ATLA2_XENLA
ID ATLA2_XENLA Reviewed; 569 AA.
AC Q6GN29;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Atlastin-2;
DE EC=3.6.5.-;
DE AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 2;
DE Short=ARL-6-interacting protein 2;
DE Short=Aip-2;
GN Name=atl2; Synonyms=arl6ip2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27619977; DOI=10.7554/elife.18605;
RA Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.;
RT "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons
RT to generate a tubular membrane network.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic reticulum
CC membranes (PubMed:19665976). Functions in endoplasmic reticulum tubular
CC network biogenesis (PubMed:19665976, PubMed:27619977).
CC {ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:27619977}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27619977}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NHH9}. Note=Localizes at endoplasmic reticulum
CC (ER) three-way tubular junctions (PubMed:27619977).
CC {ECO:0000269|PubMed:27619977}.
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; BC073692; AAH73692.1; -; mRNA.
DR RefSeq; NP_001086007.1; NM_001092538.1.
DR AlphaFoldDB; Q6GN29; -.
DR SMR; Q6GN29; -.
DR DNASU; 444436; -.
DR GeneID; 444436; -.
DR KEGG; xla:444436; -.
DR CTD; 444436; -.
DR Xenbase; XB-GENE-947240; atl2.L.
DR OMA; LEKRLQX; -.
DR OrthoDB; 1027269at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 444436; Expressed in blastula and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA: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; IMP:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP: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 Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..569
FT /note="Atlastin-2"
FT /id="PRO_0000287108"
FT TOPO_DOM 1..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..487
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 80..324
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 244..272
FT /evidence="ECO:0000255"
FT BINDING 90..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 232..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 291..294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 569 AA; 64961 MW; 42A113EA3E4E9279 CRC64;
MAEGGSLRNR TRFGSRSNEA MNHVDYPDEN FVEEIQLNSD TEVMEKPRPI QIVLAHEDDH
NFELDETALE SILMQDHIRD LNVVVLSVAG AFRKGKSFLL DFMLRFMYSQ SSSWIGGNYE
PLTGFTWRGG CERETTGIQI WSEVFVVEKP DGSKVAVILM DTQGAFDSQS TIKDCATVFA
LSTMTSSVQV YNLSQNIQED DLQHLQLFTE YGRLAMEEIY KKPFQTLMFL IRDWSYPYEH
SYGLEGGNKF LEKRLQVKQN QHEELQNVRK HIHSCFTNIG CFLLPHPGLK VATNPYFDGR
LVEIDDEFKK ELRELVPLLL APENLVEKEI SGSKVTCRDL LEYFKAYIKI YQGEELPHPK
SMLQATAEAN NMAAVAGAKD TYSRSMEQVC GGDKPYIAPS DLERKHLDLK ETCIKQFRSV
KKMGGEEFCR RYQEQLEAEI EETYANFLKH NDGKNIFYAA RTPATLFAVM FAMYIISGLT
GFIGMNSIAT ICNLIMGLTL LSFCTWAYVK YSGEFRELGT LIDQIAEIIW EQLLKPLSDN
LMEDNIRQTV RNSIKAGLTD QVSGRLKTN
