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Q8BH66 (ATLA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atlastin-1

EC=3.6.5.-
Alternative name(s):
Spastic paraplegia 3A homolog
Gene names
Name:Atl1
Synonyms:Spg3a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development By similarity.

Subunit structure

Monomer as apoprotein and in the GDP-bound form. Homodimer in the GTP-bound form. Homooligomer. Interacts (via N-terminal region) with MAP4K4 (via CNH regulatory domain). Interacts with SPAST; interaction is direct By similarity. Interacts with REEP5, RTN3 and probably RTN4 (via the transmembrane region). Interacts with REEP1 By similarity. Ref.4

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Golgi apparatus membrane; Multi-pass membrane protein By similarity. Cell projectionaxon By similarity.

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3-type GTPase family. GB1 subfamily.

Contains 1 GB1/RHD3-type G (guanine nucleotide-binding) domain.

Ontologies

Keywords
   Cellular componentCell projection
Endoplasmic reticulum
Golgi apparatus
Membrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum organization

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi cis cisterna

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Atlastin-1
PRO_0000190973

Regions

Topological domain1 – 449449Cytoplasmic By similarity
Transmembrane450 – 47021Helical; Potential
Topological domain4711Lumenal Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 55866Cytoplasmic By similarity
Domain64 – 309246GB1/RHD3-type G
Nucleotide binding74 – 818GTP By similarity
Nucleotide binding118 – 1203GTP By similarity
Nucleotide binding217 – 2182GTP By similarity
Nucleotide binding276 – 2794GTP By similarity
Region448 – 558111Sufficient for membrane association By similarity
Coiled coil412 – 43928 Potential

Amino acid modifications

Modified residue221Phosphoserine Ref.3
Modified residue231Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BH66 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4734A5D99A9171AC

FASTA55863,377
        10         20         30         40         50         60 
MAKSRRDRNS WGGFSEKSSD WSSEEEEPVR KAGPVQVLIV KDDHSFELDE AALNRILLSQ 

        70         80         90        100        110        120 
AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET 

       130        140        150        160        170        180 
TGIQIWSEVF LINKLDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ 

       190        200        210        220        230        240 
NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL 

       250        260        270        280        290        300 
KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL 

       310        320        330        340        350        360 
IPWLLSPERL DIKEINGNKI TCRGLLEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV 

       370        380        390        400        410        420 
ATAKDTYNKK MEEVCGGDKP FLAPNDLQSK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ 

       430        440        450        460        470        480 
LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI 

       490        500        510        520        530        540 
MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLCHQ 

       550 
AFPAPKSEPT QQPEKKKI 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Liver and Spinal ganglion.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"A class of dynamin-like GTPases involved in the generation of the tubular ER network."
Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH REEP5 AND RTN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK046919 mRNA. Translation: BAC32920.1.
AK050339 mRNA. Translation: BAC34198.1.
BC050784 mRNA. Translation: AAH50784.1.
AK083918 mRNA. Translation: BAC39062.1.
CCDSCCDS36465.1.
RefSeqNP_848743.1. NM_178628.5.
UniGeneMm.474462.

3D structure databases

ProteinModelPortalQ8BH66.
SMRQ8BH66. Positions 31-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BH66. 1 interaction.
MINTMINT-4135323.
STRING10090.ENSMUSP00000021466.

PTM databases

PhosphoSiteQ8BH66.

Proteomic databases

MaxQBQ8BH66.
PaxDbQ8BH66.
PRIDEQ8BH66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021466; ENSMUSP00000021466; ENSMUSG00000021066.
GeneID73991.
KEGGmmu:73991.
UCSCuc007nsy.2. mouse.

Organism-specific databases

CTD51062.
MGIMGI:1921241. Atl1.

Phylogenomic databases

eggNOGNOG325148.
GeneTreeENSGT00390000008959.
HOGENOMHOG000234332.
HOVERGENHBG062891.
InParanoidQ8BH66.
KOK17339.
OMAHLYHHAF.
OrthoDBEOG7H4DTH.
PhylomeDBQ8BH66.
TreeFamTF105251.

Gene expression databases

BgeeQ8BH66.
CleanExMM_GBP3.
GenevestigatorQ8BH66.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATL1. mouse.
NextBio339480.
PROQ8BH66.
SOURCESearch...

Entry information

Entry nameATLA1_MOUSE
AccessionPrimary (citable) accession number: Q8BH66
Secondary accession number(s): Q8BJH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot