ID   ATLA1_MOUSE             Reviewed;         558 AA.
AC   Q8BH66; Q8BJH5;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Atlastin-1;
DE            EC=3.6.5.-;
DE   AltName: Full=Spastic paraplegia 3A homolog;
GN   Name=Atl1; Synonyms=Spg3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Liver, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   INTERACTION WITH REEP5 AND RTN3.
RX   PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA   Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA   Rapoport T.A., Blackstone C.;
RT   "A class of dynamin-like GTPases involved in the generation of the tubular
RT   ER network.";
RL   Cell 138:549-561(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-22 AND SER-23, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE27.
RX   PubMed=24668814; DOI=10.1074/jbc.m113.528687;
RA   Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T.,
RA   Nakayama K.I.;
RT   "Protrudin regulates endoplasmic reticulum morphology and function
RT   associated with the pathogenesis of hereditary spastic paraplegia.";
RL   J. Biol. Chem. 289:12946-12961(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. May also regulate Golgi biogenesis. May regulate axonal
CC       development. {ECO:0000250|UniProtKB:Q8WXF7}.
CC   -!- SUBUNIT: Monomer as apoprotein and in the GDP-bound form. Homodimer in
CC       the GTP-bound form. Homooligomer. Interacts (via N-terminal region)
CC       with MAP4K4 (via CNH regulatory domain). Interacts with SPAST;
CC       interaction is direct (By similarity). Interacts with REEP5, RTN3 and
CC       probably RTN4 (via the transmembrane region) (PubMed:19665976).
CC       Interacts with REEP1. Interacts with CPT1C. Interacts with ARL6IP1 (By
CC       similarity). Interacts with ZFYVE27 (PubMed:24668814).
CC       {ECO:0000250|UniProtKB:Q6PST4, ECO:0000250|UniProtKB:Q8WXF7,
CC       ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:24668814}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8WXF7}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8WXF7}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum
CC       tubular network. {ECO:0000269|PubMed:24668814}.
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   ---------------------------------------------------------------------------
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; AK046919; BAC32920.1; -; mRNA.
DR   EMBL; AK050339; BAC34198.1; -; mRNA.
DR   EMBL; BC050784; AAH50784.1; -; mRNA.
DR   EMBL; AK083918; BAC39062.1; -; mRNA.
DR   CCDS; CCDS36465.1; -.
DR   RefSeq; NP_848743.1; NM_178628.5.
DR   AlphaFoldDB; Q8BH66; -.
DR   SMR; Q8BH66; -.
DR   BioGRID; 216409; 8.
DR   IntAct; Q8BH66; 2.
DR   MINT; Q8BH66; -.
DR   STRING; 10090.ENSMUSP00000021466; -.
DR   GlyGen; Q8BH66; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BH66; -.
DR   PhosphoSitePlus; Q8BH66; -.
DR   SwissPalm; Q8BH66; -.
DR   EPD; Q8BH66; -.
DR   jPOST; Q8BH66; -.
DR   MaxQB; Q8BH66; -.
DR   PaxDb; 10090-ENSMUSP00000021466; -.
DR   PeptideAtlas; Q8BH66; -.
DR   ProteomicsDB; 265151; -.
DR   Pumba; Q8BH66; -.
DR   Antibodypedia; 23673; 268 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000021466.10; ENSMUSP00000021466.9; ENSMUSG00000021066.10.
DR   GeneID; 73991; -.
DR   KEGG; mmu:73991; -.
DR   UCSC; uc007nsy.2; mouse.
DR   AGR; MGI:1921241; -.
DR   CTD; 51062; -.
DR   MGI; MGI:1921241; Atl1.
DR   VEuPathDB; HostDB:ENSMUSG00000021066; -.
DR   eggNOG; KOG2037; Eukaryota.
DR   GeneTree; ENSGT00940000158704; -.
DR   HOGENOM; CLU_021447_2_0_1; -.
DR   InParanoid; Q8BH66; -.
DR   OMA; GFIHNIW; -.
DR   OrthoDB; 102682at2759; -.
DR   PhylomeDB; Q8BH66; -.
DR   TreeFam; TF105251; -.
DR   BioGRID-ORCS; 73991; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Atl1; mouse.
DR   PRO; PR:Q8BH66; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8BH66; Protein.
DR   Bgee; ENSMUSG00000021066; Expressed in dorsomedial nucleus of hypothalamus and 216 other cell types or tissues.
DR   ExpressionAtlas; Q8BH66; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR   GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR   GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS: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; Q8BH66; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell projection; Coiled coil; Endoplasmic reticulum;
KW   Golgi apparatus; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..558
FT                   /note="Atlastin-1"
FT                   /id="PRO_0000190973"
FT   TOPO_DOM        1..449
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
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:0000250"
FT   DOMAIN          64..309
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..558
FT                   /note="Sufficient for membrane association"
FT                   /evidence="ECO:0000250"
FT   COILED          412..439
FT                   /evidence="ECO:0000255"
FT   BINDING         74..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..218
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..279
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         395
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD88"
SQ   SEQUENCE   558 AA;  63377 MW;  4734A5D99A9171AC CRC64;
     MAKSRRDRNS WGGFSEKSSD WSSEEEEPVR KAGPVQVLIV KDDHSFELDE AALNRILLSQ
     AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET
     TGIQIWSEVF LINKLDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ
     NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL
     KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
     IPWLLSPERL DIKEINGNKI TCRGLLEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV
     ATAKDTYNKK MEEVCGGDKP FLAPNDLQSK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ
     LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI
     MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLCHQ
     AFPAPKSEPT QQPEKKKI
//