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Protein

Caytaxin

Gene

Atcay

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the localization of mitochondria within axons and dendrites.2 Publications

GO - Molecular functioni

  • kinesin binding Source: Ensembl
  • WW domain binding Source: RGD

GO - Biological processi

Keywordsi

Biological processNeurogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Caytaxin
Gene namesi
Name:Atcay
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1309312 Atcay

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Mitochondrion, Synapse

Pathology & Biotechi

Involvement in diseasei

Defects in Atcay are the cause of primary generalized dystonia. The dt (SD-dt:JFL) rat is a spontaneous mutant that develops a dystonic motor syndrome by P12. Dystonic rats exhibit both axial and appendicular dystonia that progresses in severity with increasing postnatal age. There are no gross differences between normal and dt rats in terms of brain morphology.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004199701 – 372CaytaxinAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphoserineBy similarity1

Post-translational modificationi

Cleaved by CASP3 and CASP7. The potential C-terminal product released by CASP3 cleavage may inhibit the ERK signaling pathway through MAP2K2 (By similarity).By similarity
May be ubiquitinated by STUB1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by CASP3By similarity2

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ1M168
PRIDEiQ1M168

Expressioni

Tissue specificityi

Specifically expressed in brain. Detected in cerebellum (at protein level).1 Publication

Developmental stagei

Detected at E15, P1, P7, P14, P36 and in adult cerebellum in all neuronal populations. Peakes at P7 in hippocampus, increases linearly from P1 to P36 in cerebellum, and shows minimal developmental regulation in cerebral cortex. At E15, also detected in dorsal root and peripheral ganglia. In cerebellum, the transcript is present in the molecular, Purkinje and granular layers with higher expression in the molecular layer at P14.1 Publication

Gene expression databases

BgeeiENSRNOG00000020407 Expressed in 7 organ(s), highest expression level in brain
GenevisibleiQ1M168 RN

Interactioni

Subunit structurei

Interacts with KLC1; may link mitochondria to KLC1 and regulate mitochondria localization into neuron projections. Interacts with GLS; the interaction is direct and may control GLS localization, negatively regulating its activity. Interacts with PIN1; upon NGF stimulation (By similarity). The interaction with PIN1 (via WW domain) and GLS is competitive (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi263753, 1 interactor
ELMiQ1M168
STRINGi10116.ENSRNOP00000045560

Structurei

3D structure databases

ProteinModelPortaliQ1M168
SMRiQ1M168
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 328CRAL-TRIOPROSITE-ProRule annotationAdd BLAST158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 120Required for interaction with KLC1By similarity6
Regioni190 – 372Mediates interaction with GLSBy similarityAdd BLAST183

Domaini

The CRAL-TRIO domain is known to bind small hydrophobic molecules.By similarity

Phylogenomic databases

eggNOGiENOG410IFIP Eukaryota
ENOG410ZS9Z LUCA
GeneTreeiENSGT00420000029688
HOGENOMiHOG000230952
HOVERGENiHBG054692
InParanoidiQ1M168
KOiK18450
OMAiMRVVTHG
OrthoDBiEOG091G0E88
PhylomeDBiQ1M168

Family and domain databases

CDDicd00170 SEC14, 1 hit
Gene3Di3.40.525.10, 1 hit
InterProiView protein in InterPro
IPR022181 Bcl2-/adenovirus-E1B
IPR001251 CRAL-TRIO_dom
IPR036865 CRAL-TRIO_dom_sf
PfamiView protein in Pfam
PF12496 BNIP2, 1 hit
PF13716 CRAL_TRIO_2, 1 hit
SMARTiView protein in SMART
SM00516 SEC14, 1 hit
SUPFAMiSSF52087 SSF52087, 1 hit
PROSITEiView protein in PROSITE
PS50191 CRAL_TRIO, 1 hit

Sequencei

Sequence statusi: Complete.

