ATLA3_RAT
ID ATLA3_RAT Reviewed; 541 AA.
AC Q0ZHH6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Atlastin-3;
DE EC=3.6.5.-;
GN Name=Atl3;
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] (ISOFORM 2).
RC TISSUE=Testis;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 (By similarity). {ECO:0000250|UniProtKB:Q6DD88}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6DD88}; 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=Q0ZHH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0ZHH6-2; Sequence=VSP_025315;
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; DQ450893; ABE26990.1; -; mRNA.
DR EMBL; AABR03000230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001037706.1; NM_001044241.1.
DR AlphaFoldDB; Q0ZHH6; -.
DR SMR; Q0ZHH6; -.
DR STRING; 10116.ENSRNOP00000063444; -.
DR iPTMnet; Q0ZHH6; -.
DR PhosphoSitePlus; Q0ZHH6; -.
DR jPOST; Q0ZHH6; -.
DR PaxDb; Q0ZHH6; -.
DR PRIDE; Q0ZHH6; -.
DR GeneID; 309187; -.
DR KEGG; rno:309187; -.
DR UCSC; RGD:1309871; rat. [Q0ZHH6-1]
DR CTD; 25923; -.
DR RGD; 1309871; Atl3.
DR eggNOG; KOG2037; Eukaryota.
DR InParanoid; Q0ZHH6; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q0ZHH6; -.
DR TreeFam; TF105251; -.
DR PRO; PR:Q0ZHH6; -.
DR Proteomes; UP000002494; Unplaced.
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: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 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; 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_0000287111"
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..306
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..15
FT /note="MLSPQRTAAVASRGA -> MDPRFQYAVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14506257"
FT /id="VSP_025315"
FT CONFLICT 284..285
FT /note="EY -> D (in Ref. 1; ABE26990)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="A -> AE (in Ref. 1; ABE26990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60586 MW; F74C6CED80221EAF CRC64;
MLSPQRTAAV ASRGAGDAME NGKPGPVQVV LVHKEQHSFE LEERALASVL LQDHIRDLDV
VVVSVAGAFR KGKSFILDFM LRYLYSQKEH GHSNWLGDPE EPLTGFSWRG GSDPETTGIQ
IWSEVFTVKK PCGKEVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LVRDWSFPYE YNYGLQGGMS FLDKRLQVKE
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKEYIASEF KEQLQTLIPY
VLNPSKLMEK EINGSKVTCR GLLEYFKAYI KIYQGEDLPH PKSMLQATAA NNLAAAASAK
DIYYSSMEEI CGGEKPYLSP DILEEKHQEF KQLALDHFKK TKKMGGKDFS FRYQQELEEE
ITELYENFCK HNGSKNVFST FRTPAVLFTG IAVLYIASGL TGFIGLEVVA QLFNCMVGLL
LIALLTWGYI RYSGQYLELG GAIDSGAAYV LEQASSHIGN STQAAVRDAI AGRPPADKKS
Q
