ATLA2_MOUSE
ID ATLA2_MOUSE Reviewed; 583 AA.
AC Q6PA06; Q3UX01; Q7TMM3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Atlastin-2;
DE EC=3.6.5.-;
DE AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 2;
DE Short=ARL-6-interacting protein 2;
DE Short=Aip-2;
GN Name=Atl2; Synonyms=Arl6ip2;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Oocyte;
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).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP INTERACTION WITH REEP5 AND RTN3.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic reticulum
CC membranes. Functions in endoplasmic reticulum tubular network
CC biogenesis. {ECO:0000250|UniProtKB:Q8NHH9}.
CC -!- SUBUNIT: Interacts with REEP5 and RTN3 (PubMed:19665976). Interacts
CC with ZFYVE27 (By similarity). {ECO:0000250|UniProtKB:Q8NHH9,
CC ECO:0000269|PubMed:19665976}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NHH9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NHH9}. Note=Localizes at endoplasmic reticulum
CC (ER) three-way tubular junctions. {ECO:0000250|UniProtKB:Q8NHH9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PA06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PA06-2; Sequence=VSP_025311;
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; AK135988; BAE22763.1; -; mRNA.
DR EMBL; BC060501; AAH60501.1; -; mRNA.
DR CCDS; CCDS37700.1; -. [Q6PA06-1]
DR RefSeq; NP_062691.3; NM_019717.3. [Q6PA06-1]
DR RefSeq; NP_835151.2; NM_178050.4.
DR AlphaFoldDB; Q6PA06; -.
DR SMR; Q6PA06; -.
DR BioGRID; 207886; 5.
DR IntAct; Q6PA06; 1.
DR MINT; Q6PA06; -.
DR STRING; 10090.ENSMUSP00000064758; -.
DR iPTMnet; Q6PA06; -.
DR PhosphoSitePlus; Q6PA06; -.
DR SwissPalm; Q6PA06; -.
DR EPD; Q6PA06; -.
DR jPOST; Q6PA06; -.
DR MaxQB; Q6PA06; -.
DR PaxDb; Q6PA06; -.
DR PeptideAtlas; Q6PA06; -.
DR PRIDE; Q6PA06; -.
DR ProteomicsDB; 277068; -. [Q6PA06-1]
DR ProteomicsDB; 277069; -. [Q6PA06-2]
DR Antibodypedia; 29481; 135 antibodies from 24 providers.
DR DNASU; 56298; -.
DR Ensembl; ENSMUST00000068282; ENSMUSP00000064758; ENSMUSG00000059811. [Q6PA06-1]
DR GeneID; 56298; -.
DR KEGG; mmu:56298; -.
DR UCSC; uc008dqe.2; mouse. [Q6PA06-1]
DR CTD; 64225; -.
DR MGI; MGI:1929492; Atl2.
DR VEuPathDB; HostDB:ENSMUSG00000059811; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000155710; -.
DR HOGENOM; CLU_021447_2_1_1; -.
DR InParanoid; Q6PA06; -.
DR OMA; LEKRLQX; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q6PA06; -.
DR TreeFam; TF105251; -.
DR BioGRID-ORCS; 56298; 15 hits in 72 CRISPR screens.
DR ChiTaRS; Atl2; mouse.
DR PRO; PR:Q6PA06; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6PA06; protein.
DR Bgee; ENSMUSG00000059811; Expressed in extensor digitorum longus and 277 other tissues.
DR ExpressionAtlas; Q6PA06; baseline and differential.
DR Genevisible; Q6PA06; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR036543; Guanylate-bd_C_sf.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; GTP-binding;
KW Hydrolase; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..583
FT /note="Atlastin-2"
FT /id="PRO_0000287107"
FT TOPO_DOM 1..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..499
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 91..336
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..284
FT /evidence="ECO:0000255"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 145..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 244..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 303..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHH9"
FT MOD_RES 270
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHH9"
FT VAR_SEQ 1..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025311"
FT CONFLICT 466
FT /note="K -> R (in Ref. 1; BAE22763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 66224 MW; 9530B0F2077FE2D3 CRC64;
MAEGDEAARR QQPQQGLRRR RQTSDSSVGV NHVSSTTSLG EDYEDDDLVN SDEVMKKPCP
VQIVLAHEDD HNFELDEEAL EQILLQEHIR DLNIVVVSVA GAFRKGKSFL LDFMLRYMYN
KDSQSWIGGN NEPLTGFTWR GGCERETTGI QVWNEVFVID RPNGTKVAVL LMDTQGAFDS
QSTIKDCATV FALSTMTSSV QVYNLSQNIQ EDDLQHLQLF TEYGRLAMEE IYQKPFQTLM
FLIRDWSYPY EHSYGLEGGK QFLEKRLQVK QNQHEELQNV RKHIHNCFSN LGCFLLPHPG
LKVATNPSFD GRLKDIDEDF KRELRNLVPL LLAPENLVEK EISGSKVTCR DLVEYFKAYI
KIYQGEELPH PKSMLQATAE ANNLAAVAGA RDVYCKSMEQ VCGGDKPYIA PSDLERKHLD
LKEVALKQFR SVKKMGGDEF CRRYQDQLEA EIEETYANFI KHNDGKNIFY AARTPATLFA
VMFAMYIISG LTGFIGLNSI AVLCNLVMGL ALTSLCTWAY VKYSGEFREI GTMIDQIAET
LWEQVLKPLG DNLMEENIRQ SVTNSIKAGL TDQVSHHARL KTD
