4DCN}
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 14-179, INTERACTION WITH ARFIP2,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=22679020; DOI=10.1074/jbc.m112.365783;
RA Nakamura K., Man Z., Xie Y., Hanai A., Makyio H., Kawasaki M., Kato R.,
RA Shin H.W., Nakayama K., Wakatsuki S.;
RT "Structural basis for membrane binding specificity of the
RT Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.";
RL J. Biol. Chem. 287:25478-25489(2012).
RN [20] {ECO:0007744|PDB:5EE5}
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 15-181 IN COMPLEX WITH GTP,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARFGEF1.
RX PubMed=27373159; DOI=10.1016/j.celrep.2016.06.022;
RA Galindo A., Soler N., McLaughlin S.H., Yu M., Williams R.L., Munro S.;
RT "Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to
RT the trans-Golgi.";
RL Cell Rep. 16:839-850(2016).
CC -!- FUNCTION: GTP-binding protein that recruits several effectors, such as
CC golgins, arfaptins and Arf-GEFs to the trans-Golgi network, and
CC modulates their functions at the Golgi complex (PubMed:9624189,
CC PubMed:21239483, PubMed:27436755, PubMed:22679020, PubMed:27373159).
CC Plays thereby a role in a wide range of fundamental cellular processes,
CC including cell polarity, innate immunity, or protein secretion mediated
CC by arfaptins, which were shown to play a role in maintaining insulin
CC secretion from pancreatic beta cells (PubMed:22981988).
CC {ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:22679020,
CC ECO:0000269|PubMed:22981988, ECO:0000269|PubMed:27373159,
CC ECO:0000269|PubMed:27436755, ECO:0000269|PubMed:9624189}.
CC -!- SUBUNIT: The GTP-bound form interacts with GOLGA1 (By similarity). The
CC GTP-bound form interacts with GOLGA4 and RGPD8. The GTP-bound form
CC directly interacts with ARFIP2 (PubMed:11303027, PubMed:21239483,
CC PubMed:22679020). Binds to SCOC, preferentially in its GTP-bound form.
CC May interact with UNC119 (PubMed:11303027, PubMed:14580338). Interacts
CC with ARFIP1; this interaction directs ARFIP1 to the trans-Golgi
CC membranes (PubMed:21239483, PubMed:22981988). Interacts with ARFGEF1
CC (via N-terminus) (PubMed:27436755, PubMed:27373159).
CC {ECO:0000250|UniProtKB:P61212, ECO:0000269|PubMed:11303027,
CC ECO:0000269|PubMed:14580338, ECO:0000269|PubMed:21239483,
CC ECO:0000269|PubMed:22679020, ECO:0000269|PubMed:22981988,
CC ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755}.
CC -!- INTERACTION:
CC P40616; P53367: ARFIP1; NbExp=2; IntAct=EBI-1052746, EBI-2808808;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11303027}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11303027}; Cytoplasmic side
CC {ECO:0000269|PubMed:11303027}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:27373159,
CC ECO:0000269|PubMed:27436755}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40616-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40616-2; Sequence=VSP_056566;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, lung and liver (at
CC protein level). Detected in fetal heart, lung, liver and kidney.
CC Detected in adult heart, placenta, lung, liver, skeletal muscle, kidney
CC and pancreas. {ECO:0000269|PubMed:9624189}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; L28997; AAC37567.1; -; mRNA.
DR EMBL; AF493887; AAM12601.1; -; mRNA.
DR EMBL; BT007260; AAP35924.1; -; mRNA.
DR EMBL; AK301701; BAG63173.1; -; mRNA.
DR EMBL; AK311793; BAG34736.1; -; mRNA.
DR EMBL; BX537387; CAD97629.1; -; mRNA.
DR EMBL; AC063948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97658.1; -; Genomic_DNA.
DR EMBL; BC007000; AAH07000.1; -; mRNA.
DR CCDS; CCDS44958.1; -. [P40616-1]
DR RefSeq; NP_001168.1; NM_001177.5. [P40616-1]
DR PDB; 1UPT; X-ray; 1.70 A; A/C/E/G=15-181.
DR PDB; 4DCN; X-ray; 3.01 A; A/B=14-179.
DR PDB; 5EE5; X-ray; 2.28 A; B=15-181.
DR PDB; 5J5C; X-ray; 3.40 A; A=16-181.
