ID ATLA1_HUMAN Reviewed; 558 AA. AC Q8WXF7; A6NND5; A8K2C0; G5E9T1; O95890; Q69YH7; Q96FK0; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 184. DE RecName: Full=Atlastin-1; DE EC=3.6.5.-; DE AltName: Full=Brain-specific GTP-binding protein; DE AltName: Full=GTP-binding protein 3; DE Short=GBP-3; DE Short=hGBP3; DE AltName: Full=Guanine nucleotide-binding protein 3; DE AltName: Full=Spastic paraplegia 3 protein A; GN Name=ATL1; Synonyms=GBP3, SPG3A; 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] (ISOFORM 1), AND VARIANTS SPG3 CYS-239; ARG-258 RP AND TYR-259. RX PubMed=11685207; DOI=10.1038/ng758; RA Zhao X., Alvarado D., Rainier S., Lemons R., Hedera P., Weber C.H., RA Tukel T., Apak M., Heiman-Patterson T., Ming L., Bui M., Fink J.K.; RT "Mutations in a newly identified GTPase gene cause autosomal dominant RT hereditary spastic paraplegia."; RL Nat. Genet. 29:326-331(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MAP4K4. RX PubMed=12387898; DOI=10.1016/s0014-5793(02)03467-1; RA Luan Z., Zhang Y., Liu A., Man Y., Cheng L., Hu G.; RT "A novel GTP-binding protein hGBP3 interacts with NIK/HGK."; RL FEBS Lett. 530:233-238(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thalamus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Endometrium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-43 AND RP CYS-193. RC 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-558 (ISOFORM 1). RC TISSUE=Brain; RA Mei G., Yu W., Gibbs R.A.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, REGION, TOPOLOGY, AND RP SUBUNIT. 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 [10] RP INTERACTION WITH SPAST, AND SUBCELLULAR LOCATION. RX PubMed=16339213; DOI=10.1093/hmg/ddi447; RA Sanderson C.M., Connell J.W., Edwards T.L., Bright N.A., Duley S., RA Thompson A., Luzio J.P., Reid E.; RT "Spastin and atlastin, two proteins mutated in autosomal-dominant RT hereditary spastic paraplegia, are binding partners."; RL Hum. Mol. Genet. 15:307-318(2006). RN [11] RP INTERACTION WITH SPAST. RX PubMed=16815977; DOI=10.1073/pnas.0510863103; RA Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.; RT "Interaction of two hereditary spastic paraplegia gene products, spastin RT and atlastin, suggests a common pathway for axonal maintenance."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SPG3 PRO-161; RP CYS-239 AND TRP-495, MUTAGENESIS OF PHE-151; THR-162 AND SER-398, RP INTERACTION WITH TMED2, AND TISSUE SPECIFICITY. RX PubMed=17321752; DOI=10.1016/j.mcn.2007.01.012; RA Namekawa M., Muriel M.-P., Janer A., Latouche M., Dauphin A., Debeir T., RA Martin E., Duyckaerts C., Prigent A., Depienne C., Sittler A., Brice A., RA Ruberg M.; RT "Mutations in the SPG3A gene encoding the GTPase atlastin interfere with RT vesicle trafficking in the ER/Golgi interface and Golgi morphogenesis."; RL Mol. Cell. Neurosci. 35:1-13(2007). RN [13] RP FUNCTION, CHARACTERIZATION OF VARIANT SPAG3 GLN-217, MUTAGENESIS OF LYS-80, RP 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [15] RP FUNCTION, INTERACTION WITH REEP5; RTN3 AND RTN4, AND SUBCELLULAR LOCATION. 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 [16] RP INTERACTION WITH REEP1. RX PubMed=20200447; DOI=10.1172/jci40979; RA Park S.H., Zhu P.P., Parker R.L., Blackstone C.; RT "Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 RT coordinate microtubule interactions with the tubular ER network."; RL J. Clin. Invest. 