ID   ATLA3_HUMAN             Reviewed;         541 AA.
AC   Q6DD88; Q8N7W5; Q9H8Q5; Q9UFL1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   28-JAN-2026, entry version 160.
DE   RecName: Full=Atlastin-3 {ECO:0000303|PubMed:14506257};
DE            Short=AT3 {ECO:0000303|PubMed:18270207};
DE            Short=ATL-3 {ECO:0000303|PubMed:27619977};
DE            EC=3.6.5.- {ECO:0000269|PubMed:37102997};
GN   Name=ATL3 {ECO:0000312|HGNC:HGNC:24526};
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary, 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   FUNCTION, TOPOLOGY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73
RP   AND ARG-213, 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   [7]
RP   FUNCTION, 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [11]
RP   INTERACTION WITH ZFYVE27, AND SUBCELLULAR LOCATION.
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   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HSN1F CYS-192,
RP   AND CHARACTERIZATION OF VARIANT HSN1F CYS-192.
RX   PubMed=24459106; DOI=10.1093/brain/awt357;
RA   Kornak U., Mademan I., Schinke M., Voigt M., Krawitz P., Hecht J.,
RA   Barvencik F., Schinke T., Giesselmann S., Beil F.T., Pou-Serradell A.,
RA   Vilchez J.J., Beetz C., Deconinck T., Timmerman V., Kaether C.,
RA   De Jonghe P., Huebner C.A., Gal A., Amling M., Mundlos S., Baets J.,
RA   Kurth I.;
RT   "Sensory neuropathy with bone destruction due to a mutation in the
RT   membrane-shaping atlastin GTPase 3.";
RL   Brain 137:683-692(2014).
RN   [13]
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   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25548161; DOI=10.1073/pnas.1423026112;
RA   Chen S., Desai T., McNew J.A., Gerard P., Novick P.J., Ferro-Novick S.;
RT   "Lunapark stabilizes nascent three-way junctions in the endoplasmic
RT   reticulum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:418-423(2015).
RN   [15]
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   [16]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-73 AND ARG-213.
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   [17]
RP   INTERACTION WITH REEP5.
RX   PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA   Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA   Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA   Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA   Scott I.C., Gramolini A.O.;
RT   "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT   cardiac functional defects.";
RL   Nat. Commun. 11:965-965(2020).
RN   [18]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-70;
RP   PRO-338 AND ILE-503, AND CHARACTERIZATION OF VARIANT HSN1F CYS-192.
RX   PubMed=37102997; DOI=10.1083/jcb.202211021;
RA   Bryce S., Stolzer M., Crosby D., Yang R., Durand D., Lee T.H.;
RT   "Human atlastin-3 is a constitutive ER membrane fusion catalyst.";
RL   J. Cell Biol. 222:0-0(2023).
RN   [19] {ECO:0007744|PDB:5VGR}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 21-442 IN COMPLEX WITH GDP,
RP   CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ARG-109.
RX   PubMed=28602821; DOI=10.1016/j.str.2017.05.007;
RA   O'Donnell J.P., Cooley R.B., Kelly C.M., Miller K., Andersen O.S.,
RA   Rusinova R., Sondermann H.;
RT   "Timing and Reset Mechanism of GTP Hydrolysis-Driven Conformational Changes
RT   of Atlastin.";
RL   Structure 25:997-1010.e4(2017).
RN   [20] {ECO:0007744|PDB:6XJO}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-334 IN COMPLEX WITH GDP AND
RP   MG(2+), CATALYTIC ACTIVITY, SUBUNIT, AND REGION.
RX   PubMed=34546351; DOI=10.1083/jcb.202104128;
RA   Kelly C.M., Byrnes L.J., Neela N., Sondermann H., O'Donnell J.P.;
RT   "The hypervariable region of atlastin-1 is a site for intrinsic and
RT   extrinsic regulation.";
RL   J. Cell Biol. 220:e202104128-e202104128(2021).
CC   -!- FUNCTION: Atlastin-3 (ATL3) is a membrane-anchored GTPase that mediates
CC       the GTP-dependent fusion of endoplasmic reticulum (ER) membranes,
CC       maintaining the continuous ER network. It facilitates the formation of
CC       three-way junctions where ER tubules intersect (PubMed:18270207,
CC       PubMed:19665976, PubMed:24459106, PubMed:27619977, PubMed:37102997).
