ATCAY_MOUSE
ID ATCAY_MOUSE Reviewed; 372 AA.
AC Q8BHE3; Q3TR94;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Caytaxin;
GN Name=Atcay;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISEASE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14556008; DOI=10.1038/ng1255;
RA Bomar J.M., Benke P.J., Slattery E.L., Puttagunta R., Taylor L.P.,
RA Seong E., Nystuen A., Chen W., Albin R.L., Patel P.D., Kittles R.A.,
RA Sheffield V.C., Burmeister M.;
RT "Mutations in a novel gene encoding a CRAL-TRIO domain cause human Cayman
RT ataxia and ataxia/dystonia in the jittery mouse.";
RL Nat. Genet. 35:264-269(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Hypothalamus, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP INTERACTION WITH GLS, AND TISSUE SPECIFICITY.
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 [5]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17157273; DOI=10.1016/j.brainres.2006.10.068;
RA Hayakawa Y., Itoh M., Yamada A., Mitsuda T., Nakagawa T.;
RT "Expression and localization of Cayman ataxia-related protein, Caytaxin, is
RT regulated in a developmental- and spatial-dependent manner.";
RL Brain Res. 1129:100-109(2007).
RN [6]
RP FUNCTION IN MITOCHONDRIA LOCALIZATION, INTERACTION WITH KLC1, AND
RP MUTAGENESIS OF 115-GLU--GLU-117 AND 118-TRP--ASP-120.
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP PROTEOLYTIC PROCESSING BY CASP3.
RX PubMed=21369758; DOI=10.1007/s11064-011-0430-5;
RA Itoh M., Li S., Ohta K., Yamada A., Hayakawa-Yano Y., Ueda M., Hida Y.,
RA Suzuki Y., Ohta E., Mizuno A., Banno Y., Nakagawa T.;
RT "Cayman ataxia-related protein is a presynapse-specific caspase-3
RT substrate.";
RL Neurochem. Res. 36:1304-1313(2011).
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: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 (via WW
CC domain); upon NGF stimulation (By similarity). The interaction with
CC PIN1 and GLS is competitive (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:Q1M168}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q1M168}. Presynapse
CC {ECO:0000269|PubMed:17157273}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q1M168}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q1M168}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q86WG3}.
CC -!- TISSUE SPECIFICITY: Neuronal tissues specific. Strongly expressed in
CC brain. Expressed in virtually all parts of the adult brain, including
CC cortex, cerebellum and olfactory bulbs. Enriched in hippocampus,
CC cerebellar cortex, deep cerebellar nuclei, and pontine nuclei (at
CC protein level). {ECO:0000269|PubMed:14556008,
CC ECO:0000269|PubMed:16899818, ECO:0000269|PubMed:17157273}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo, where it is also completely
CC restricted to neuronal tissues, including brain, dorsal root ganglia
CC and enteric nervous system. MRNA and protein expressions are not
CC correlated during development. {ECO:0000269|PubMed:14556008,
CC ECO:0000269|PubMed:17157273}.
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. {ECO:0000269|PubMed:21369758}.
CC -!- PTM: May be ubiquitinated by STUB1. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Atcay are the cause of jittery phenotype,
CC which is characterized by severe truncal and limb ataxia and death due
CC to starvation and dehydration by 3-4 weeks of age.
CC {ECO:0000269|PubMed:14556008}.
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DR EMBL; AY349150; AAQ90064.1; -; mRNA.
DR EMBL; AK028298; BAC25867.1; -; mRNA.
DR EMBL; AK038483; BAC30014.1; -; mRNA.
DR EMBL; AK038990; BAC30195.1; -; mRNA.
DR EMBL; AK039411; BAC30342.1; -; mRNA.
DR EMBL; AK162959; BAE37136.1; -; mRNA.
DR EMBL; BC048903; AAH48903.1; -; mRNA.
DR CCDS; CCDS24047.1; -.
DR RefSeq; NP_848777.1; NM_178662.3.
DR AlphaFoldDB; Q8BHE3; -.
DR BioGRID; 200865; 2.
DR ELM; Q8BHE3; -.
DR STRING; 10090.ENSMUSP00000036721; -.
DR iPTMnet; Q8BHE3; -.
DR PhosphoSitePlus; Q8BHE3; -.
DR SwissPalm; Q8BHE3; -.
DR MaxQB; Q8BHE3; -.
DR PaxDb; Q8BHE3; -.
DR PeptideAtlas; Q8BHE3; -.
DR PRIDE; Q8BHE3; -.
DR ProteomicsDB; 265173; -.
DR Antibodypedia; 23397; 68 antibodies from 19 providers.
DR DNASU; 16467; -.
DR Ensembl; ENSMUST00000047408; ENSMUSP00000036721; ENSMUSG00000034958.
DR GeneID; 16467; -.
DR KEGG; mmu:16467; -.
DR UCSC; uc007ggo.1; mouse.
DR CTD; 85300; -.
DR MGI; MGI:2448730; Atcay.
DR VEuPathDB; HostDB:ENSMUSG00000034958; -.
DR eggNOG; KOG3308; Eukaryota.
DR GeneTree; ENSGT00940000158364; -.
DR HOGENOM; CLU_039135_0_0_1; -.
DR InParanoid; Q8BHE3; -.
DR OMA; AKNMPGN; -.
DR OrthoDB; 755773at2759; -.
DR PhylomeDB; Q8BHE3; -.
DR TreeFam; TF324164; -.
DR BioGRID-ORCS; 16467; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Atcay; mouse.
DR PRO; PR:Q8BHE3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BHE3; protein.
DR Bgee; ENSMUSG00000034958; Expressed in cortical plate and 124 other tissues.
DR ExpressionAtlas; Q8BHE3; baseline and differential.
DR Genevisible; Q8BHE3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR GO; GO:2000212; P:negative regulation of glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IDA: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_0000210769"
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:0000269|PubMed:19861499"
FT REGION 190..372
FT /note="Mediates interaction with GLS"
FT /evidence="ECO:0000250"
FT REGION 329..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Basic and acidic 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:0007744|PubMed:21183079"
SQ SEQUENCE 372 AA; 42178 MW; 299146667F722C11 CRC64;
MGTTEATLRM ENVDVRDEWQ DEDLPRPLPE DTGVERLGGA VEDSSSPPST LNLSGAHRKR
KTLVAPEINI SLDQSEGSLL SDDFLDTPDD LDINVDDIET PDETDSLEFL GNGNELEWED
DTPVATAKNM PGDSADLFGD GSAEDGSAAN GRLWRTVIIG EQEHRIDLHM IRPYMKVVTH
GGYYGEGLNA IIVFAACFLP DSSSPDYHYI MENLFLYVIS SLELLVAEDY MIVYLNGATP
RRRMPGIGWL KKCYHMIDRR LRKNLKSLII VHPSWFIRTV LAISRPFISV KFISKIQYVH
SLEELERLIP MEHVQLPDCV LQYEEQRLRA KRESTRPPQP EFLLPRSEEK PETVEEEDRA
AEATEDQETS MS