120:1097-1110(2010). RN [17] 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 [18] RP INTERACTION WITH CPT1C. RX PubMed=25751282; DOI=10.1001/jamaneurol.2014.4769; RA Rinaldi C., Schmidt T., Situ A.J., Johnson J.O., Lee P.R., Chen K.L., RA Bott L.C., Fado R., Harmison G.H., Parodi S., Grunseich C., Renvoise B., RA Biesecker L.G., De Michele G., Santorelli F.M., Filla A., Stevanin G., RA Duerr A., Brice A., Casals N., Traynor B.J., Blackstone C., Ulmer T.S., RA Fischbeck K.H.; RT "Mutation in CPT1C Associated with pure autosomal dominant spastic RT paraplegia."; RL JAMA Neurol. 72:561-570(2015). RN [19] RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT GLN-217, AND RP MUTAGENESIS OF LYS-80. 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). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-447 IN COMPLEX WITH GDP, RP FUNCTION, CHARACTERIZATION OF VARIANT CYS-196, CHARACTERIZATION OF VARIANT RP SPAG3 GLN-217, MUTAGENESIS OF ARG-77; GLN-191 AND HIS-247, AND SUBUNIT. RX PubMed=21220294; DOI=10.1073/pnas.1012792108; RA Byrnes L.J., Sondermann H.; RT "Structural basis for the nucleotide-dependent dimerization of the large G RT protein atlastin-1/SPG3A."; RL Proc. Natl. Acad. Sci. U.S.A. 108:2216-2221(2011). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 18-447IN COMPLEX WITH GDP, AND RP SUBUNIT. RX PubMed=21368113; DOI=10.1073/pnas.1101643108; RA Bian X., Klemm R.W., Liu T.Y., Zhang M., Sun S., Sui X., Liu X., RA Rapoport T.A., Hu J.; RT "Structures of the atlastin GTPase provide insight into homotypic fusion of RT endoplasmic reticulum membranes."; RL Proc. Natl. Acad. Sci. U.S.A. 108:3976-3981(2011). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 1-446 IN COMPLEX WITH GTP ANALOG, RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-77. RX PubMed=23334294; DOI=10.1038/emboj.2012.353; RA Byrnes L.J., Singh A., Szeto K., Benvin N.M., O'Donnell J.P., Zipfel W.R., RA Sondermann H.; RT "Structural basis for conformational switching and GTP loading of the large RT G protein atlastin."; RL EMBO J. 32:369-384(2013). RN [23] RP VARIANT SPG3 GLN-217. RX PubMed=12112092; DOI=10.1002/ana.10185; RA Muglia M., Magariello A., Nicoletti G., Patitucci A., Gabriele A.L., RA Conforti F.L., Mazzei R., Caracciolo M., Ardito B., Lastilla M., RA Tedeschi G., Quattrone A.; RT "Further evidence that SPG3A gene mutations cause autosomal dominant RT hereditary spastic paraplegia."; RL Ann. Neurol. 51:794-795(2002). RN [24] RP VARIANT SPG3 VAL-408. RX PubMed=12939451; DOI=10.1212/01.wnl.0000078189.73611.df; RA Dalpozzo F., Rossetto M.G., Boaretto F., Sartori E., Mostacciuolo M.L., RA Daga A., Bassi M.T., Martinuzzi A.; RT "Infancy onset hereditary spastic paraplegia associated with a novel RT atlastin mutation."; RL Neurology 61:580-581(2003). RN [25] RP VARIANTS SPG3 PRO-161 AND PRO-247. RX PubMed=14695538; DOI=10.1002/humu.9205; RA Sauter S.M., Engel W., Neumann L.M., Kunze J., Neesen J.; RT "Novel mutations in the Atlastin gene (SPG3A) in families with autosomal RT dominant hereditary spastic paraplegia and evidence for late onset forms of RT HSP linked to the SPG3A locus."; RL Hum. Mutat. 23:98-98(2004). RN [26] RP VARIANT SPG3 TRP-415. RX PubMed=15184642; DOI=10.1212/01.wnl.0000127698.88895.85; RA D'Amico A., Tessa A., Sabino A., Bertini E., Santorelli F.M., Servidei S.; RT "Incomplete penetrance in an SPG3A-linked family with a new mutation in the RT atlastin gene."; RL Neurology 62:2138-2139(2004). RN [27] RP VARIANT SPG3 TRP-157. RX PubMed=16533974; DOI=10.1001/archneur.63.3.445; RA Rainier S., Sher C., Reish O., Thomas D., Fink J.K.; RT "De novo occurrence of novel SPG3A/atlastin mutation presenting as cerebral RT palsy."; RL Arch. Neurol. 