CC       Two atlastin-3 on neighboring ER tubules bind GTP and form loose
CC       homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon
CC       GTP hydrolysis, the 3HB regions tighten, pulling the membranes together
CC       to drive their fusion. After fusion, the homodimer disassembles upon
CC       release of inorganic phosphate (Pi). Subsequently, GDP dissociates,
CC       resetting the monomers to a conformation ready for a new fusion cycle
CC       (By similarity). {ECO:0000250|UniProtKB:Q8WXF7,
CC       ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976,
CC       ECO:0000269|PubMed:24459106, ECO:0000269|PubMed:27619977,
CC       ECO:0000269|PubMed:37102997}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:28602821, ECO:0000269|PubMed:34546351,
CC         ECO:0000269|PubMed:37102997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000305|PubMed:37102997};
CC   -!- SUBUNIT: Monomeric and homodimeric. The homodimer, transiently formed
CC       by two molecules on opposing membranes, is the active form mediating ER
CC       membrane fusion (PubMed:18270207, PubMed:34546351). Interacts with
CC       ZFYVE27; both proteins are involved in endoplasmic reticulum tubular
CC       network organization (PubMed:23969831). Interacts with REEP5; both
CC       proteins are involved in endoplasmic reticulum tubular network
CC       organization (PubMed:32075961). {ECO:0000269|PubMed:18270207,
CC       ECO:0000269|PubMed:23969831, ECO:0000269|PubMed:32075961,
CC       ECO:0000269|PubMed:34546351}.
CC   -!- INTERACTION:
CC       Q6DD88; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-6165882, EBI-3892947;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976,
CC       ECO:0000269|PubMed:23969831, ECO:0000269|PubMed:24459106,
CC       ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977,
CC       ECO:0000269|PubMed:37102997}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18270207}. Note=Localizes to endoplasmic reticulum
CC       tubules and accumulates in punctuate structures corresponding to 3-way
CC       junctions, which represent crossing-points at which the tubules build a
CC       polygonal network. {ECO:0000269|PubMed:23969831,
CC       ECO:0000269|PubMed:24459106, ECO:0000269|PubMed:27619977}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central nervous system and in
CC       dorsal root ganglia neurons. Expressed in peripheral tissues (at
CC       protein level). {ECO:0000269|PubMed:18270207,
CC       ECO:0000269|PubMed:24459106}.
CC   -!- DOMAIN: The GB1/RHD3-type G domain mediates GTP-binding and hydrolysis
CC       as well as homodimerization. {ECO:0000269|PubMed:28602821}.
CC   -!- DOMAIN: The two three-helix bundle (3HB) regions in the homodimer are
CC       loosely associated initially, but they tighten upon GTP hydrolysis,
CC       facilitating the fusion of membranes. {ECO:0000250|UniProtKB:Q8WXF7}.
CC   -!- DISEASE: Neuropathy, hereditary sensory, 1F (HSN1F) [MIM:615632]: An
CC       autosomal dominant sensory neuropathy affecting the lower limbs. Distal
CC       sensory impairment becomes apparent during the second or third decade
CC       of life, resulting in painless ulceration of the feet with poor
CC       healing, which can progress to osteomyelitis, bone destruction, and
CC       amputation. There is no autonomic involvement, spasticity, or cognitive
CC       impairment. {ECO:0000269|PubMed:24459106, ECO:0000269|PubMed:37102997}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       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=BAC05111.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AK097588; BAC05111.1; ALT_SEQ; mRNA.
DR   EMBL; AK023383; BAB14552.1; -; mRNA.
DR   EMBL; AL117600; CAB56010.2; -; mRNA.
DR   EMBL; BC077727; AAH77727.1; -; mRNA.
DR   CCDS; CCDS41663.1; -.
DR   PIR; T17320; T17320.
DR   RefSeq; NP_001276977.1; NM_001290048.1.
DR   RefSeq; NP_056274.3; NM_015459.4.
DR   PDB; 5VGR; X-ray; 2.10 A; A/B=21-442.
DR   PDB; 6XJO; X-ray; 2.10 A; A/B=1-334.
DR   PDBsum; 5VGR; -.
