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Protein

Atlastin-3

Gene

Atl3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748GTPBy similarity
Nucleotide bindingi114 – 1163GTPBy similarity
Nucleotide bindingi213 – 2142GTPBy similarity
Nucleotide bindingi272 – 2754GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Atlastin-3 (EC:3.6.5.-)
Gene namesi
Name:Atl3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1309871. Atl3.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Localizes to endoplasmic reticulum tubules and accumulates in punctuate structures corresponding to 3-way junctions, which represent crossing-points at which the tubules build a polygonal network.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 445445CytoplasmicBy similarityAdd
BLAST
Transmembranei446 – 46621HelicalSequence analysisAdd
BLAST
Topological domaini467 – 4671LumenalSequence analysis
Transmembranei468 – 48821HelicalSequence analysisAdd
BLAST
Topological domaini489 – 54153CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Atlastin-3PRO_0000287111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ0ZHH6.
PRIDEiQ0ZHH6.

PTM databases

iPTMnetiQ0ZHH6.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063444.

Structurei

3D structure databases

ProteinModelPortaliQ0ZHH6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 306250GB1/RHD3-type GAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ0ZHH6.
KOiK17339.
PhylomeDBiQ0ZHH6.
TreeFamiTF105251.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q0ZHH6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSPQRTAAV ASRGAGDAME NGKPGPVQVV LVHKEQHSFE LEERALASVL
60 70 80 90 100
LQDHIRDLDV VVVSVAGAFR KGKSFILDFM LRYLYSQKEH GHSNWLGDPE
110 120 130 140 150
EPLTGFSWRG GSDPETTGIQ IWSEVFTVKK PCGKEVAVVL MDTQGAFDSQ
160 170 180 190 200
STVKDCATIF ALSTMTSSVQ IYNLSQNIQE DDLQQLQLFT EYGRLAMDEI
210 220 230 240 250
FQKPFQTLMF LVRDWSFPYE YNYGLQGGMS FLDKRLQVKE HQHEEIQNVR
260 270 280 290 300
NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKEYIASEF KEQLQTLIPY
310 320 330 340 350
VLNPSKLMEK EINGSKVTCR GLLEYFKAYI KIYQGEDLPH PKSMLQATAA
360 370 380 390 400
NNLAAAASAK DIYYSSMEEI CGGEKPYLSP DILEEKHQEF KQLALDHFKK
410 420 430 440 450
TKKMGGKDFS FRYQQELEEE ITELYENFCK HNGSKNVFST FRTPAVLFTG
460 470 480 490 500
IAVLYIASGL TGFIGLEVVA QLFNCMVGLL LIALLTWGYI RYSGQYLELG
510 520 530 540
GAIDSGAAYV LEQASSHIGN STQAAVRDAI AGRPPADKKS Q
Length:541
Mass (Da):60,586
Last modified:May 15, 2007 - v2
Checksum:iF74C6CED80221EAF
GO
Isoform 2 (identifier: Q0ZHH6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLSPQRTAAVASRGA → MDPRFQYAVT

Show »
Length:536
Mass (Da):60,298
Checksum:iEE05AA8CC91ECDD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2852EY → D in ABE26990 (PubMed:14506257).Curated
Sequence conflicti349 – 3491A → AE in ABE26990 (PubMed:14506257).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MLSPQ…ASRGA → MDPRFQYAVT in isoform 2. 1 PublicationVSP_025315Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ450893 mRNA. Translation: ABE26990.1.
AABR03000230 Genomic DNA. No translation available.
RefSeqiNP_001037706.1. NM_001044241.1.
UniGeneiRn.202359.

Genome annotation databases

GeneIDi309187.
KEGGirno:309187.
UCSCiRGD:1309871. rat. [Q0ZHH6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ450893 mRNA. Translation: ABE26990.1.
AABR03000230 Genomic DNA. No translation available.
RefSeqiNP_001037706.1. NM_001044241.1.
UniGeneiRn.202359.

3D structure databases

ProteinModelPortaliQ0ZHH6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063444.

PTM databases

iPTMnetiQ0ZHH6.

Proteomic databases

PaxDbiQ0ZHH6.
PRIDEiQ0ZHH6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi309187.
KEGGirno:309187.
UCSCiRGD:1309871. rat. [Q0ZHH6-1]

Organism-specific databases

CTDi25923.
RGDi1309871. Atl3.

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ0ZHH6.
KOiK17339.
PhylomeDBiQ0ZHH6.
TreeFamiTF105251.

Miscellaneous databases

NextBioi660382.
PROiQ0ZHH6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin."
    Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R., Blackstone C.
    J. Biol. Chem. 278:49063-49071(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiATLA3_RAT
AccessioniPrimary (citable) accession number: Q0ZHH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: January 20, 2016
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.