63:445-447(2006). RN [28] RP VARIANT SPG3 ASN-436 DEL, AND CHARACTERIZATION OF VARIANT SPG3 ASN-436 DEL. RX PubMed=17427918; DOI=10.1002/ana.21114; RA Meijer I.A., Dion P., Laurent S., Dupre N., Brais B., Levert A., RA Puymirat J., Rioux M.F., Sylvain M., Zhu P.P., Soderblom C., Stadler J., RA Blackstone C., Rouleau G.A.; RT "Characterization of a novel SPG3A deletion in a French-Canadian family."; RL Ann. Neurol. 61:599-603(2007). RN [29] RP VARIANTS SPG3 GLU-154; CYS-239; ILE-253; VAL-413; TRP-415; THR-440 AND RP TRP-495. RX PubMed=20932283; DOI=10.1186/1471-2377-10-89; RA Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., RA Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., RA Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., RA Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.; RT "Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in Spanish RT patients with hereditary spastic paraplegia."; RL BMC Neurol. 10:89-89(2010). RN [30] RP VARIANTS HSN1D GLN-66 AND LYS-355, AND CHARACTERIZATION OF VARIANTS HSN1D RP GLN-66 AND LYS-355. RX PubMed=21194679; DOI=10.1016/j.ajhg.2010.12.003; RA Guelly C., Zhu P.P., Leonardis L., Papic L., Zidar J., Schabhuttl M., RA Strohmaier H., Weis J., Strom T.M., Baets J., Willems J., De Jonghe P., RA Reilly M.M., Frohlich E., Hatz M., Trajanoski S., Pieber T.R., RA Janecke A.R., Blackstone C., Auer-Grumbach M.; RT "Targeted high-throughput sequencing identifies mutations in atlastin-1 as RT a cause of hereditary sensory neuropathy type I."; RL Am. J. Hum. Genet. 88:99-105(2011). RN [31] RP VARIANT CYS-196, AND VARIANTS SPG3 CYS-239; ILE-253 AND TRP-495. RX PubMed=20718791; DOI=10.1111/j.1399-0004.2010.01501.x; RA McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., RA Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.; RT "Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic RT paraplegia."; RL Clin. Genet. 79:523-530(2011). RN [32] RP VARIANT SPG3 CYS-416. RX PubMed=21336785; DOI=10.1007/s00415-011-5934-z; RA Orlacchio A., Montieri P., Babalini C., Gaudiello F., Bernardi G., RA Kawarai T.; RT "Late-onset hereditary spastic paraplegia with thin corpus callosum caused RT by a new SPG3A mutation."; RL J. Neurol. 258:1361-1363(2011). RN [33] RP VARIANTS SPG3 GLN-415 AND TRP-415. RX PubMed=23483706; DOI=10.1002/humu.22309; RA Varga R.E., Schuele R., Fadel H., Valenzuela I., Speziani F., Gonzalez M., RA Rudenskaia G., Nuernberg G., Thiele H., Altmueller J., Alvarez V., RA Gamez J., Garbern J.Y., Nuernberg P., Zuchner S., Beetz C.; RT "Do not trust the pedigree: reduced and sex-dependent penetrance at a novel RT mutation hotspot in ATL1 blurs autosomal dominant inheritance of spastic RT paraplegia."; RL Hum. Mutat. 34:860-863(2013). RN [34] RP VARIANT SPG3 GLN-118. RX PubMed=24473461; DOI=10.1038/ejhg.2014.5; RA Khan T.N., Klar J., Tariq M., Anjum Baig S., Malik N.A., Yousaf R., RA Baig S.M., Dahl N.; RT "Evidence for autosomal recessive inheritance in SPG3A caused by RT homozygosity for a novel ATL1 missense mutation."; RL Eur. J. Hum. Genet. 22:1180-1184(2014). RN [35] RP VARIANT SPG3 ILE-253. RX PubMed=24604904; DOI=10.1136/jnnp-2013-306740; RA Klein C.J., Middha S., Duan X., Wu Y., Litchy W.J., Gu W., Dyck P.J., RA Gavrilova R.H., Smith D.I., Kocher J.P., Dyck P.J.; RT "Application of whole exome sequencing in undiagnosed inherited RT polyneuropathies."; RL J. Neurol. Neurosurg. Psych. 85:1265-1272(2014). 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:27619977). May also regulate Golgi biogenesis. May CC regulate axonal development. {ECO:0000269|PubMed:14506257, CC ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207, CC ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21220294, CC ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:25751282, CC ECO:0000269|PubMed:27619977}. CC -!