DR   PDBsum; 6XJO; -.
DR   AlphaFoldDB; Q6DD88; -.
DR   SMR; Q6DD88; -.
DR   BioGRID; 117423; 240.
DR   CORUM; Q6DD88; -.
DR   FunCoup; Q6DD88; 1859.
DR   IntAct; Q6DD88; 136.
DR   MINT; Q6DD88; -.
DR   STRING; 9606.ENSP00000381844; -.
DR   TCDB; 1.N.5.1.7; the endoplasmic reticulum fusion gtpase, atlastin (atlastin) family.
DR   GlyGen; Q6DD88; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q6DD88; -.
DR   MetOSite; Q6DD88; -.
DR   PhosphoSitePlus; Q6DD88; -.
DR   SwissPalm; Q6DD88; -.
DR   BioMuta; ATL3; -.
DR   DMDM; 74736374; -.
DR   jPOST; Q6DD88; -.
DR   MassIVE; Q6DD88; -.
DR   PaxDb; 9606-ENSP00000381844; -.
DR   PeptideAtlas; Q6DD88; -.
DR   PRIDE; Q6DD88; -.
DR   ProteomicsDB; 66223; -.
DR   Pumba; Q6DD88; -.
DR   TopDownProteomics; Q6DD88; -.
DR   Antibodypedia; 28987; 232 antibodies from 27 providers.
DR   DNASU; 25923; -.
DR   Ensembl; ENST00000398868.8; ENSP00000381844.3; ENSG00000184743.14.
DR   GeneID; 25923; -.
DR   KEGG; hsa:25923; -.
DR   MANE-Select; ENST00000398868.8; ENSP00000381844.3; NM_015459.5; NP_056274.3.
DR   UCSC; uc001nxk.2; human.
DR   AGR; HGNC:24526; -.
DR   ClinPGx; PA164716353; -.
DR   CTD; 25923; -.
DR   DisGeNET; 25923; -.
DR   GeneCards; ATL3; -.
DR   HGNC; HGNC:24526; ATL3.
DR   HPA; ENSG00000184743; Low tissue specificity.
DR   MalaCards; ATL3; -.
DR   MIM; 609369; gene.
DR   MIM; 615632; phenotype.
DR   OpenTargets; ENSG00000184743; -.
DR   Orphanet; 36386; Hereditary sensory and autonomic neuropathy type 1.
DR   VEuPathDB; HostDB:ENSG00000184743; -.
DR   eggNOG; KOG2037; Eukaryota.
DR   GeneTree; ENSGT00940000158566; -.
DR   InParanoid; Q6DD88; -.
DR   OMA; QYQKNME; -.
DR   OrthoDB; 7788754at2759; -.
DR   PAN-GO; Q6DD88; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6DD88; -.
DR   PathwayCommons; Q6DD88; -.
DR   SignaLink; Q6DD88; -.
DR   Agora; ENSG00000184743; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 25923; 24 hits in 1161 CRISPR screens.
DR   ChiTaRS; ATL3; human.
DR   GenomeRNAi; 25923; -.
DR   Pharos; Q6DD88; Tbio.
DR   PRO; PR:Q6DD88; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q6DD88; protein.
DR   Bgee; ENSG00000184743; Expressed in upper arm skin and 199 other cell types or tissues.
DR   ExpressionAtlas; Q6DD88; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR   GO; GO:0098826; C:endoplasmic reticulum tubular network 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:0140523; F:GTPase-dependent fusogenic activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IDA:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR   GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IBA:GO_Central.
DR   CDD; cd01851; GBP; 1.
DR   DisProt; DP03688; -.
DR   FunFam; 1.20.58.420:FF:000001; Atlastin-1 isoform 1; 1.
DR   FunFam; 3.40.50.300:FF:000314; Atlastin-2 isoform 2; 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; 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   PANTHER; PTHR10751; GUANYLATE BINDING PROTEIN; 1.
DR   Pfam; PF02263; GBP; 1.
