ATCAY_RAT
ID ATCAY_RAT Reviewed; 372 AA.
AC Q1M168;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Caytaxin;
GN Name=Atcay;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISEASE, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=16246457; DOI=10.1016/j.molbrainres.2005.09.009;
RA Xiao J., Ledoux M.S.;
RT "Caytaxin deficiency causes generalized dystonia in rats.";
RL Brain Res. Mol. Brain Res. 141:181-192(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH GLS.
RX PubMed=16899818; DOI=10.1242/jcs.03061;
RA Buschdorf J.P., Li Chew L., Zhang B., Cao Q., Liang F.Y., Liou Y.C.,
RA Zhou Y.T., Low B.C.;
RT "Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to
RT neurite terminals and reduces glutamate levels.";
RL J. Cell Sci. 119:3337-3350(2006).
RN [6]
RP FUNCTION IN MITOCHONDRIA LOCALIZATION, INTERACTION WITH KLC1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19861499; DOI=10.1242/jcs.048579;
RA Aoyama T., Hata S., Nakao T., Tanigawa Y., Oka C., Kawaichi M.;
RT "Cayman ataxia protein caytaxin is transported by kinesin along neurites
RT through binding to kinesin light chains.";
RL J. Cell Sci. 122:4177-4185(2009).
CC -!- FUNCTION: Functions in the development of neural tissues, particularly
CC the postnatal maturation of the cerebellar cortex. May play a role in
CC neurotransmission through regulation of glutaminase/GLS, an enzyme
CC responsible for the production in neurons of the glutamate
CC neurotransmitter. Alternatively, may regulate the localization of
CC mitochondria within axons and dendrites. {ECO:0000269|PubMed:16246457,
CC ECO:0000269|PubMed:19861499}.
CC -!- SUBUNIT: Interacts with KLC1; may link mitochondria to KLC1 and
CC regulate mitochondria localization into neuron projections. Interacts
CC with GLS; the interaction is direct and may control GLS localization,
CC negatively regulating its activity. Interacts with PIN1; upon NGF
CC stimulation (By similarity). The interaction with PIN1 (via WW domain)
CC and GLS is competitive (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:19861499}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19861499}. Presynapse
CC {ECO:0000269|PubMed:19861499}. Mitochondrion
CC {ECO:0000269|PubMed:19861499}. Cell projection, growth cone
CC {ECO:0000269|PubMed:19861499}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q86WG3}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. Detected in
CC cerebellum (at protein level). {ECO:0000269|PubMed:16246457}.
CC -!- DEVELOPMENTAL STAGE: Detected at E15, P1, P7, P14, P36 and in adult
CC cerebellum in all neuronal populations. Peakes at P7 in hippocampus,
CC increases linearly from P1 to P36 in cerebellum, and shows minimal
CC developmental regulation in cerebral cortex. At E15, also detected in
CC dorsal root and peripheral ganglia. In cerebellum, the transcript is
CC present in the molecular, Purkinje and granular layers with higher
CC expression in the molecular layer at P14.
CC {ECO:0000269|PubMed:16246457}.
CC -!- DOMAIN: The CRAL-TRIO domain is known to bind small hydrophobic
CC molecules. {ECO:0000250}.
CC -!- PTM: Cleaved by CASP3 and CASP7. The potential C-terminal product
CC released by CASP3 cleavage may inhibit the ERK signaling pathway
CC through MAP2K2 (By similarity). {ECO:0000250}.
CC -!- PTM: May be ubiquitinated by STUB1. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Atcay are the cause of primary generalized
CC dystonia. The dt (SD-dt:JFL) rat is a spontaneous mutant that develops
CC a dystonic motor syndrome by P12. Dystonic rats exhibit both axial and
CC appendicular dystonia that progresses in severity with increasing
CC postnatal age. There are no gross differences between normal and dt
CC rats in terms of brain morphology. {ECO:0000269|PubMed:16246457}.
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DR EMBL; AY611623; AAT11790.1; -; mRNA.
DR EMBL; AABR06047713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474029; EDL89182.1; -; Genomic_DNA.
DR EMBL; BC128695; AAI28696.1; -; mRNA.
DR RefSeq; NP_001035280.1; NM_001040190.1.
DR AlphaFoldDB; Q1M168; -.
DR BioGRID; 263753; 1.
DR ELM; Q1M168; -.
DR STRING; 10116.ENSRNOP00000045560; -.
DR PaxDb; Q1M168; -.
DR PRIDE; Q1M168; -.
DR GeneID; 362826; -.
DR KEGG; rno:362826; -.
DR UCSC; RGD:1309312; rat.
DR CTD; 85300; -.
DR RGD; 1309312; Atcay.
DR VEuPathDB; HostDB:ENSRNOG00000020407; -.
DR eggNOG; KOG3308; Eukaryota.
DR HOGENOM; CLU_039135_0_0_1; -.
DR InParanoid; Q1M168; -.
DR OMA; AKNMPGN; -.
DR OrthoDB; 755773at2759; -.
DR PhylomeDB; Q1M168; -.
DR PRO; PR:Q1M168; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000020407; Expressed in frontal cortex and 12 other tissues.
DR Genevisible; Q1M168; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0048311; P:mitochondrion distribution; IMP:UniProtKB.
DR GO; GO:2000212; P:negative regulation of glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Mitochondrion; Neurogenesis; Phosphoprotein;
KW Reference proteome; Synapse; Transport; Ubl conjugation.
FT CHAIN 1..372
FT /note="Caytaxin"
FT /id="PRO_0000419970"
FT DOMAIN 171..328
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..120
FT /note="Required for interaction with KLC1"
FT /evidence="ECO:0000250"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..372
FT /note="Mediates interaction with GLS"
FT /evidence="ECO:0000250"
FT REGION 330..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 105..106
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHE3"
SQ SEQUENCE 372 AA; 42117 MW; 091E21129D1ADD34 CRC64;
MGTTEATLRM ENVDVRDEWQ DEDLPRPLPE DTGEDHLGGT VEDSSSPPST LNLSGAHRKR
KTLVAPEINI SLDQSEGSLL SDDFLDTPDD LDINVDDIET PDETDSLEFL GNGNELEWED
DTPVATAKNM PGDSADLFGD GSGEDGSAAN GRLWRTVIIG EQEHRIDLHM IRPYMKVVTH
GGYYGEGLNA IIVFAACFLP DSSSPDYHYI MENLFLYVIS SLELLVAEDY MIVYLNGATP
RRRMPGIGWL KKCYHMIDRR LRKNLKSLII VHPSWFIRTV LAISRPFISV KFISKIQYVH
SLEELEQLIP MEHVQLPACV LQYEEQRLRA KRESARPPQP EFLLPRSEEK PETVEEEDRA
AEVTEDQETS MS
