ATLA2_HUMAN
ID ATLA2_HUMAN Reviewed; 583 AA.
AC Q8NHH9; B7Z1X2; B7Z7X8; Q4ZG30; Q7Z630; Q8NHH8; Q9H5M7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
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 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 [GENOMIC DNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-18.
RA Gorry M.C., Zhang Y., Marks J.J., Suppe B., Hart P.S., Cortelli J.R.,
RA Pallos D., Hart T.C.;
RT "Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC TISSUE=Cerebellum, and Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 IDENTIFICATION.
RX PubMed=14506257; DOI=10.1074/jbc.m306702200;
RA Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R.,
RA Blackstone C.;
RT "Cellular localization, oligomerization, and membrane association of the
RT hereditary spastic paraplegia 3A (SPG3A) protein atlastin.";
RL J. Biol. Chem. 278:49063-49071(2003).
RN [7]
RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-107 AND
RP ARG-244, AND TISSUE SPECIFICITY.
RX PubMed=18270207; DOI=10.1093/hmg/ddn046;
RA Rismanchi N., Soderblom C., Stadler J., Zhu P.-P., Blackstone C.;
RT "Atlastin GTPases are required for Golgi apparatus and ER morphogenesis.";
RL Hum. Mol. Genet. 17:1591-1604(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH ZFYVE27.
RX PubMed=23969831; DOI=10.1073/pnas.1307391110;
RA Chang J., Lee S., Blackstone C.;
RT "Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and
RT regulates network formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013).
RN [15]
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 [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-270, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17]
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 [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-107.
RX PubMed=27619977; DOI=10.7554/elife.18605;
RA Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.;
RT "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons
RT to generate a tubular membrane network.";
RL Elife 5:0-0(2016).
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 (PubMed:18270207, PubMed:19665976, PubMed:27619977).
CC {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976,
CC ECO:0000269|PubMed:27619977}.
CC -!- SUBUNIT: Interacts with REEP5 and RTN3 (PubMed:19665976). Interacts
CC with ZFYVE27 (PubMed:23969831). {ECO:0000269|PubMed:19665976,
CC ECO:0000269|PubMed:23969831}.
CC -!- INTERACTION:
CC Q8NHH9; Q5T4F4: ZFYVE27; NbExp=2; IntAct=EBI-2410430, EBI-3892947;
CC Q8NHH9; Q60870: Reep5; Xeno; NbExp=2; IntAct=EBI-2410430, EBI-2410304;
CC Q8NHH9; Q9ES97-3: Rtn3; Xeno; NbExp=2; IntAct=EBI-2410430, EBI-1487798;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:27619977}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18270207}. Note=Localizes at
CC endoplasmic reticulum (ER) three-way tubular junctions
CC (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=AT2b;
CC IsoId=Q8NHH9-1; Sequence=Displayed;
CC Name=2; Synonyms=AT2a;
CC IsoId=Q8NHH9-2; Sequence=VSP_025310;
CC Name=3;
CC IsoId=Q8NHH9-3; Sequence=VSP_025309;
CC Name=4;
CC IsoId=Q8NHH9-4; Sequence=VSP_041604, VSP_041605;
CC Name=5;
CC IsoId=Q8NHH9-5; Sequence=VSP_041604;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral tissues (at protein level).
CC {ECO:0000269|PubMed:18270207}.
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; AF449187; AAM97341.1; -; Genomic_DNA.
DR EMBL; AF449176; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449177; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449178; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449179; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449180; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449181; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449182; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449183; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449184; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449185; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449186; AAM97341.1; JOINED; Genomic_DNA.
DR EMBL; AF449187; AAM97342.1; -; Genomic_DNA.
DR EMBL; AF449176; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449177; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449178; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449179; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449180; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449181; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449182; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449183; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449184; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449185; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AF449186; AAM97342.1; JOINED; Genomic_DNA.
DR EMBL; AK026946; BAB15598.1; -; mRNA.
DR EMBL; AK294049; BAH11658.1; -; mRNA.
DR EMBL; AK302621; BAH13764.1; -; mRNA.
DR EMBL; AK225190; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016995; AAX88950.1; -; Genomic_DNA.
DR EMBL; BC053508; AAH53508.1; -; mRNA.
DR CCDS; CCDS1795.1; -. [Q8NHH9-2]
DR CCDS; CCDS46260.1; -. [Q8NHH9-1]
DR CCDS; CCDS77402.1; -. [Q8NHH9-5]
DR CCDS; CCDS86831.1; -. [Q8NHH9-3]
DR RefSeq; NP_001129145.1; NM_001135673.3. [Q8NHH9-1]
DR RefSeq; NP_001295005.1; NM_001308076.1. [Q8NHH9-5]
DR RefSeq; NP_001317387.1; NM_001330458.1. [Q8NHH9-3]
DR RefSeq; NP_001317388.1; NM_001330459.1. [Q8NHH9-4]
DR RefSeq; NP_001317389.1; NM_001330460.1.
DR RefSeq; NP_071769.2; NM_022374.4. [Q8NHH9-2]
DR AlphaFoldDB; Q8NHH9; -.
DR SMR; Q8NHH9; -.
DR BioGRID; 122115; 95.
DR CORUM; Q8NHH9; -.
DR IntAct; Q8NHH9; 38.
DR MINT; Q8NHH9; -.
DR STRING; 9606.ENSP00000368237; -.
DR TCDB; 9.B.390.1.1; the tmcc/tex28 (tm-tex) family.
DR GlyGen; Q8NHH9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NHH9; -.
