ATLA1_RAT
ID ATLA1_RAT Reviewed; 558 AA.
AC Q6PST4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Atlastin-1;
DE EC=3.6.5.-;
DE AltName: Full=Spastic paraplegia 3A homolog;
GN Name=Atl1; Synonyms=Spg3a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
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 [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 FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-217; ARG-239 AND
RP HIS-258, AND DEVELOPMENTAL STAGE.
RX PubMed=16537571; DOI=10.1093/hmg/ddl054;
RA Zhu P.-P., Soderblom C., Tao-Cheng J.-H., Stadler J., Blackstone C.;
RT "SPG3A protein atlastin-1 is enriched in growth cones and promotes axon
RT elongation during neuronal development.";
RL Hum. Mol. Genet. 15:1343-1353(2006).
RN [4]
RP INTERACTION WITH REEP5; RTN3 AND RTN4.
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].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP INTERACTION WITH ARL6IP1.
RX PubMed=24262037; DOI=10.1042/bj20131186;
RA Yamamoto Y., Yoshida A., Miyazaki N., Iwasaki K., Sakisaka T.;
RT "Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-
RT like fashion.";
RL Biochem. J. 458:69-79(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 ECO:0000269|PubMed:16537571}.
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 RTN4 (via the transmembrane region) (PubMed:19665976). Interacts with
CC REEP1 (By similarity). Interacts with CPT1C (By similarity). Interacts
CC with ARL6IP1 (PubMed:24262037). Interacts with ZFYVE27 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH66, ECO:0000250|UniProtKB:Q8WXF7,
CC ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:24262037}.
CC -!- INTERACTION:
CC Q6PST4; Q9JK11-1: Rtn4; NbExp=6; IntAct=EBI-2410213, EBI-919989;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14506257}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14506257}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14506257}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14506257}. Cell projection, axon
CC {ECO:0000269|PubMed:16537571}. Note=Localizes to endoplasmic reticulum
CC tubular network. {ECO:0000250|UniProtKB:Q8BH66}.
CC -!- TISSUE SPECIFICITY: Detected in brain where it is abundant in lamina V
CC of the cerebral cortex. Also expressed within the hippocampus, mainly
CC in pyramidal neurons in CA1 and CA3. Weakly expressed in the striatum
CC and more robustly in amygdala and several thalamic nuclei. Also
CC detected in several mesopontine nuclei (at protein level).
CC {ECO:0000269|PubMed:14506257}.
CC -!- DEVELOPMENTAL STAGE: Expression increases gradually from E18 through
CC adulthood. {ECO:0000269|PubMed:16537571}.
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; AY581896; AAS89975.1; -; mRNA.
DR EMBL; BC092645; AAH92645.1; -; mRNA.
DR RefSeq; NP_001009831.1; NM_001009831.2.
DR AlphaFoldDB; Q6PST4; -.
DR SMR; Q6PST4; -.
DR BioGRID; 263689; 2.
DR IntAct; Q6PST4; 2.
DR MINT; Q6PST4; -.
DR STRING; 10116.ENSRNOP00000041993; -.
DR iPTMnet; Q6PST4; -.
DR PhosphoSitePlus; Q6PST4; -.
DR SwissPalm; Q6PST4; -.
DR jPOST; Q6PST4; -.
DR PaxDb; Q6PST4; -.
DR PRIDE; Q6PST4; -.
DR Ensembl; ENSRNOT00000046085; ENSRNOP00000041993; ENSRNOG00000005063.
DR GeneID; 362750; -.
DR KEGG; rno:362750; -.
DR UCSC; RGD:1359232; rat.
DR CTD; 51062; -.
DR RGD; 1359232; Atl1.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000158704; -.
DR HOGENOM; CLU_021447_2_0_1; -.
DR InParanoid; Q6PST4; -.
DR OMA; GFIHNIW; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q6PST4; -.
DR TreeFam; TF105251; -.
DR PRO; PR:Q6PST4; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005063; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q6PST4; RN.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA: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; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP: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_0000384814"
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..447
FT /note="Redistribution to soluble cell fraction"
FT /evidence="ECO:0000250"
FT REGION 1..29
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:22673903"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 395
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DD88"
FT MUTAGEN 217
FT /note="R->Q: Loss of GTPase activity. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:16537571"
FT MUTAGEN 239
FT /note="R->C: Loss of GTPase activity. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:16537571"
FT MUTAGEN 258
FT /note="H->R: Loss of GTPase activity. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:16537571"
SQ SEQUENCE 558 AA; 63375 MW; 4FFDE569007E171F CRC64;
MAKSRRDRNS WGGFSEKSSD WSSEEEEPVR KAGPVQVLIV KDDHSFELDE AALNRILLSE
AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET
TGIQIWSEVF LINKLDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ
NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL
KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
IPWLLSPESL DIKEINGNKI TCRGLLEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV
ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLQLKEDSVK LFRGVKKMGG EEFSRRYLQQ
LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI
MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYQQ
AFPAPKSEPT EQPEKKKI
