ATLA1_MACFA
ID ATLA1_MACFA Reviewed; 558 AA.
AC Q60HD2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Atlastin-1;
DE EC=3.6.5.-;
GN Name=ATL1; ORFNames=QflA-10403;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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. 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.
CC Interacts with REEP1. Interacts with CPT1C. Interacts with ARL6IP1.
CC Interacts with ZFYVE27. {ECO:0000250|UniProtKB:Q6PST4,
CC ECO:0000250|UniProtKB:Q8BH66, ECO:0000250|UniProtKB:Q8WXF7}.
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:0000250|UniProtKB:Q8BH66}.
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; AB125195; BAD51983.1; -; mRNA.
DR RefSeq; NP_001274574.1; NM_001287645.1.
DR RefSeq; XP_005561274.1; XM_005561217.2.
DR AlphaFoldDB; Q60HD2; -.
DR SMR; Q60HD2; -.
DR STRING; 9541.XP_005561274.1; -.
DR Ensembl; ENSMFAT00000019921; ENSMFAP00000045617; ENSMFAG00000000528.
DR GeneID; 102139537; -.
DR CTD; 51062; -.
DR VEuPathDB; HostDB:ENSMFAG00000000528; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000158704; -.
DR OrthoDB; 1027269at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
DR Bgee; ENSMFAG00000000528; Expressed in temporal lobe and 11 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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; ISS: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 2: Evidence at transcript 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_0000190972"
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..27
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: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"
SQ SEQUENCE 558 AA; 63515 MW; 4B3EDB8B2B091886 CRC64;
MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLIV KDDHSFELDE TALNRILLSE
AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET
TGIQIWSEVF 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 FLAPNDLQSK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ
LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI
MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ
AFPTPKSEST EQSEKKKM