DR PhosphoSitePlus; Q8NHH9; -.
DR BioMuta; ATL2; -.
DR DMDM; 147742983; -.
DR EPD; Q8NHH9; -.
DR jPOST; Q8NHH9; -.
DR MassIVE; Q8NHH9; -.
DR MaxQB; Q8NHH9; -.
DR PaxDb; Q8NHH9; -.
DR PeptideAtlas; Q8NHH9; -.
DR PRIDE; Q8NHH9; -.
DR ProteomicsDB; 6903; -.
DR ProteomicsDB; 73710; -. [Q8NHH9-1]
DR ProteomicsDB; 73711; -. [Q8NHH9-2]
DR ProteomicsDB; 73712; -. [Q8NHH9-3]
DR ProteomicsDB; 73713; -. [Q8NHH9-4]
DR Antibodypedia; 29481; 135 antibodies from 24 providers.
DR DNASU; 64225; -.
DR Ensembl; ENST00000378954.9; ENSP00000368237.4; ENSG00000119787.14. [Q8NHH9-1]
DR Ensembl; ENST00000402054.5; ENSP00000384062.1; ENSG00000119787.14. [Q8NHH9-3]
DR Ensembl; ENST00000419554.6; ENSP00000415336.2; ENSG00000119787.14. [Q8NHH9-2]
DR Ensembl; ENST00000452935.6; ENSP00000390743.2; ENSG00000119787.14. [Q8NHH9-5]
DR Ensembl; ENST00000651368.1; ENSP00000498813.1; ENSG00000119787.14. [Q8NHH9-3]
DR GeneID; 64225; -.
DR KEGG; hsa:64225; -.
DR MANE-Select; ENST00000378954.9; ENSP00000368237.4; NM_001135673.4; NP_001129145.1.
DR UCSC; uc002rqq.4; human. [Q8NHH9-1]
DR CTD; 64225; -.
DR DisGeNET; 64225; -.
DR GeneCards; ATL2; -.
DR HGNC; HGNC:24047; ATL2.
DR HPA; ENSG00000119787; Low tissue specificity.
DR MIM; 609368; gene.
DR neXtProt; NX_Q8NHH9; -.
DR OpenTargets; ENSG00000119787; -.
DR PharmGKB; PA164716322; -.
DR VEuPathDB; HostDB:ENSG00000119787; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000155710; -.
DR HOGENOM; CLU_021447_2_1_1; -.
DR InParanoid; Q8NHH9; -.
DR OMA; LEKRLQX; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q8NHH9; -.
DR TreeFam; TF105251; -.
DR PathwayCommons; Q8NHH9; -.
DR SignaLink; Q8NHH9; -.
DR BioGRID-ORCS; 64225; 463 hits in 1082 CRISPR screens.
DR ChiTaRS; ATL2; human.
DR GenomeRNAi; 64225; -.
DR Pharos; Q8NHH9; Tbio.
DR PRO; PR:Q8NHH9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NHH9; protein.
DR Bgee; ENSG00000119787; Expressed in secondary oocyte and 187 other tissues.
DR ExpressionAtlas; Q8NHH9; baseline and differential.
DR Genevisible; Q8NHH9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA: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; IDA:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR003191; Guanylate-bd/ATL_C.
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 Pfam; PF02841; GBP_C; 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_0000287105"
FT TOPO_DOM 1..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18270207"
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:0000269|PubMed:18270207"
FT DOMAIN 91..336
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..284
FT /evidence="ECO:0000255"
FT COMPBIAS 27..44
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:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 270
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025309"
FT VAR_SEQ 1..39
FT /note="MAEGDEAARGQQPHQGLWRRRRTSDPSAAVNHVSSTTSL -> MVLKKGIKF
FT FQRLINSKSLRF (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041604"
FT VAR_SEQ 545..583
FT /note="VLKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD -> RSPRKVFSK
FT LFEVTRRRMVHRALSSAQRQRLSSNNNKKKN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041605"
FT VAR_SEQ 546..583
FT /note="LKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD -> FSKLFEVTRR
FT RMVHRALSSAQRQRLSSNNNKKKN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025310"
FT VARIANT 18
FT /note="W -> R (in dbSNP:rs3731847)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_032265"
FT VARIANT 272
FT /note="N -> S (in dbSNP:rs34873284)"
FT /id="VAR_032266"
FT VARIANT 420
FT /note="D -> H (in dbSNP:rs7582826)"
FT /id="VAR_032267"
FT MUTAGEN 107
FT /note="K->A: Alters endoplasmic reticulum morphology."
FT /evidence="ECO:0000269|PubMed:18270207,
FT ECO:0000269|PubMed:27619977"
FT MUTAGEN 244
FT /note="R->Q: Alters endoplasmic reticulum morphogenesis."
FT /evidence="ECO:0000269|PubMed:18270207"
FT CONFLICT 509
FT /note="G -> E (in Ref. 2; BAB15598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 66229 MW; 885738C43996DEBF CRC64;
MAEGDEAARG QQPHQGLWRR RRTSDPSAAV NHVSSTTSLG ENYEDDDLVN 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 RDTYCKSMEQ VCGGDKPYIA PSDLERKHLD
LKEVAIKQFR SVKKMGGDEF CRRYQDQLEA EIEETYANFI KHNDGKNIFY AARTPATLFA
VMFAMYIISG LTGFIGLNSI AVLCNLVMGL ALIFLCTWAY VKYSGEFREI GTVIDQIAET
LWEQVLKPLG DNLMEENIRQ SVTNSIKAGL TDQVSHHARL KTD
