ATLA1_MOUSE
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 03-AUG-2022, entry version 148.
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}.
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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; 4.
DR IntAct; Q8BH66; 2.
DR MINT; Q8BH66; -.
DR STRING; 10090.ENSMUSP00000021466; -.
DR iPTMnet; Q8BH66; -.
DR PhosphoSitePlus; Q8BH66; -.
DR SwissPalm; Q8BH66; -.
DR EPD; Q8BH66; -.
DR jPOST; Q8BH66; -.
DR MaxQB; Q8BH66; -.
DR PaxDb; Q8BH66; -.
DR PeptideAtlas; Q8BH66; -.
DR PRIDE; Q8BH66; -.
DR ProteomicsDB; 265151; -.
DR Antibodypedia; 23673; 247 antibodies from 29 providers.
DR Ensembl; ENSMUST00000021466; ENSMUSP00000021466; ENSMUSG00000021066.
DR GeneID; 73991; -.
DR KEGG; mmu:73991; -.
DR UCSC; uc007nsy.2; mouse.
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; 1027269at2759; -.
DR PhylomeDB; Q8BH66; -.
DR TreeFam; TF105251; -.
DR BioGRID-ORCS; 73991; 0 hits in 71 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 213 other tissues.
DR ExpressionAtlas; Q8BH66; baseline and differential.
DR Genevisible; Q8BH66; MM.
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:0016021; C:integral component of 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 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 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