- SUBUNIT: Monomer as apoprotein and in the GDP-bound form. Homodimer in CC the GTP-bound form. Interacts (via N-terminal region) with MAP4K4 (via CC CNH regulatory domain). Interacts with REEP5, RTN3 and RTN4 (via the CC transmembrane region). Interacts with SPAST; interaction is direct. May CC interact with TMED2. Interacts with REEP1. Interacts with CPT1C. CC Interacts with ARL6IP1 (By similarity). Interacts with ZFYVE27 CC (PubMed:23969831). {ECO:0000250|UniProtKB:Q6PST4, CC ECO:0000250|UniProtKB:Q8BH66, ECO:0000269|PubMed:12387898, CC ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, CC ECO:0000269|PubMed:16815977, ECO:0000269|PubMed:17321752, CC ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:20200447, CC ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:21368113, CC ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:23969831}. CC -!- INTERACTION: CC Q8WXF7; Q8WXF7: ATL1; NbExp=13; IntAct=EBI-2410266, EBI-2410266; CC Q8WXF7; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-2410266, EBI-1045797; CC Q8WXF7; P50570-2: DNM2; NbExp=3; IntAct=EBI-2410266, EBI-10968534; CC Q8WXF7; P42858: HTT; NbExp=18; IntAct=EBI-2410266, EBI-466029; CC Q8WXF7; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2410266, EBI-1055254; CC Q8WXF7; P02545: LMNA; NbExp=3; IntAct=EBI-2410266, EBI-351935; CC Q8WXF7; P19404: NDUFV2; NbExp=3; IntAct=EBI-2410266, EBI-713665; CC Q8WXF7; P35240: NF2; NbExp=3; IntAct=EBI-2410266, EBI-1014472; CC Q8WXF7; Q96CV9: OPTN; NbExp=3; IntAct=EBI-2410266, EBI-748974; CC Q8WXF7; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-2410266, EBI-25929070; CC Q8WXF7; O00628-2: PEX7; NbExp=3; IntAct=EBI-2410266, EBI-25882083; CC Q8WXF7; P50897: PPT1; NbExp=3; IntAct=EBI-2410266, EBI-1237011; CC Q8WXF7; P04156: PRNP; NbExp=3; IntAct=EBI-2410266, EBI-977302; CC Q8WXF7; P41219: PRPH; NbExp=3; IntAct=EBI-2410266, EBI-752074; CC Q8WXF7; P51149: RAB7A; NbExp=3; IntAct=EBI-2410266, EBI-1056089; CC Q8WXF7; Q9NQC3-1: RTN4; NbExp=2; IntAct=EBI-2410266, EBI-715972; CC Q8WXF7; Q16637: SMN2; NbExp=3; IntAct=EBI-2410266, EBI-395421; CC Q8WXF7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2410266, EBI-5235340; CC Q8WXF7; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2410266, EBI-12806590; CC Q8WXF7; P54577: YARS1; NbExp=3; IntAct=EBI-2410266, EBI-1048893; CC Q8WXF7; Q5T4F4: ZFYVE27; NbExp=6; IntAct=EBI-2410266, EBI-3892947; CC Q8WXF7; Q60870: Reep5; Xeno; NbExp=2; IntAct=EBI-2410266, EBI-2410304; CC Q8WXF7; Q9ES97-3: Rtn3; Xeno; NbExp=3; IntAct=EBI-2410266, EBI-1487798; CC Q8WXF7; Q9JK11-3: Rtn4; Xeno; NbExp=2; IntAct=EBI-2410266, EBI-920002; CC Q8WXF7-1; Q8WXF7-1: ATL1; NbExp=4; IntAct=EBI-15590227, EBI-15590227; CC Q8WXF7-1; Q9UBP0: SPAST; NbExp=4; IntAct=EBI-15590227, EBI-1222832; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, CC ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:19665976, CC ECO:0000269|PubMed:27619977}; Multi-pass membrane protein CC {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, CC ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:19665976}. Golgi CC apparatus membrane {ECO:0000269|PubMed:14506257, CC ECO:0000269|PubMed:17321752}; Multi-pass membrane protein CC {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752}. Cell CC projection, axon {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to CC endoplasmic reticulum tubular network (PubMed:27619977). CC {ECO:0000269|PubMed:27619977}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WXF7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WXF7-2; Sequence=VSP_044864; CC -!