DR   Pfam; PF02841; GBP_C; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Endoplasmic reticulum;
KW   GTP-binding; Hydrolase; Magnesium; Membrane; Neuropathy;
KW   Nucleotide-binding; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..541
FT                   /note="Atlastin-3"
FT                   /id="PRO_0000287109"
FT   TOPO_DOM        1..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:18270207"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:18270207"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:18270207"
FT   DOMAIN          57..305
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..25
FT                   /note="N-terminal hypervariable region (HVR)"
FT                   /evidence="ECO:0000269|PubMed:34546351"
FT   REGION          343..434
FT                   /note="3HB (three-helix bundle) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF7"
FT   BINDING         70
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         71
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         72
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         73
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         74
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         75
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         109
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:34546351,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         213
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         214
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   BINDING         272
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR"
FT   BINDING         275
FT                   /ligand="GDP"
FT                   /ligand_id="ChEBI:CHEBI:58189"
FT                   /evidence="ECO:0000269|PubMed:28602821,
FT                   ECO:0000269|PubMed:34546351, ECO:0007744|PDB:5VGR,
FT                   ECO:0007744|PDB:6XJO"
FT   MOD_RES         391
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         192
FT                   /note="Y -> C (in HSN1F; loss of localization to
FT                   endoplasmic reticulum tubular network membrane; loss of
FT                   GTPase-dependent fusogenic activity; the mutant protein
FT                   accumulates in condensed structures near the nucleus and
FT                   localizes to unbranched tubules; has a dominant-negative
FT                   disruptive effect on the regular structure of the
FT                   endoplasmic reticulum; dbSNP:rs587777108)"
FT                   /evidence="ECO:0000269|PubMed:24459106,
FT                   ECO:0000269|PubMed:37102997"
FT                   /id="VAR_070973"
FT   MUTAGEN         70
FT                   /note="R->E: Loss of GTPase-dependent fusogenic activity."
FT                   /evidence="ECO:0000269|PubMed:37102997"
FT   MUTAGEN         73
FT                   /note="K->A: Changed endoplasmic reticulum tubular network
FT                   membrane organization."
FT                   /evidence="ECO:0000269|PubMed:18270207,
FT                   ECO:0000269|PubMed:27619977"
FT   MUTAGEN         109
FT                   /note="R->A: Decreased GTPase activity."
FT                   /evidence="ECO:0000269|PubMed:28602821"
FT   MUTAGEN         213
FT                   /note="R->Q: Changed endoplasmic reticulum tubular network
FT                   membrane organization."
FT                   /evidence="ECO:0000269|PubMed:18270207,
FT                   ECO:0000269|PubMed:27619977"
FT   MUTAGEN         338
FT                   /note="P->R: Loss of GTPase-dependent fusogenic activity."
FT                   /evidence="ECO:0000269|PubMed:37102997"
FT   MUTAGEN         503
FT                   /note="I->D: Loss of GTPase-dependent fusogenic activity."
FT                   /evidence="ECO:0000269|PubMed:37102997"
FT   CONFLICT        49
FT                   /note="I -> T (in Ref. 1; BAB14552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="T -> A (in Ref. 2; CAB56010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="N -> S (in Ref. 1; BAC05111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="Q -> R (in Ref. 2; CAB56010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="W -> R (in Ref. 2; CAB56010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="N -> Y (in Ref. 2; CAB56010)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..21
FT                   /evidence="ECO:0007829|PDB:6XJO"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:6XJO"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   TURN            53..57
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          58..68
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           73..88
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          135..145
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:6XJO"
FT   HELIX           157..166
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          168..177
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           180..184
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           187..200
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          204..213
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           225..235
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           244..250
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          257..264
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           270..273
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           282..284
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           287..301
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   TURN            303..305
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           318..331
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           340..371
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           380..400
FT                   /evidence="ECO:0007829|PDB:5VGR"
FT   HELIX           407..434
FT                   /evidence="ECO:0007829|PDB:5VGR"
SQ   SEQUENCE   541 AA;  60542 MW;  E5C58A53F93B42D0 CRC64;
     MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL LQDHIRDLDV
     VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE EPLTGFSWRG GSDPETTGIQ
     IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE
     DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE
     HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV
     LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK
     DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK TKKMGGKDFS FRYQQELEEE
     IKELYENFCK HNGSKNVFST FRTPAVLFTG IVALYIASGL TGFIGLEVVA QLFNCMVGLL
     LIALLTWGYI RYSGQYRELG GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA
     Q
//