ATLA1_HUMAN
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 03-AUG-2022, entry version 175.
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};
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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; 47.
DR CORUM; Q8WXF7; -.
DR DIP; DIP-53502N; -.
DR IntAct; Q8WXF7; 31.
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; Q8WXF7; -.
DR PeptideAtlas; Q8WXF7; -.
DR PRIDE; Q8WXF7; -.
DR ProteomicsDB; 34035; -.
DR ProteomicsDB; 75028; -. [Q8WXF7-1]
DR Antibodypedia; 23673; 247 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 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 PhylomeDB; Q8WXF7; -.
DR TreeFam; TF105251; -.
DR PathwayCommons; Q8WXF7; -.
DR SignaLink; Q8WXF7; -.
DR BioGRID-ORCS; 51062; 29 hits in 1071 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 170 other tissues.
DR ExpressionAtlas; Q8WXF7; baseline and differential.
DR Genevisible; Q8WXF7; HS.
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:0016021; C:integral component of 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 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 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; unknown pathological 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
