ARL8A_MOUSE
ID ARL8A_MOUSE Reviewed; 186 AA.
AC Q8VEH3; Q99KS1; Q9CTB0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-186.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=30174114; DOI=10.1016/j.neuron.2018.08.004;
RA Vukoja A., Rey U., Petzoldt A.G., Ott C., Vollweiter D., Quentin C.,
RA Puchkov D., Reynolds E., Lehmann M., Hohensee S., Rosa S., Lipowsky R.,
RA Sigrist S.J., Haucke V.;
RT "Presynaptic Biogenesis Requires Axonal Transport of Lysosome-Related
RT Vesicles.";
RL Neuron 99:1216-1232(2018).
CC -!- FUNCTION: Plays a role in lysosomes motility (PubMed:30174114). In
CC neurons, mediates the anterograde axonal long-range transport of
CC presynaptic lysosome-related vesicles required for presynaptic
CC biogenesis and synaptic function (PubMed:30174114). May play a role in
CC chromosome segregation (By similarity). {ECO:0000250|UniProtKB:Q9NVJ2,
CC ECO:0000269|PubMed:30174114}.
CC -!- SUBUNIT: Interacts with PLEKHM1. {ECO:0000250|UniProtKB:Q96BM9}.
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AB185207; BAD30091.1; -; mRNA.
DR EMBL; BC004035; AAH04035.1; -; mRNA.
DR EMBL; BC018479; AAH18479.1; -; mRNA.
DR EMBL; AK004080; BAB23160.1; -; mRNA.
DR CCDS; CCDS15316.1; -.
DR RefSeq; NP_081099.1; NM_026823.2.
DR AlphaFoldDB; Q8VEH3; -.
DR SMR; Q8VEH3; -.
DR BioGRID; 213014; 3.
DR IntAct; Q8VEH3; 2.
DR STRING; 10090.ENSMUSP00000027684; -.
DR iPTMnet; Q8VEH3; -.
DR PhosphoSitePlus; Q8VEH3; -.
DR SwissPalm; Q8VEH3; -.
DR EPD; Q8VEH3; -.
DR jPOST; Q8VEH3; -.
DR MaxQB; Q8VEH3; -.
DR PaxDb; Q8VEH3; -.
DR PeptideAtlas; Q8VEH3; -.
DR PRIDE; Q8VEH3; -.
DR ProteomicsDB; 282020; -.
DR TopDownProteomics; Q8VEH3; -.
DR Antibodypedia; 34522; 230 antibodies from 23 providers.
DR DNASU; 68724; -.
DR Ensembl; ENSMUST00000027684; ENSMUSP00000027684; ENSMUSG00000026426.
DR GeneID; 68724; -.
DR KEGG; mmu:68724; -.
DR UCSC; uc007csu.1; mouse.
DR CTD; 127829; -.
DR MGI; MGI:1915974; Arl8a.
DR VEuPathDB; HostDB:ENSMUSG00000026426; -.
DR eggNOG; KOG0075; Eukaryota.
DR GeneTree; ENSGT00940000159657; -.
DR HOGENOM; CLU_040729_10_0_1; -.
DR InParanoid; Q8VEH3; -.
DR OMA; KIDIQPH; -.
DR OrthoDB; 1123043at2759; -.
DR PhylomeDB; Q8VEH3; -.
DR TreeFam; TF105470; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 68724; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Arl8a; mouse.
DR PRO; PR:Q8VEH3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VEH3; protein.
DR Bgee; ENSMUSG00000026426; Expressed in cortical plate and 250 other tissues.
DR ExpressionAtlas; Q8VEH3; baseline and differential.
DR Genevisible; Q8VEH3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008089; P:anterograde axonal transport; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
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 Cell cycle; Cell division; Cell projection; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Endosome; GTP-binding; Lysosome; Membrane;
KW Mitosis; Nucleotide-binding; Protein transport; Reference proteome;
KW Synapse; Transport.
FT CHAIN 1..186
FT /note="ADP-ribosylation factor-like protein 8A"
FT /id="PRO_0000232917"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
SQ SEQUENCE 186 AA; 21390 MW; EE51413EF78D5F64 CRC64;
MIALFNKLLD WFKALFWKEE MELTLVGLQY SGKTTFVNVI ASGQFNEDMI PTVGFNMRKI
TKGNVTIKLW DIGGQPRFRS MWERYCRGVS AIVYMVDAAD QEKIEASKNE LHNLLDKPQL
QGIPVLVLGN KRDLAGALDE KELIEKMNLS AIQDREICCY SISCKEKDNI DITLQWLIQH
SKSRRS