- TISSUE SPECIFICITY: Expressed predominantly in the adult and fetal CC central nervous system. Measurable expression in all tissues examined, CC although expression in adult brain is at least 50-fold higher than in CC other tissues. Detected predominantly in pyramidal neurons in the CC cerebral cortex and the hippocampus of the brain. Expressed in upper CC and lower motor neurons (at protein level). CC {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, CC ECO:0000269|PubMed:18270207}. CC -!- DISEASE: Spastic paraplegia 3, autosomal dominant (SPG3) [MIM:182600]: CC A form of spastic paraplegia, a neurodegenerative disorder CC characterized by a slow, gradual, progressive weakness and spasticity CC of the lower limbs. Rate of progression and the severity of symptoms CC are quite variable. Initial symptoms may include difficulty with CC balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. CC {ECO:0000269|PubMed:11685207, ECO:0000269|PubMed:12112092, CC ECO:0000269|PubMed:12939451, ECO:0000269|PubMed:14695538, CC ECO:0000269|PubMed:15184642, ECO:0000269|PubMed:16533974, CC ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:17427918, CC ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283, CC ECO:0000269|PubMed:21336785, ECO:0000269|PubMed:23483706, CC ECO:0000269|PubMed:24473461, ECO:0000269|PubMed:24604904}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Neuropathy, hereditary sensory, 1D (HSN1D) [MIM:613708]: A CC disease characterized by adult-onset distal axonal sensory neuropathy CC leading to mutilating ulcerations as well as hyporeflexia. Some CC patients may show features suggesting upper neuron involvement. CC {ECO:0000269|PubMed:21194679}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU01052}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD20047.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAK51160.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY032844; AAK51160.1; ALT_INIT; mRNA. DR EMBL; AF444143; AAL37898.1; -; mRNA. DR EMBL; AK290185; BAF82874.1; -; mRNA. DR EMBL; AL833591; CAH10392.1; -; mRNA. DR EMBL; AL118556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471078; EAW65705.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65706.1; -; Genomic_DNA. DR EMBL; BC010708; AAH10708.2; -; mRNA. DR EMBL; AF131801; AAD20047.1; ALT_INIT; mRNA. DR CCDS; CCDS32077.1; -. [Q8WXF7-2] DR CCDS; CCDS9700.1; -. [Q8WXF7-1] DR RefSeq; NP_001121185.1; NM_001127713.1. [Q8WXF7-2] DR RefSeq; NP_056999.2; NM_015915.4. [Q8WXF7-1] DR RefSeq; NP_853629.2; NM_181598.3. [Q8WXF7-2] DR PDB; 3Q5D; X-ray; 2.70 A; A=1-447. DR PDB; 3Q5E; X-ray; 3.01 A; A/C/E/G=1-447. DR PDB; 3QNU; X-ray; 2.80 A; A=18-447. DR PDB; 3QOF; X-ray; 2.80 A; A/B/C/D=18-447. DR PDB; 4IDN; X-ray; 2.25 A; A/B=1-446. DR PDB; 4IDO; X-ray; 2.09 A; A/B=1-446. DR PDB; 4IDP; X-ray; 2.59 A; A/B/C/D=1-446. DR PDB; 4IDQ; X-ray; 2.30 A; A/B/C/D=1-446. DR PDB; 6B9D; X-ray; 1.95 A; A/B=1-446. DR PDB; 6B9E; X-ray; 1.99 A; A/B=1-446. DR PDB; 6B9F; X-ray; 1.90 A; A/B=1-446. DR PDB; 6B9G; X-ray; 3.00 A; A/B/C/D=1-339. DR PDB; 6XJN; X-ray; 2.20 A; A=1-439. DR PDB; 7OL3; X-ray; 1.90 A; A/B=1-449. DR PDBsum; 3Q5D; -. DR PDBsum; 3Q5E; -. DR PDBsum; 3QNU; -. DR PDBsum; 3QOF; -. DR PDBsum; 4IDN; -. DR PDBsum; 4IDO; -. DR PDBsum; 4IDP; -. DR PDBsum; 4IDQ; -. DR PDBsum; 6B9D; -. DR PDBsum; 6B9E; -. DR PDBsum; 6B9F; -. DR PDBsum; 6B9G; -. DR PDBsum; 6XJN; -. DR PDBsum; 7OL3; -. DR AlphaFoldDB; Q8WXF7; -. DR SMR; Q8WXF7; -. DR BioGRID; 119254; 57. DR CORUM; Q8WXF7; -. DR DIP; DIP-53502N; -. DR IntAct; Q8WXF7; 32. DR MINT; Q8WXF7; -. DR STRING; 9606.ENSP00000351155; -. DR TCDB; 1.N.5.1.1; the endoplasmic reticulum fusion gtpase, atlastin (atlastin) family. DR iPTMnet; Q8WXF7; -. DR PhosphoSitePlus; Q8WXF7; -. DR SwissPalm; Q8WXF7; -. DR BioMuta; ATL1; -. DR DMDM; 37999727; -. DR