Q1M168-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGTTEATLRM ENVDVRDEWQ DEDLPRPLPE DTGEDHLGGT VEDSSSPPST
60 70 80 90 100
LNLSGAHRKR KTLVAPEINI SLDQSEGSLL SDDFLDTPDD LDINVDDIET
110 120 130 140 150
PDETDSLEFL GNGNELEWED DTPVATAKNM PGDSADLFGD GSGEDGSAAN
160 170 180 190 200
GRLWRTVIIG EQEHRIDLHM IRPYMKVVTH GGYYGEGLNA IIVFAACFLP
210 220 230 240 250
DSSSPDYHYI MENLFLYVIS SLELLVAEDY MIVYLNGATP RRRMPGIGWL
260 270 280 290 300
KKCYHMIDRR LRKNLKSLII VHPSWFIRTV LAISRPFISV KFISKIQYVH
310 320 330 340 350
SLEELEQLIP MEHVQLPACV LQYEEQRLRA KRESARPPQP EFLLPRSEEK
360 370
PETVEEEDRA AEVTEDQETS MS
Length:372
Mass (Da):42,117
Last modified:May 30, 2006 - v1
Checksum:i091E21129D1ADD34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY611623 mRNA Translation: AAT11790.1
AABR06047713 Genomic DNA No translation available.
CH474029 Genomic DNA Translation: EDL89182.1
BC128695 mRNA Translation: AAI28696.1
RefSeqiNP_001035280.1, NM_001040190.1
UniGeneiRn.198771

Genome annotation databases

EnsembliENSRNOT00000041325; ENSRNOP00000045560; ENSRNOG00000020407
GeneIDi362826
KEGGirno:362826
UCSCiRGD:1309312 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY611623 mRNA Translation: AAT11790.1
AABR06047713 Genomic DNA No translation available.
CH474029 Genomic DNA Translation: EDL89182.1
BC128695 mRNA Translation: AAI28696.1
RefSeqiNP_001035280.1, NM_001040190.1
UniGeneiRn.198771

3D structure databases

ProteinModelPortaliQ1M168
SMRiQ1M168
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi263753, 1 interactor
ELMiQ1M168
STRINGi10116.ENSRNOP00000045560

Proteomic databases

PaxDbiQ1M168
PRIDEiQ1M168

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041325; ENSRNOP00000045560; ENSRNOG00000020407
GeneIDi362826
KEGGirno:362826
UCSCiRGD:1309312 rat

Organism-specific databases

CTDi85300
RGDi1309312 Atcay

Phylogenomic databases

eggNOGiENOG410IFIP Eukaryota
ENOG410ZS9Z LUCA
GeneTreeiENSGT00420000029688
HOGENOMiHOG000230952
HOVERGENiHBG054692
InParanoidiQ1M168
KOiK18450
OMAiMRVVTHG
OrthoDBiEOG091G0E88
PhylomeDBiQ1M168

Miscellaneous databases

PROiPR:Q1M168

Gene expression databases

BgeeiENSRNOG00000020407 Expressed in 7 organ(s), highest expression level in brain
GenevisibleiQ1M168 RN

Family and domain databases

CDDicd00170 SEC14, 1 hit
Gene3Di3.40.525.10, 1 hit
InterProiView protein in InterPro
IPR022181 Bcl2-/adenovirus-E1B
IPR001251 CRAL-TRIO_dom
IPR036865 CRAL-TRIO_dom_sf
PfamiView protein in Pfam
PF12496 BNIP2, 1 hit
PF13716 CRAL_TRIO_2, 1 hit
SMARTiView protein in SMART
SM00516 SEC14, 1 hit
SUPFAMiSSF52087 SSF52087, 1 hit
PROSITEiView protein in PROSITE
PS50191 CRAL_TRIO, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiATCAY_RAT
AccessioniPrimary (citable) accession number: Q1M168
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: May 30, 2006
Last modified: September 12, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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