AR2BP_MOUSE
ID AR2BP_MOUSE Reviewed; 163 AA.
AC Q9D385; Q9CQW6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ADP-ribosylation factor-like protein 2-binding protein;
DE Short=ARF-like 2-binding protein;
DE AltName: Full=Binder of ARF2 protein 1;
GN Name=Arl2bp; Synonyms=Bart, Bart1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Medulla oblongata, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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 [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=10488091; DOI=10.1074/jbc.274.39.27553;
RA Sharer J.D., Kahn R.A.;
RT "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and
RT initial characterization.";
RL J. Biol. Chem. 274:27553-27561(1999).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH ARL2 AND SLC25A4, INTERACTION WITH ARL2,
RP AND TISSUE SPECIFICITY.
RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT transporter.";
RL Mol. Biol. Cell 13:71-83(2002).
RN [6]
RP INTERACTION WITH STAT2; STAT3 AND STAT4, AND TISSUE SPECIFICITY.
RX PubMed=18234692; DOI=10.1093/intimm/dxm154;
RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
RA Matsuda T.;
RT "BART is essential for nuclear retention of STAT3.";
RL Int. Immunol. 20:395-403(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, 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 [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23849777; DOI=10.1016/j.ajhg.2013.06.003;
RA Davidson A.E., Schwarz N., Zelinger L., Stern-Schneider G., Shoemark A.,
RA Spitzbarth B., Gross M., Laxer U., Sosna J., Sergouniotis P.I.,
RA Waseem N.H., Wilson R., Kahn R.A., Plagnol V., Wolfrum U., Banin E.,
RA Hardcastle A.J., Cheetham M.E., Sharon D., Webster A.R.;
RT "Mutations in ARL2BP, encoding ADP-ribosylation-factor-like 2 binding
RT protein, cause autosomal-recessive retinitis pigmentosa.";
RL Am. J. Hum. Genet. 93:321-329(2013).
CC -!- FUNCTION: Together with ARL2, plays a role in the nuclear
CC translocation, retention and transcriptional activity of STAT3. May
CC play a role as an effector of ARL2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GTP bound ARL2 and ARL3; the complex ARL2-
CC ARL2BP as well as ARL2BP alone, binds to SLC25A4/ANT1. Interaction with
CC ARL2 may be required for targeting to cilia basal body (By similarity).
CC Interacts with STAT3; interaction is enhanced with ARL2. Found in a
CC complex with ARL2BP, ARL2 and SLC25A6 (By similarity). Found in a
CC complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and
CC STAT4. {ECO:0000250, ECO:0000269|PubMed:11809823,
CC ECO:0000269|PubMed:18234692}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23849777}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:23849777}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:23849777}. Note=Detected in the midbody
CC matrix. Not detected in the Golgi, nucleus and on the mitotic spindle.
CC Centrosome-associated throughout the cell cycle. Not detected to
CC interphase microtubules (By similarity). The complex formed with
CC ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. In retina
CC photoreceptor cells, localized in the distal connecting cilia, basal
CC body, ciliary-associated centriole, and ciliary rootlet. Interaction
CC with ARL2 may be required for cilia basal body localization (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D385-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D385-2; Sequence=VSP_025320, VSP_025319;
CC -!- TISSUE SPECIFICITY: Widely expressed, with most abundant activity in
CC brain, especially in hippocampus and cortex. Also expressed in lung,
CC cerebellum, liver, kidney, retina, spleen, muscle and heart (at protein
CC level). {ECO:0000269|PubMed:10488091, ECO:0000269|PubMed:11809823,
CC ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:23849777}.
CC -!- SIMILARITY: Belongs to the ARL2BP family. {ECO:0000305}.
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DR EMBL; AK006418; BAB24578.1; -; mRNA.
DR EMBL; AK006646; BAB24686.1; -; mRNA.
DR EMBL; AK018229; BAB31126.1; -; mRNA.
DR EMBL; AK155242; BAE33143.1; -; mRNA.
DR EMBL; AK161325; BAE36323.1; -; mRNA.
DR EMBL; CT010168; CAJ18376.1; -; mRNA.
DR EMBL; BC002131; AAH02131.1; -; mRNA.
DR EMBL; BC024708; AAH24708.1; -; mRNA.
DR CCDS; CCDS22545.1; -. [Q9D385-1]
DR CCDS; CCDS40440.1; -. [Q9D385-2]
DR RefSeq; NP_077153.1; NM_024191.2. [Q9D385-1]
DR RefSeq; NP_077231.1; NM_024269.4. [Q9D385-2]
DR AlphaFoldDB; Q9D385; -.
DR SMR; Q9D385; -.
DR BioGRID; 223398; 1.
DR STRING; 10090.ENSMUSP00000034228; -.
DR iPTMnet; Q9D385; -.
DR PhosphoSitePlus; Q9D385; -.
DR EPD; Q9D385; -.
DR MaxQB; Q9D385; -.
DR PaxDb; Q9D385; -.
DR PeptideAtlas; Q9D385; -.
DR PRIDE; Q9D385; -.
DR ProteomicsDB; 296339; -. [Q9D385-1]
DR ProteomicsDB; 296340; -. [Q9D385-2]
DR Antibodypedia; 28836; 322 antibodies from 25 providers.
DR Ensembl; ENSMUST00000034228; ENSMUSP00000034228; ENSMUSG00000031776. [Q9D385-1]
DR Ensembl; ENSMUST00000109527; ENSMUSP00000105153; ENSMUSG00000031776. [Q9D385-2]
DR GeneID; 107566; -.
DR KEGG; mmu:107566; -.
DR UCSC; uc009mwt.3; mouse. [Q9D385-1]
DR UCSC; uc009mwu.3; mouse. [Q9D385-2]
DR CTD; 23568; -.
DR MGI; MGI:1349429; Arl2bp.
DR VEuPathDB; HostDB:ENSMUSG00000031776; -.
DR eggNOG; ENOG502RYJD; Eukaryota.
DR GeneTree; ENSGT00390000015052; -.
DR HOGENOM; CLU_116781_0_0_1; -.
DR InParanoid; Q9D385; -.
DR OMA; LIQRNFM; -.
DR OrthoDB; 1403493at2759; -.
DR PhylomeDB; Q9D385; -.
DR TreeFam; TF315143; -.
DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR BioGRID-ORCS; 107566; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Arl2bp; mouse.
DR PRO; PR:Q9D385; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D385; protein.
DR Bgee; ENSMUSG00000031776; Expressed in seminiferous tubule of testis and 261 other tissues.
DR ExpressionAtlas; Q9D385; baseline and differential.
DR Genevisible; Q9D385; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR Gene3D; 1.20.1520.10; -; 1.
DR InterPro; IPR038849; ARL2BP.
DR InterPro; IPR023379; BART_dom.
DR InterPro; IPR042541; BART_sf.
DR PANTHER; PTHR15487; PTHR15487; 1.
DR Pfam; PF11527; ARL2_Bind_BART; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..163
FT /note="ADP-ribosylation factor-like protein 2-binding
FT protein"
FT /id="PRO_0000287115"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025320"
FT VAR_SEQ 12..13
FT /note="SF -> MR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025319"
SQ SEQUENCE 163 AA; 18754 MW; AE489178C0382255 CRC64;
MDALEEESFA LSFSSASDAE FDAVVGCLED IIMDDEFQLL QRNFMDKYYQ EFEDTEENKL
TYTPIFNEYI SLVEKYIEEQ LLERIPGFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA
FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSTPASQNN LRH