EPD; Q8WXF7; -. DR jPOST; Q8WXF7; -. DR MassIVE; Q8WXF7; -. DR MaxQB; Q8WXF7; -. DR PaxDb; 9606-ENSP00000351155; -. DR PeptideAtlas; Q8WXF7; -. DR ProteomicsDB; 34035; -. DR ProteomicsDB; 75028; -. [Q8WXF7-1] DR Pumba; Q8WXF7; -. DR Antibodypedia; 23673; 268 antibodies from 29 providers. DR DNASU; 51062; -. DR Ensembl; ENST00000358385.12; ENSP00000351155.7; ENSG00000198513.14. [Q8WXF7-1] DR Ensembl; ENST00000441560.6; ENSP00000413675.2; ENSG00000198513.14. [Q8WXF7-2] DR Ensembl; ENST00000553509.2; ENSP00000450989.2; ENSG00000198513.14. [Q8WXF7-2] DR Ensembl; ENST00000556478.3; ENSP00000501428.2; ENSG00000198513.14. [Q8WXF7-2] DR GeneID; 51062; -. DR KEGG; hsa:51062; -. DR MANE-Select; ENST00000358385.12; ENSP00000351155.7; NM_015915.5; NP_056999.2. DR UCSC; uc001wyd.5; human. [Q8WXF7-1] DR AGR; HGNC:11231; -. DR CTD; 51062; -. DR DisGeNET; 51062; -. DR GeneCards; ATL1; -. DR GeneReviews; ATL1; -. DR HGNC; HGNC:11231; ATL1. DR HPA; ENSG00000198513; Tissue enhanced (brain). DR MalaCards; ATL1; -. DR MIM; 182600; phenotype. DR MIM; 606439; gene. DR MIM; 613708; phenotype. DR neXtProt; NX_Q8WXF7; -. DR OpenTargets; ENSG00000198513; -. DR Orphanet; 100984; Autosomal dominant spastic paraplegia type 3. DR Orphanet; 36386; Hereditary sensory and autonomic neuropathy type 1. DR PharmGKB; PA36061; -. DR VEuPathDB; HostDB:ENSG00000198513; -. DR eggNOG; KOG2037; Eukaryota. DR GeneTree; ENSGT00940000158704; -. DR HOGENOM; CLU_021447_2_0_1; -. DR InParanoid; Q8WXF7; -. DR OMA; GFIHNIW; -. DR OrthoDB; 102682at2759; -. DR PhylomeDB; Q8WXF7; -. DR TreeFam; TF105251; -. DR PathwayCommons; Q8WXF7; -. DR SignaLink; Q8WXF7; -. DR BioGRID-ORCS; 51062; 29 hits in 1151 CRISPR screens. DR ChiTaRS; ATL1; human. DR EvolutionaryTrace; Q8WXF7; -. DR GeneWiki; Atlastin; -. DR GenomeRNAi; 51062; -. DR Pharos; Q8WXF7; Tbio. DR PRO; PR:Q8WXF7; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q8WXF7; Protein. DR Bgee; ENSG00000198513; Expressed in middle temporal gyrus and 172 other cell types or tissues. DR ExpressionAtlas; Q8WXF7; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB. DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB. DR GO; GO:0007029; P:endoplasmic reticulum organization; IDA:UniProtKB. DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR CDD; cd01851; GBP; 1. DR Gene3D; 1.20.58.420; AHSP; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR10751:SF15; ATLASTIN-1; 1. DR PANTHER; PTHR10751; GUANYLATE BINDING PROTEIN; 1. DR Pfam; PF02263; GBP; 1. DR SUPFAM; SSF48340; Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51715; G_GB1_RHD3; 1. DR Genevisible; Q8WXF7; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell projection; KW Coiled coil; Disease variant; Endoplasmic reticulum; Golgi apparatus; KW GTP-binding; Hereditary spastic paraplegia; Hydrolase; Membrane; KW Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..558 FT /note="Atlastin-1" FT /id="PRO_0000190971" FT TOPO_DOM 1..449 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:14506257" FT TRANSMEM 450..470 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 471 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 472..492 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 493..558 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:14506257" FT DOMAIN 64..309 FT /note="GB1/RHD3-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..558 FT /note="Sufficient for membrane association" FT COILED 412..439 FT /evidence="ECO:0000255" FT BINDING 74..81 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 118..120 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 217..218 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 276..279 