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Protein

Atlastin-3

Gene

ATL3

Organism
Homo sapiens (Human)
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.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi67 – 74GTPBy similarity8
Nucleotide bindingi114 – 116GTPBy similarity3
Nucleotide bindingi213 – 214GTPBy similarity2
Nucleotide bindingi272 – 275GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: UniProtKB

GO - Biological processi

  • endoplasmic reticulum organization Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:24526. ATL3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 445Cytoplasmic1 PublicationAdd BLAST445
Transmembranei446 – 466HelicalSequence analysisAdd BLAST21
Topological domaini467LumenalSequence analysis1
Transmembranei468 – 488HelicalSequence analysisAdd BLAST21
Topological domaini489 – 541Cytoplasmic1 PublicationAdd BLAST53

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum tubular network Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory, 1F (HSN1F)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant sensory neuropathy affecting the lower limbs. Distal sensory impairment becomes apparent during the second or third decade of life, resulting in painless ulceration of the feet with poor healing, which can progress to osteomyelitis, bone destruction, and amputation. There is no autonomic involvement, spasticity, or cognitive impairment.
See also OMIM:615632
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070973192Y → C in HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum. 1 PublicationCorresponds to variant rs587777108dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73K → A: Alters endoplasmic reticulum morphogenesis. 1 Publication1
Mutagenesisi213R → Q: Alters endoplasmic reticulum morphogenesis. 1 Publication1

Keywords - Diseasei

Disease mutation, Neuropathy

Organism-specific databases

DisGeNETi25923.
MalaCardsiATL3.
MIMi615632. phenotype.
OpenTargetsiENSG00000184743.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA164716353.

Polymorphism and mutation databases

BioMutaiATL3.
DMDMi74736374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002871091 – 541Atlastin-3Add BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei391N6-acetyllysineCombined sources1
Modified residuei535PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6DD88.
MaxQBiQ6DD88.
PaxDbiQ6DD88.
PeptideAtlasiQ6DD88.
PRIDEiQ6DD88.
TopDownProteomicsiQ6DD88.

PTM databases

iPTMnetiQ6DD88.
PhosphoSitePlusiQ6DD88.
SwissPalmiQ6DD88.

Expressioni

Tissue specificityi

Expressed in the central nervous system and in dorsal root ganglia neurons. Expressed in peripheral tissues (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000184743.
CleanExiHS_ATL3.
ExpressionAtlasiQ6DD88. baseline and differential.
GenevisibleiQ6DD88. HS.

Interactioni

Subunit structurei

Interacts with ZFYVE27 (PubMed:23969831).1 Publication

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117423. 79 interactors.
IntActiQ6DD88. 48 interactors.
MINTiMINT-3308360.
STRINGi9606.ENSP00000381844.

Structurei

3D structure databases

ProteinModelPortaliQ6DD88.
SMRiQ6DD88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 305GB1/RHD3-type GAdd BLAST249

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ6DD88.
KOiK17339.
OMAiWAFIRYS.
OrthoDBiEOG091G053P.
PhylomeDBiQ6DD88.
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.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6DD88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL
60 70 80 90 100
LQDHIRDLDV VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE
110 120 130 140 150
EPLTGFSWRG GSDPETTGIQ IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ
160 170 180 190 200
STVKDCATIF ALSTMTSSVQ IYNLSQNIQE DDLQQLQLFT EYGRLAMDEI
210 220 230 240 250
FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE HQHEEIQNVR
260 270 280 290 300
NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV
310 320 330 340 350
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA
360 370 380 390 400
NNLAAAASAK DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK
410 420 430 440 450
TKKMGGKDFS FRYQQELEEE IKELYENFCK HNGSKNVFST FRTPAVLFTG
460 470 480 490 500
IVALYIASGL TGFIGLEVVA QLFNCMVGLL LIALLTWGYI RYSGQYRELG
510 520 530 540
GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA Q
Length:541
Mass (Da):60,542
Last modified:August 16, 2004 - v1
Checksum:iE5C58A53F93B42D0
GO

Sequence cautioni

The sequence BAC05111 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49I → T in BAB14552 (PubMed:14702039).Curated1
Sequence conflicti158T → A in CAB56010 (PubMed:17974005).Curated1
Sequence conflicti173N → S in BAC05111 (PubMed:14702039).Curated1
Sequence conflicti202Q → R in CAB56010 (PubMed:17974005).Curated1
Sequence conflicti215W → R in CAB56010 (PubMed:17974005).Curated1
Sequence conflicti351N → Y in CAB56010 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070973192Y → C in HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum. 1 PublicationCorresponds to variant rs587777108dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097588 mRNA. Translation: BAC05111.1. Sequence problems.
AK023383 mRNA. Translation: BAB14552.1.
AL117600 mRNA. Translation: CAB56010.2.
BC077727 mRNA. Translation: AAH77727.1.
CCDSiCCDS41663.1.
PIRiT17320.
RefSeqiNP_001276977.1. NM_001290048.1.
NP_056274.3. NM_015459.4.
UniGeneiHs.356719.

Genome annotation databases

EnsembliENST00000398868; ENSP00000381844; ENSG00000184743.
GeneIDi25923.
KEGGihsa:25923.
UCSCiuc001nxk.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097588 mRNA. Translation: BAC05111.1. Sequence problems.
AK023383 mRNA. Translation: BAB14552.1.
AL117600 mRNA. Translation: CAB56010.2.
BC077727 mRNA. Translation: AAH77727.1.
CCDSiCCDS41663.1.
PIRiT17320.
RefSeqiNP_001276977.1. NM_001290048.1.
NP_056274.3. NM_015459.4.
UniGeneiHs.356719.

3D structure databases

ProteinModelPortaliQ6DD88.
SMRiQ6DD88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117423. 79 interactors.
IntActiQ6DD88. 48 interactors.
MINTiMINT-3308360.
STRINGi9606.ENSP00000381844.

PTM databases

iPTMnetiQ6DD88.
PhosphoSitePlusiQ6DD88.
SwissPalmiQ6DD88.

Polymorphism and mutation databases

BioMutaiATL3.
DMDMi74736374.

Proteomic databases

EPDiQ6DD88.
MaxQBiQ6DD88.
PaxDbiQ6DD88.
PeptideAtlasiQ6DD88.
PRIDEiQ6DD88.
TopDownProteomicsiQ6DD88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398868; ENSP00000381844; ENSG00000184743.
GeneIDi25923.
KEGGihsa:25923.
UCSCiuc001nxk.2. human.

Organism-specific databases

CTDi25923.
DisGeNETi25923.
GeneCardsiATL3.
HGNCiHGNC:24526. ATL3.
MalaCardsiATL3.
MIMi609369. gene.
615632. phenotype.
neXtProtiNX_Q6DD88.
OpenTargetsiENSG00000184743.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA164716353.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ6DD88.
KOiK17339.
OMAiWAFIRYS.
OrthoDBiEOG091G053P.
PhylomeDBiQ6DD88.
TreeFamiTF105251.

Miscellaneous databases

GenomeRNAii25923.
PROiQ6DD88.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184743.
CleanExiHS_ATL3.
ExpressionAtlasiQ6DD88. baseline and differential.
GenevisibleiQ6DD88. HS.

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.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATLA3_HUMAN
AccessioniPrimary (citable) accession number: Q6DD88
Secondary accession number(s): Q8N7W5, Q9H8Q5, Q9UFL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: August 16, 2004
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.