DR PDBsum; 1UPT; -.
DR PDBsum; 4DCN; -.
DR PDBsum; 5EE5; -.
DR PDBsum; 5J5C; -.
DR AlphaFoldDB; P40616; -.
DR SMR; P40616; -.
DR BioGRID; 106893; 79.
DR CORUM; P40616; -.
DR IntAct; P40616; 36.
DR MINT; P40616; -.
DR STRING; 9606.ENSP00000261636; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR iPTMnet; P40616; -.
DR MetOSite; P40616; -.
DR PhosphoSitePlus; P40616; -.
DR SwissPalm; P40616; -.
DR BioMuta; ARL1; -.
DR DMDM; 728888; -.
DR EPD; P40616; -.
DR jPOST; P40616; -.
DR MassIVE; P40616; -.
DR MaxQB; P40616; -.
DR PaxDb; P40616; -.
DR PeptideAtlas; P40616; -.
DR PRIDE; P40616; -.
DR ProteomicsDB; 5387; -.
DR ProteomicsDB; 55375; -. [P40616-1]
DR TopDownProteomics; P40616-1; -. [P40616-1]
DR Antibodypedia; 30383; 289 antibodies from 26 providers.
DR DNASU; 400; -.
DR Ensembl; ENST00000261636.13; ENSP00000261636.8; ENSG00000120805.14. [P40616-1]
DR Ensembl; ENST00000536227.5; ENSP00000441808.1; ENSG00000120805.14. [P40616-2]
DR Ensembl; ENST00000551828.5; ENSP00000448850.1; ENSG00000120805.14. [P40616-2]
DR GeneID; 400; -.
DR KEGG; hsa:400; -.
DR MANE-Select; ENST00000261636.13; ENSP00000261636.8; NM_001177.6; NP_001168.1.
DR UCSC; uc001tib.4; human. [P40616-1]
DR CTD; 400; -.
DR DisGeNET; 400; -.
DR GeneCards; ARL1; -.
DR HGNC; HGNC:692; ARL1.
DR HPA; ENSG00000120805; Low tissue specificity.
DR MIM; 603425; gene.
DR neXtProt; NX_P40616; -.
DR OpenTargets; ENSG00000120805; -.
DR PharmGKB; PA24985; -.
DR VEuPathDB; HostDB:ENSG00000120805; -.
DR eggNOG; KOG0072; Eukaryota.
DR GeneTree; ENSGT00940000155118; -.
DR HOGENOM; CLU_040729_9_4_1; -.
DR InParanoid; P40616; -.
DR OMA; QEGMDWL; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; P40616; -.
DR TreeFam; TF105461; -.
DR PathwayCommons; P40616; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; P40616; -.
DR BioGRID-ORCS; 400; 96 hits in 1086 CRISPR screens.
DR ChiTaRS; ARL1; human.
DR EvolutionaryTrace; P40616; -.
DR GeneWiki; ARL1; -.
DR GenomeRNAi; 400; -.
DR Pharos; P40616; Tbio.
DR PRO; PR:P40616; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P40616; protein.
DR Bgee; ENSG00000120805; Expressed in islet of Langerhans and 213 other tissues.
DR ExpressionAtlas; P40616; baseline and differential.
DR Genevisible; P40616; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:CACAO.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0031584; P:activation of phospholipase D activity; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0009404; P:toxin metabolic process; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Golgi apparatus; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor-like protein 1"
FT /id="PRO_0000207450"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14580338,
FT ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14580338"
FT BINDING 45..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14580338,
FT ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14580338"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14580338,
FT ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14580338,
FT ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14580338,
FT ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056566"
FT MUTAGEN 31
FT /note="T->N: Loss of interaction with ARFIP1 and ARFIP2."
FT /evidence="ECO:0000269|PubMed:21239483"
FT MUTAGEN 71
FT /note="Q->L: Altered Golgi structure with an engorged
FT lumen. Interacts with ARFIP2, GOLGA4, RGPD8, SCOC and
FT UNC119."
FT /evidence="ECO:0000269|PubMed:11303027"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1UPT"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1UPT"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1UPT"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1UPT"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5EE5"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1UPT"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1UPT"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1UPT"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1UPT"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:1UPT"
SQ SEQUENCE 181 AA; 20418 MW; 9FB736C8ED60DC3D CRC64;
MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN
LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI
LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR
Q
