ATLA3_MOUSE
ID ATLA3_MOUSE Reviewed; 541 AA.
AC Q91YH5; Q3UGW3; Q8C0L7; Q8C174; Q99LZ9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Atlastin-3;
DE EC=3.6.5.-;
GN Name=Atl3;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Skin, and Thymus;
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] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [4]
RP INTERACTION WITH REEP5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
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 (By similarity). {ECO:0000250|UniProtKB:Q6DD88}.
CC -!- SUBUNIT: Interacts with ZFYVE27 (By similarity). Interacts with REEP5
CC (PubMed:32075961). {ECO:0000250|UniProtKB:Q6DD88,
CC ECO:0000269|PubMed:32075961}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32075961}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubules and
CC accumulates in punctuate structures corresponding to 3-way junctions,
CC which represent crossing-points at which the tubules build a polygonal
CC network. {ECO:0000250|UniProtKB:Q6DD88}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YH5-2; Sequence=VSP_025314;
CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes (at protein level).
CC {ECO:0000269|PubMed:32075961}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH02149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK028842; BAC26148.1; -; mRNA.
DR EMBL; AK030660; BAC27066.1; -; mRNA.
DR EMBL; AK077752; BAC36992.1; -; mRNA.
DR EMBL; AK147720; BAE28094.1; -; mRNA.
DR EMBL; AK169476; BAE41194.1; -; mRNA.
DR EMBL; BC002149; AAH02149.1; ALT_INIT; mRNA.
DR EMBL; BC017138; AAH17138.1; -; mRNA.
DR CCDS; CCDS29527.1; -. [Q91YH5-1]
DR RefSeq; NP_001156977.1; NM_001163505.1.
DR RefSeq; NP_666203.3; NM_146091.4. [Q91YH5-1]
DR AlphaFoldDB; Q91YH5; -.
DR SMR; Q91YH5; -.
DR BioGRID; 224585; 2.
DR IntAct; Q91YH5; 1.
DR STRING; 10090.ENSMUSP00000025668; -.
DR iPTMnet; Q91YH5; -.
DR PhosphoSitePlus; Q91YH5; -.
DR SwissPalm; Q91YH5; -.
DR EPD; Q91YH5; -.
DR jPOST; Q91YH5; -.
DR MaxQB; Q91YH5; -.
DR PaxDb; Q91YH5; -.
DR PeptideAtlas; Q91YH5; -.
DR PRIDE; Q91YH5; -.
DR ProteomicsDB; 265152; -. [Q91YH5-1]
DR ProteomicsDB; 265153; -. [Q91YH5-2]
DR Antibodypedia; 28987; 240 antibodies from 27 providers.
DR DNASU; 109168; -.
DR Ensembl; ENSMUST00000025668; ENSMUSP00000025668; ENSMUSG00000024759. [Q91YH5-1]
DR GeneID; 109168; -.
DR KEGG; mmu:109168; -.
DR UCSC; uc008glg.2; mouse. [Q91YH5-1]
DR CTD; 25923; -.
DR MGI; MGI:1924270; Atl3.
DR VEuPathDB; HostDB:ENSMUSG00000024759; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000158566; -.
DR HOGENOM; CLU_021447_2_0_1; -.
DR InParanoid; Q91YH5; -.
DR OMA; QYQKNME; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q91YH5; -.
DR TreeFam; TF105251; -.
DR BioGRID-ORCS; 109168; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Atl3; mouse.
DR PRO; PR:Q91YH5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91YH5; protein.
DR Bgee; ENSMUSG00000024759; Expressed in seminiferous tubule of testis and 225 other tissues.
DR ExpressionAtlas; Q91YH5; baseline and differential.
DR Genevisible; Q91YH5; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProt.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:UniProt.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:UniProt.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; GTP-binding;
KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..541
FT /note="Atlastin-3"
FT /id="PRO_0000287110"
FT TOPO_DOM 1..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 57..305
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 213..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DD88"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025314"
FT CONFLICT 271
FT /note="Q -> K (in Ref. 1; BAC27066)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="H -> N (in Ref. 1; BAE28094)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="Y -> C (in Ref. 1; BAC26148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60575 MW; 8D183335EAF88542 CRC64;
MLSPQRTAAV ASRGAGDAME NGKPGPVQVV LVHKEQHSFE LEERALASVL LQDHIRDLDV
VVVSVAGAFR KGKSFILDFM LRYLYSQKEG GHSDWLGDPE EPLTGFSWRG GSDPETTGIQ
IWSEVFTVKK PCGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LIRDWSFPYE YNYGLQGGMA FLDKRLHVKE
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPNFDG KLKDIASEFK EQLQALIPYV
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK
DIYYNNMEEI CGGEKPYLSP DILEEKHLEF KQLALDHFKK IKKMGGKDFS FRYQQELEEE
IKELYENFCK HNGSKNVFST FRTPAVLFTG IAALYIASGF TGFIGLEVVA QLFNCMVGLL
LIALLTWGYI RYSGQYRELG GAIDSGAAYV LEQASSHIGN STQAAVRDAV VGRPPADKKS
Q
