ARL8A_HUMAN
ID ARL8A_HUMAN Reviewed; 186 AA.
AC Q96BM9; B3KXD0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=ADP-ribosylation factor-like protein 8A;
DE AltName: Full=ADP-ribosylation factor-like protein 10B;
DE AltName: Full=Novel small G protein indispensable for equal chromosome segregation 2;
GN Name=ARL8A; Synonyms=ARL10B, GIE2;
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 TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15331635; DOI=10.1242/jcs.01347;
RA Okai T., Araki Y., Tada M., Tateno T., Kontani K., Katada T.;
RT "Novel small GTPase subfamily capable of associating with tubulin is
RT required for chromosome segregation.";
RL J. Cell Sci. 117:4705-4715(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16537643; DOI=10.1242/jcs.02958;
RA Hofmann I., Munro S.;
RT "An N-terminally acetylated Arf-like GTPase is localised to lysosomes and
RT affects their motility.";
RL J. Cell Sci. 119:1494-1503(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
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 [11]
RP INTERACTION WITH PLEKHM1.
RX PubMed=28325809; DOI=10.1083/jcb.201607085;
RA Marwaha R., Arya S.B., Jagga D., Kaur H., Tuli A., Sharma M.;
RT "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to
RT lysosomes.";
RL J. Cell Biol. 216:1051-1070(2017).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-186 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Structure of human ADP-ribosylation factor-like 10B.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in lysosome motility (By similarity). In
CC neurons, mediates the anterograde axonal long-range transport of
CC presynaptic lysosome-related vesicles required for presynaptic
CC biogenesis and synaptic function (By similarity). May play a role in
CC chromosome segregation (By similarity). {ECO:0000250|UniProtKB:Q9CQW2,
CC ECO:0000250|UniProtKB:Q9NVJ2}.
CC -!- SUBUNIT: Interacts with PLEKHM1. {ECO:0000269|PubMed:28325809}.
CC -!- INTERACTION:
CC Q96BM9; Q96EN8: MOCOS; NbExp=3; IntAct=EBI-4401082, EBI-1220583;
CC Q96BM9; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-4401082, EBI-1053259;
CC Q96BM9; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-4401082, EBI-742688;
CC Q96BM9; P07919: UQCRH; NbExp=6; IntAct=EBI-4401082, EBI-1224427;
CC Q96BM9; PRO_0000041224 [Q86500]; Xeno; NbExp=2; IntAct=EBI-4401082, EBI-11478518;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9NVJ2}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9CQW2}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9NVJ2}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9CQW2}. Synapse {ECO:0000250|UniProtKB:Q9CQW2}.
CC Note=Localizes with microtubules at the spindle mid-zone during
CC mitosis. {ECO:0000250|UniProtKB:Q9NVJ2}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15331635}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AB118752; BAD23993.1; -; mRNA.
DR EMBL; AK127138; BAG54442.1; -; mRNA.
DR EMBL; AL592300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91395.1; -; Genomic_DNA.
DR EMBL; BC015408; AAH15408.1; -; mRNA.
DR CCDS; CCDS1421.1; -.
DR RefSeq; NP_001243058.1; NM_001256129.1.
DR RefSeq; NP_620150.1; NM_138795.3.
DR PDB; 1ZD9; X-ray; 1.70 A; A=18-186.
DR PDB; 2H18; X-ray; 1.90 A; A=9-182.
DR PDB; 4ILE; X-ray; 2.68 A; A=1-181.
DR PDBsum; 1ZD9; -.
DR PDBsum; 2H18; -.
DR PDBsum; 4ILE; -.
DR AlphaFoldDB; Q96BM9; -.
DR SMR; Q96BM9; -.
DR BioGRID; 126084; 59.
DR IntAct; Q96BM9; 14.
DR MINT; Q96BM9; -.
DR STRING; 9606.ENSP00000272217; -.
DR GlyGen; Q96BM9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BM9; -.
DR PhosphoSitePlus; Q96BM9; -.
DR BioMuta; ARL8A; -.
DR DMDM; 74751775; -.
DR EPD; Q96BM9; -.
DR jPOST; Q96BM9; -.
DR MassIVE; Q96BM9; -.
DR MaxQB; Q96BM9; -.
DR PaxDb; Q96BM9; -.
DR PeptideAtlas; Q96BM9; -.
DR PRIDE; Q96BM9; -.
DR ProteomicsDB; 76090; -.
DR Antibodypedia; 34522; 230 antibodies from 23 providers.
DR DNASU; 127829; -.
DR Ensembl; ENST00000272217.7; ENSP00000272217.2; ENSG00000143862.8.
DR GeneID; 127829; -.
DR KEGG; hsa:127829; -.
DR MANE-Select; ENST00000272217.7; ENSP00000272217.2; NM_138795.4; NP_620150.1.
DR UCSC; uc001gxk.3; human.
DR CTD; 127829; -.
DR DisGeNET; 127829; -.
DR GeneCards; ARL8A; -.
DR HGNC; HGNC:25192; ARL8A.
DR HPA; ENSG00000143862; Low tissue specificity.
DR MIM; 616597; gene.
DR neXtProt; NX_Q96BM9; -.
DR OpenTargets; ENSG00000143862; -.
DR PharmGKB; PA134905021; -.
DR VEuPathDB; HostDB:ENSG00000143862; -.
DR eggNOG; KOG0075; Eukaryota.
DR GeneTree; ENSGT00940000159657; -.
DR HOGENOM; CLU_040729_10_0_1; -.
DR InParanoid; Q96BM9; -.
DR OMA; KIDIQPH; -.
DR OrthoDB; 1123043at2759; -.
DR PhylomeDB; Q96BM9; -.
DR TreeFam; TF105470; -.
DR PathwayCommons; Q96BM9; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q96BM9; -.
DR BioGRID-ORCS; 127829; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; ARL8A; human.
DR EvolutionaryTrace; Q96BM9; -.
DR GeneWiki; ARL8A; -.
DR GenomeRNAi; 127829; -.
DR Pharos; Q96BM9; Tbio.
DR PRO; PR:Q96BM9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96BM9; protein.
DR Bgee; ENSG00000143862; Expressed in cortical plate and 170 other tissues.
DR ExpressionAtlas; Q96BM9; baseline and differential.
DR Genevisible; Q96BM9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd04159; Arl10_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044154; Arl8a/8b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
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; Cell cycle; Cell division; Cell projection;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Endosome; GTP-binding;
KW Lysosome; Membrane; Mitosis; Nucleotide-binding; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..186
FT /note="ADP-ribosylation factor-like protein 8A"
FT /id="PRO_0000232916"
FT INTRAMEM 1..19
FT /note="Note=Mediates targeting to membranes"
FT /evidence="ECO:0000250"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:2H18"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1ZD9"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2H18"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1ZD9"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1ZD9"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1ZD9"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1ZD9"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1ZD9"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1ZD9"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1ZD9"
SQ SEQUENCE 186 AA; 21416 MW; EE5141235CE0F414 CRC64;
MIALFNKLLD WFKALFWKEE MELTLVGLQY SGKTTFVNVI ASGQFNEDMI PTVGFNMRKI
TKGNVTIKLW DIGGQPRFRS MWERYCRGVS AIVYMVDAAD QEKIEASKNE LHNLLDKPQL
QGIPVLVLGN KRDLPGALDE KELIEKMNLS AIQDREICCY SISCKEKDNI DITLQWLIQH
SKSRRS
