ARF3_HUMAN
ID ARF3_HUMAN Reviewed; 181 AA.
AC P61204; A8K6G8; B7ZB63; P16587;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=ADP-ribosylation factor 3;
GN Name=ARF3;
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=Cerebellum;
RX PubMed=2474826; DOI=10.1073/pnas.86.16.6101;
RA Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J.,
RA Vaughan M.;
RT "Molecular cloning, characterization, and expression of human ADP-
RT ribosylation factors: two guanine nucleotide-dependent activators of
RT cholera toxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1744102; DOI=10.1016/s0021-9258(18)54462-8;
RA Tsai S.C., Haun R.S., Tsuchiya M., Moss J., Vaughan M.;
RT "Isolation and characterization of the human gene for ADP-ribosylation
RT factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera
RT toxin.";
RL J. Biol. Chem. 266:23053-23059(1991).
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 Trachea;
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 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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, and Skin;
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 [9]
RP INTERACTION WITH PRKCABP.
RX PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
RA Takeya R., Takeshige K., Sumimoto H.;
RT "Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation
RT factors.";
RL Biochem. Biophys. Res. Commun. 267:149-155(2000).
RN [10]
RP INTERACTION WITH PI4KB AND NCS1, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions with
RT NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
CC -!- FUNCTION: GTP-binding protein that functions as an allosteric activator
CC of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
CC Involved in protein trafficking; may modulate vesicle budding and
CC uncoating within the Golgi apparatus.
CC -!- SUBUNIT: Interacts with PRKCABP. Interacts with PI4KB and NCS1/FREQ at
CC the Golgi complex. {ECO:0000269|PubMed:10623590,
CC ECO:0000269|PubMed:17555535}.
CC -!- INTERACTION:
CC P61204; P05067: APP; NbExp=3; IntAct=EBI-641535, EBI-77613;
CC P61204; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-641535, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61204-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61204-2; Sequence=VSP_056935;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; M74493; AAA58359.1; -; Genomic_DNA.
DR EMBL; M33384; AAA83931.1; -; mRNA.
DR EMBL; M74491; AAB59425.1; -; mRNA.
DR EMBL; AF493882; AAM12596.1; -; mRNA.
DR EMBL; BT006670; AAP35316.1; -; mRNA.
DR EMBL; AK291633; BAF84322.1; -; mRNA.
DR EMBL; AK316528; BAH14899.1; -; mRNA.
DR EMBL; AC073610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58026.1; -; Genomic_DNA.
DR EMBL; BC007647; AAH07647.1; -; mRNA.
DR EMBL; BC007762; AAH07762.1; -; mRNA.
DR EMBL; BC017565; AAH17565.1; -; mRNA.
DR EMBL; BC028402; AAH28402.1; -; mRNA.
DR CCDS; CCDS8774.1; -. [P61204-1]
DR PIR; A41570; A41570.
DR RefSeq; NP_001650.1; NM_001659.2. [P61204-1]
DR RefSeq; XP_005268913.1; XM_005268856.1. [P61204-1]
DR PDB; 6II6; X-ray; 2.10 A; C/D=13-176.
DR PDBsum; 6II6; -.
DR AlphaFoldDB; P61204; -.
DR SMR; P61204; -.
DR BioGRID; 106872; 67.
DR IntAct; P61204; 19.
DR MINT; P61204; -.
DR STRING; 9606.ENSP00000256682; -.
DR GlyGen; P61204; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P61204; -.
DR MetOSite; P61204; -.
DR PhosphoSitePlus; P61204; -.
DR SwissPalm; P61204; -.
DR BioMuta; ARF3; -.
DR DMDM; 47117657; -.
DR OGP; P16587; -.
DR EPD; P61204; -.
DR jPOST; P61204; -.
DR MassIVE; P61204; -.
DR MaxQB; P61204; -.
DR PaxDb; P61204; -.
DR PeptideAtlas; P61204; -.
DR PRIDE; P61204; -.
DR ProteomicsDB; 57274; -. [P61204-1]
DR ProteomicsDB; 7097; -.
DR TopDownProteomics; P61204-1; -. [P61204-1]
DR Antibodypedia; 25743; 125 antibodies from 28 providers.
DR DNASU; 377; -.
DR Ensembl; ENST00000256682.9; ENSP00000256682.4; ENSG00000134287.10. [P61204-1]
DR Ensembl; ENST00000447318.6; ENSP00000395370.2; ENSG00000134287.10. [P61204-2]
DR Ensembl; ENST00000541959.5; ENSP00000438510.1; ENSG00000134287.10. [P61204-1]
DR GeneID; 377; -.
DR KEGG; hsa:377; -.
DR MANE-Select; ENST00000256682.9; ENSP00000256682.4; NM_001659.3; NP_001650.1.
DR UCSC; uc001rsr.3; human. [P61204-1]
DR CTD; 377; -.
DR DisGeNET; 377; -.
DR GeneCards; ARF3; -.
DR HGNC; HGNC:654; ARF3.
DR HPA; ENSG00000134287; Low tissue specificity.
DR MIM; 103190; gene.
DR neXtProt; NX_P61204; -.
DR OpenTargets; ENSG00000134287; -.
DR PharmGKB; PA24936; -.
DR VEuPathDB; HostDB:ENSG00000134287; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61204; -.
DR OMA; LYHESCK; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P61204; -.
DR TreeFam; TF300808; -.
DR PathwayCommons; P61204; -.
DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P61204; -.
DR BioGRID-ORCS; 377; 25 hits in 1060 CRISPR screens.
DR ChiTaRS; ARF3; human.
DR GeneWiki; ARF3; -.
DR GenomeRNAi; 377; -.
DR Pharos; P61204; Tbio.
DR PRO; PR:P61204; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P61204; protein.
DR Bgee; ENSG00000134287; Expressed in prefrontal cortex and 209 other tissues.
DR ExpressionAtlas; P61204; baseline and differential.
DR Genevisible; P61204; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IGI:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
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; Cytoplasm; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 3"
FT /id="PRO_0000207386"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
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 VAR_SEQ 50..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056935"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6II6"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6II6"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:6II6"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6II6"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6II6"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6II6"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6II6"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:6II6"
SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64;
MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
K
