ATLA2_MACFA
ID ATLA2_MACFA Reviewed; 565 AA.
AC Q95LN3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Atlastin-2;
DE EC=3.6.5.-;
GN Name=ATL2; ORFNames=QtsA-18427;
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=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
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. {ECO:0000250|UniProtKB:Q8NHH9}.
CC -!- SUBUNIT: Interacts with REEP5 and RTN3. Interacts with ZFYVE27.
CC {ECO:0000250|UniProtKB:Q8NHH9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NHH9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NHH9}. Note=Localizes at endoplasmic reticulum
CC (ER) three-way tubular junctions. {ECO:0000250|UniProtKB:Q8NHH9}.
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; AB072755; BAB69724.1; -; mRNA.
DR RefSeq; NP_001274612.1; NM_001287683.1.
DR AlphaFoldDB; Q95LN3; -.
DR SMR; Q95LN3; -.
DR STRING; 9541.XP_005576148.1; -.
DR Ensembl; ENSMFAT00000011612; ENSMFAP00000037362; ENSMFAG00000037890.
DR GeneID; 102144447; -.
DR CTD; 64225; -.
DR VEuPathDB; HostDB:ENSMFAG00000037890; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000155710; -.
DR OrthoDB; 1027269at2759; -.
DR Proteomes; UP000233100; Chromosome 13.
DR Bgee; ENSMFAG00000037890; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; 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:0007030; P:Golgi 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; 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 Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Methylation; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..565
FT /note="Atlastin-2"
FT /id="PRO_0000287106"
FT TOPO_DOM 1..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 73..318
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 238..266
FT /evidence="ECO:0000255"
FT BINDING 83..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 226..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 285..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 252
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHH9"
SQ SEQUENCE 565 AA; 64528 MW; 188AAEDFDF0BD29E CRC64;
MVLKKGVKFF QRLINSKSLR FGENYEDDDL VNSDEVMKKP CPVQIVLAHE DDHNFELDEE
ALEQILLQEH IRDLNIVVVS VAGAFRKGKS FLLDFMLRYM YNKDSQSWIG GNNEPLTGFT
WRGGCERETT GIQVWNEVFV IDRPNGTKVA VLLMDTQGAF DSQSTIKDCA TVFALSTMTS
SVQVYNLSQN IQEDDLQHLQ LFTEYGRLAM EEIYQKPFQT LMFLIRDWSY PYEHSYGLEG
GKQFLEKRLQ VKKNQHEELQ NVRKHIHNCF SNLGCFLLPH PGLKVATNPS FDGRLKDIDE
DFKRELRNLV PLLLAPENLV EKEISGSKVT CRDLVEYFKA YIKIYQGEEL PHPKSMLQAT
AEANNLAAVA GARDTYCKSM EQVCGGDKPY IAPSDLERKH LDLKEVAIKQ FRSVKKMGGD
EFCRRYQDQL EAEIEETYAN FIKHNDGKNI FYAARTPATL FAVMFAMYII SGLTGFIGLN
SIAVLCNLVM GLALTFLCTW AYVKYSGEFR EIGTMIDQIA ETLWEQVLKP LGDNLMEENI
RQSVTNSIKA GLTDQVSHHA RLKTD