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BH66" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BH66" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BH66" FT MOD_RES 395 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6DD88" FT VAR_SEQ 518..522 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_044864" FT VARIANT 43 FT /note="D -> E (in dbSNP:rs17850684)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058963" FT VARIANT 66 FT /note="E -> Q (in HSN1D; shows no significant changes in FT GTPase activity and no changes in endoplasmic reticulum FT morphology; dbSNP:rs200314808)" FT /evidence="ECO:0000269|PubMed:21194679" FT /id="VAR_065508" FT VARIANT 118 FT /note="R -> Q (in SPG3; dbSNP:rs606231265)" FT /evidence="ECO:0000269|PubMed:24473461" FT /id="VAR_071874" FT VARIANT 154 FT /note="Q -> E (in SPG3)" FT /evidence="ECO:0000269|PubMed:20932283" FT /id="VAR_067655" FT VARIANT 157 FT /note="L -> W (in SPG3; dbSNP:rs119476051)" FT /evidence="ECO:0000269|PubMed:16533974" FT /id="VAR_065509" FT VARIANT 161 FT /note="A -> P (in SPG3; affects endoplasmic reticulum and FT Golgi morphology)" FT /evidence="ECO:0000269|PubMed:14695538, FT ECO:0000269|PubMed:17321752" FT /id="VAR_019446" FT VARIANT 193 FT /note="F -> C (in dbSNP:rs17850683)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058964" FT VARIANT 196 FT /note="Y -> C (in a patient with hereditary spastic FT paraplegia; uncertain significance; no effect on FT homodimerization and GTPase activity; dbSNP:rs1555364246)" FT /evidence="ECO:0000269|PubMed:20718791, FT ECO:0000269|PubMed:21220294" FT /id="VAR_067656" FT VARIANT 217 FT /note="R -> Q (in SPG3; abolishes homodimerization and FT GTPase activity and alters endoplasmic reticulum FT morphology; dbSNP:rs119476049)" FT /evidence="ECO:0000269|PubMed:12112092, FT ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:21220294, FT ECO:0000269|PubMed:27619977" FT /id="VAR_017146" FT VARIANT 239 FT /note="R -> C (in SPG3; affects endoplasmic reticulum and FT Golgi morphology; dbSNP:rs119476046)" FT /evidence="ECO:0000269|PubMed:11685207, FT ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:20718791, FT ECO:0000269|PubMed:20932283" FT /id="VAR_017147" FT VARIANT 247 FT /note="H -> P (in SPG3)" FT /evidence="ECO:0000269|PubMed:14695538" FT /id="VAR_019447" FT VARIANT 253 FT /note="V -> I (in SPG3; dbSNP:rs864622520)" FT /evidence="ECO:0000269|PubMed:20718791, FT ECO:0000269|PubMed:20932283, ECO:0000269|PubMed:24604904" FT /id="VAR_067657" FT VARIANT 258 FT /note="H -> R (in SPG3; dbSNP:rs119476048)" FT /evidence="ECO:0000269|PubMed:11685207" FT /id="VAR_017148" FT VARIANT 259 FT /note="S -> Y (in SPG3; dbSNP:rs119476047)" FT /evidence="ECO:0000269|PubMed:11685207" FT /id="VAR_017149" FT VARIANT 355 FT /note="N -> K (in HSN1D; the mutant protein has decreased FT GTPase activity compared to wild-type and causes disruption FT of endoplasmic reticulum network morphology; FT dbSNP:rs1555365597)" FT /evidence="ECO:0000269|PubMed:21194679" FT /id="VAR_065510" FT VARIANT 408 FT /note="M -> V (in SPG3; dbSNP:rs28939094)" FT /evidence="ECO:0000269|PubMed:12939451" FT /id="VAR_065511" FT VARIANT 413 FT /note="F -> V (in SPG3)" FT /evidence="ECO:0000269|PubMed:20932283" FT /id="VAR_067658" FT VARIANT 415 FT /note="R -> Q (in SPG3; dbSNP:rs397514712)" FT /evidence="ECO:0000269|PubMed:23483706" FT /id="VAR_071708" FT VARIANT 415 FT /note="R -> W (in SPG3; dbSNP:rs119476050)" FT /evidence="ECO:0000269|PubMed:15184642, FT ECO:0000269|PubMed:20932283, ECO:0000269|PubMed:23483706" FT /id="VAR_065512" FT VARIANT 416 FT /note="R -> C (in SPG3; dbSNP:rs387906941)" FT /evidence="ECO:0000269|PubMed:21336785" FT /id="VAR_071709" FT VARIANT 436 FT /note="Missing (in SPG3; does not affect GTPase activity; FT does not affect interaction with SPAST; patients' FT lymphoblasts show decreased protein levels but normal FT levels of mRNA; dbSNP:rs1595625206)" FT /evidence="ECO:0000269|PubMed:17427918" FT /id="VAR_065513" FT VARIANT 440 FT /note="N -> T (in SPG3)" FT /evidence="ECO:0000269|PubMed:20932283" FT /id="VAR_067659" FT VARIANT 495 FT /note="R -> W (in SPG3; affects endoplasmic reticulum and FT Golgi morphology; dbSNP:rs864622269)" FT /evidence="ECO:0000269|PubMed:17321752, FT ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283" FT /id="VAR_067660" FT MUTAGEN 77 FT /note="R->A: Abolishes GTPase activity and impairs FT homodimerization." FT /evidence="ECO:0000269|PubMed:21220294, FT ECO:0000269|PubMed:23334294" FT MUTAGEN 77 FT /note="R->E: Abolishes homodimerization." FT /evidence="ECO:0000269|PubMed:21220294, FT ECO:0000269|PubMed:23334294" FT MUTAGEN 80 FT /note="K->A: Alters endoplasmic reticulum morphogenesis." FT /evidence="ECO:0000269|PubMed:18270207, FT ECO:0000269|PubMed:27619977" FT MUTAGEN 151 FT /note="F->S: Affects endoplasmic reticulum and Golgi FT morphology." FT /evidence="ECO:0000269|PubMed:17321752" FT MUTAGEN 162 FT /note="T->P: Affects endoplasmic reticulum and Golgi FT morphology." FT /evidence="ECO:0000269|PubMed:17321752" FT MUTAGEN 191 FT /note="Q->R: Abolishes homodimerization." FT /evidence="ECO:0000269|PubMed:21220294" FT MUTAGEN 247 FT /note="H->R: Impairs homodimerization and GTPase activity." FT /evidence="ECO:0000269|PubMed:21220294" FT MUTAGEN 398 FT /note="S->Y: Affects endoplasmic reticulum and Golgi FT morphology." FT /evidence="ECO:0000269|PubMed:17321752" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:6XJN" FT STRAND 23..30 FT /evidence="ECO:0007829|PDB:6XJN" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:3QOF" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 50..57 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 60..64 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 65..79 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:6B9D" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 122..128 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:3Q5D" FT STRAND 139..147 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:6XJN" FT HELIX 157..170 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 172..181 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 184..199 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 208..217 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 229..240 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:6XJN" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 261..268 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:6B9G" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 291..305 FT /evidence="ECO:0007829|PDB:6B9F" FT TURN 307..309 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 322..337 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 347..375 FT /evidence="ECO:0007829|PDB:6B9F" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:3Q5D" FT HELIX 384..404 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 410..437 FT /evidence="ECO:0007829|PDB:6B9F" FT HELIX 443..446 FT /evidence="ECO:0007829|PDB:6B9F" SQ SEQUENCE 558 AA; 63544 MW; 68A33C39DD43504C CRC64; MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLIV KDDHSFELDE TALNRILLSE AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET TGIQIWSEIF LINKPDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL IPWLLSPESL DIKEINGNKI TCRGLVEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ AFPTPKSEST EQSEKKKM //