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Protein

Atlastin-1

Gene

Atl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. May also regulate Golgi biogenesis. May regulate axonal development (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 818GTPBy similarity
Nucleotide bindingi118 – 1203GTPBy similarity
Nucleotide bindingi217 – 2182GTPBy similarity
Nucleotide bindingi276 – 2794GTPBy 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-1 (EC:3.6.5.-)
Alternative name(s):
Spastic paraplegia 3A homolog
Gene namesi
Name:Atl1
Synonyms:Spg3a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1921241. Atl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 449449CytoplasmicBy similarityAdd
BLAST
Transmembranei450 – 47021HelicalSequence AnalysisAdd
BLAST
Topological domaini471 – 4711LumenalSequence Analysis
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST
Topological domaini493 – 55866CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Atlastin-1PRO_0000190973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei395 – 3951N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BH66.
PaxDbiQ8BH66.
PRIDEiQ8BH66.

PTM databases

PhosphoSiteiQ8BH66.

Expressioni

Gene expression databases

BgeeiQ8BH66.
CleanExiMM_GBP3.
GenevestigatoriQ8BH66.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ8BH66. 1 interaction.
MINTiMINT-4135323.
STRINGi10090.ENSMUSP00000021466.

Structurei

3D structure databases

ProteinModelPortaliQ8BH66.
SMRiQ8BH66. Positions 31-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 309246GB1/RHD3-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni448 – 558111Sufficient for membrane associationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili412 – 43928Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG325148.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ8BH66.
KOiK17339.
OMAiHLYHHAF.
OrthoDBiEOG7H4DTH.
PhylomeDBiQ8BH66.
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]

Sequencei

Sequence statusi: Complete.

Q8BH66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSRRDRNS WGGFSEKSSD WSSEEEEPVR KAGPVQVLIV KDDHSFELDE
60 70 80 90 100
AALNRILLSQ AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV
110 120 130 140 150
GDYNEPLTGF SWRGGSERET TGIQIWSEVF LINKLDGKKV AVLLMDTQGT
160 170 180 190 200
FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ NVQEDDLQHL QLFTEYGRLA
210 220 230 240 250
MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL KVSGNQHEEL
260 270 280 290 300
QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
310 320 330 340 350
IPWLLSPERL DIKEINGNKI TCRGLLEYFK AYIKIYQGEE LPHPKSMLQA
360 370 380 390 400
TAEANNLAAV ATAKDTYNKK MEEVCGGDKP FLAPNDLQSK HLQLKEESVK
410 420 430 440 450
LFRGVKKMGG EEFSRRYLQQ LESEIDELYI QYIKHNDSKN IFHAARTPAT
460 470 480 490 500
LFVVIFITYV IAGVTGFIGL DIIASLCNMI MGLTLITLCT WAYIRYSGEY
510 520 530 540 550
RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLCHQ AFPAPKSEPT

QQPEKKKI
Length:558
Mass (Da):63,377
Last modified:March 1, 2003 - v1
Checksum:i4734A5D99A9171AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046919 mRNA. Translation: BAC32920.1.
AK050339 mRNA. Translation: BAC34198.1.
BC050784 mRNA. Translation: AAH50784.1.
AK083918 mRNA. Translation: BAC39062.1.
CCDSiCCDS36465.1.
RefSeqiNP_848743.1. NM_178628.5.
UniGeneiMm.474462.

Genome annotation databases

EnsembliENSMUST00000021466; ENSMUSP00000021466; ENSMUSG00000021066.
GeneIDi73991.
KEGGimmu:73991.
UCSCiuc007nsy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046919 mRNA. Translation: BAC32920.1.
AK050339 mRNA. Translation: BAC34198.1.
BC050784 mRNA. Translation: AAH50784.1.
AK083918 mRNA. Translation: BAC39062.1.
CCDSiCCDS36465.1.
RefSeqiNP_848743.1. NM_178628.5.
UniGeneiMm.474462.

3D structure databases

ProteinModelPortaliQ8BH66.
SMRiQ8BH66. Positions 31-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BH66. 1 interaction.
MINTiMINT-4135323.
STRINGi10090.ENSMUSP00000021466.

PTM databases

PhosphoSiteiQ8BH66.

Proteomic databases

MaxQBiQ8BH66.
PaxDbiQ8BH66.
PRIDEiQ8BH66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021466; ENSMUSP00000021466; ENSMUSG00000021066.
GeneIDi73991.
KEGGimmu:73991.
UCSCiuc007nsy.2. mouse.

Organism-specific databases

CTDi51062.
MGIiMGI:1921241. Atl1.

Phylogenomic databases

eggNOGiNOG325148.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ8BH66.
KOiK17339.
OMAiHLYHHAF.
OrthoDBiEOG7H4DTH.
PhylomeDBiQ8BH66.
TreeFamiTF105251.

Miscellaneous databases

ChiTaRSiAtl1. mouse.
NextBioi339480.
PROiQ8BH66.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH66.
CleanExiMM_GBP3.
GenevestigatoriQ8BH66.

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. "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.
    , 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. 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.

Entry informationi

Entry nameiATLA1_MOUSE
AccessioniPrimary (citable) accession number: Q8BH66
Secondary accession number(s): Q8BJH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 105 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.