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Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (ATP/GTP-binding protein 1) (Nervous system nuclear protein induced by axotomy protein 1)

 CBPC1_MOUSE             Reviewed;        1218 AA.
Q641K1; Q3TDS0; Q3V147; Q6P9R9; Q8C1K8; Q9D962; Q9EQI4;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 2.
10-MAY-2017, entry version 106.
RecName: Full=Cytosolic carboxypeptidase 1;
EC=3.4.17.-;
AltName: Full=ATP/GTP-binding protein 1;
AltName: Full=Nervous system nuclear protein induced by axotomy protein 1;
Name=Agtpbp1; Synonyms=Ccp1, Nna1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INDUCTION BY AXON REGENERATION, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
PubMed=11083920; DOI=10.1006/mcne.2000.0900;
Harris A., Morgan J.I., Pecot M., Soumare A., Osborne A., Soares H.D.;
"Regenerating motor neurons express Nna1, a novel ATP/GTP-binding
protein related to zinc carboxypeptidases.";
Mol. Cell. Neurosci. 16:578-596(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1115-1218 (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Pancreas, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INVOLVEMENT IN PCD, INDUCTION BY AXONAL REGENERATION, AND TISSUE
SPECIFICITY.
PubMed=11884758; DOI=10.1126/science.1068912;
Fernandez-Gonzalez A., La Spada A.R., Treadaway J., Higdon J.C.,
Harris B.S., Sidman R.L., Morgan J.I., Zuo J.;
"Purkinje cell degeneration (pcd) phenotypes caused by mutations in
the axotomy-induced gene, Nna1.";
Science 295:1904-1906(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
VARIANT PCD ASP-832 INS.
PubMed=16465590; DOI=10.1007/s00335-005-0096-x;
Chakrabarti L., Neal J.T., Miles M., Martinez R.A., Smith A.C.,
Sopher B.L., La Spada A.R.;
"The Purkinje cell degeneration 5J mutation is a single amino acid
insertion that destabilizes Nna1 protein.";
Mamm. Genome 17:103-110(2006).
[7]
INVOLVEMENT IN PCD.
PubMed=16942761; DOI=10.1016/j.brainres.2006.07.065;
Wang T., Morgan J.I.;
"The Purkinje cell degeneration (pcd) mouse: an unexpected molecular
link between neuronal degeneration and regeneration.";
Brain Res. 1140:26-40(2007).
[8]
INVOLVEMENT IN PCD, AND MUTAGENESIS OF 971-ASN-ARG-972.
PubMed=16952463; DOI=10.1016/j.mcn.2006.07.009;
Wang T., Parris J., Li L., Morgan J.I.;
"The carboxypeptidase-like substrate-binding site in Nna1 is essential
for the rescue of the Purkinje cell degeneration (pcd) phenotype.";
Mol. Cell. Neurosci. 33:200-213(2006).
[9]
INVOLVEMENT IN PCD, AND MUTAGENESIS OF HIS-912 AND GLU-915.
PubMed=18602413; DOI=10.1016/j.visres.2008.05.026;
Chakrabarti L., Eng J., Martinez R.A., Jackson S., Huang J.,
Possin D.E., Sopher B.L., La Spada A.R.;
"The zinc-binding domain of Nna1 is required to prevent retinal
photoreceptor loss and cerebellar ataxia in Purkinje cell degeneration
(pcd) mice.";
Vision Res. 48:1999-2005(2008).
[10]
FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN PCD, INTERACTION WITH
MYLK, AND MUTAGENESIS OF HIS-912 AND GLU-915.
PubMed=21074048; DOI=10.1016/j.cell.2010.10.014;
Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C.,
Bosson A., Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N.,
Larroque C., Desagher S., Holzer M., Andrieux A., Moutin M.J.,
Janke C.;
"A family of protein-deglutamylating enzymes associated with
neurodegeneration.";
Cell 143:564-578(2010).
[11]
INVOLVEMENT IN PCD, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-912
AND GLU-915.
PubMed=20620870; DOI=10.1016/j.neuron.2010.05.024;
Chakrabarti L., Zahra R., Jackson S.M., Kazemi-Esfarjani P.,
Sopher B.L., Mason A.G., Toneff T., Ryu S., Shaffer S., Kansy J.W.,
Eng J., Merrihew G., MacCoss M.J., Murphy A., Goodlett D.R., Hook V.,
Bennett C.L., Pallanck L.J., La Spada A.R.;
"Mitochondrial dysfunction in NnaD mutant flies and Purkinje cell
degeneration mice reveals a role for Nna proteins in neuronal
bioenergetics.";
Neuron 66:835-847(2010).
[12]
INVOLVEMENT IN PCD.
PubMed=20920790; DOI=10.1016/j.neuron.2010.08.013;
Li J., Gu X., Ma Y., Calicchio M.L., Kong D., Teng Y.D., Yu L.,
Crain A.M., Vartanian T.K., Pasqualini R., Arap W., Libermann T.A.,
Snyder E.Y., Sidman R.L.;
"Nna1 mediates Purkinje cell dendritic development via lysyl oxidase
propeptide and NF-kappaB signaling.";
Neuron 68:45-60(2010).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25103237; DOI=10.1091/mbc.E14-06-1072;
Tort O., Tanco S., Rocha C., Bieche I., Seixas C., Bosc C.,
Andrieux A., Moutin M.J., Aviles F.X., Lorenzo J., Janke C.;
"The cytosolic carboxypeptidases CCP2 and CCP3 catalyze
posttranslational removal of acidic amino acids.";
Mol. Biol. Cell 25:3017-3027(2014).
-!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
target proteins. Catalyzes the deglutamylation of polyglutamate
side chains generated by post-translational polyglutamylation in
proteins such as tubulins. Also removes gene-encoded
polyglutamates from the carboxy-terminus of target proteins such
as MYLK. Acts as a long-chain deglutamylase and specifically
shortens long polyglutamate chains, while it is not able to remove
the branching point glutamate, a process catalyzed by AGBL5/CCP5.
Deglutamylation plays a key role in cerebellar Purkinje cell
differentiation, accumulation of tubulin polyglutamylation causing
neurodegeneration. {ECO:0000269|PubMed:21074048,
ECO:0000269|PubMed:25103237}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with MYLK. {ECO:0000269|PubMed:21074048}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}.
Cytoplasm, cytosol {ECO:0000269|PubMed:11083920}. Nucleus
{ECO:0000269|PubMed:11083920}. Mitochondrion
{ECO:0000269|PubMed:20620870}. Note=Localizes in both the
cytoplasm and nuclei of interphase and dividing cells.
{ECO:0000250|UniProtKB:Q9UPW5}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q641K1-1; Sequence=Displayed;
Name=2;
IsoId=Q641K1-2; Sequence=VSP_029047, VSP_029048;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q641K1-3; Sequence=VSP_029045, VSP_029046;
Note=No experimental confirmation available. Apparent retained
intron. May be produced at very low levels due to a premature
stop codon in the mRNA, leading to nonsense-mediated mRNA
decay.;
Name=4;
IsoId=Q641K1-4; Sequence=VSP_038803, VSP_038805;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q641K1-5; Sequence=VSP_038804;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the
cerebellum and cortex of adult mouse brain. Expressed at similar
levels in both the cerebellum and the cortex throughout all
developmental stages. Also expressed in sciatic nerve transection,
spinal motor neurons undergoing axon regeneration, testis, heart
and in developing brain. Expression in cranial motor nuclei is the
same as that observed in uninjured primary motor neurons.
Expression is prevalent in sensory neurons and hippocampal CA3
neurons in addition to regenerating motor neurons.
{ECO:0000269|PubMed:11884758, ECO:0000269|PubMed:21074048,
ECO:0000269|PubMed:25103237}.
-!- DEVELOPMENTAL STAGE: Highly expressed in differentiating neurons.
From E16.5, expression is widespread in brain, spinal cord, and
peripheral nervous tissue. Within the developing CNS, expression
is restricted to regions of brain and spinal cord containing
differentiating neurons. {ECO:0000269|PubMed:11083920}.
-!- INDUCTION: By axonal regeneration. {ECO:0000269|PubMed:11083920,
ECO:0000269|PubMed:11884758}.
-!- DISEASE: Note=Defects in Agtpbp1 are the cause of Purkinje cell
degeneration (pcd). Pcd is a spontaneous mutation that causes
adult-onset degeneration of cerebellar Purkinje neurons, retinal
photoreceptors, olfactory bulb mitral neurons, and selected
thalamic neurons, and has defective spermatogenesis. Defects in
mitochondrial metabolic functions are also observed. The molecular
causes of neurodegeneration are still unclear, but they are
probably due to an accumulation of glutamylation, either tubulin
hyperglutamylation or another hyperglutamylated target proteins.
An increase of intranuclear localization of lysyl oxidase (Lox)
propeptide, which interferes with NF-kappa-B Rela signaling and
microtubule-associated protein regulation of microtubule stability
is also observed, possibly leading to underdevelopment of Purkinje
cell dendrites. {ECO:0000269|PubMed:11884758,
ECO:0000269|PubMed:16465590, ECO:0000269|PubMed:16942761,
ECO:0000269|PubMed:16952463, ECO:0000269|PubMed:18602413,
ECO:0000269|PubMed:20620870, ECO:0000269|PubMed:20920790,
ECO:0000269|PubMed:21074048}.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG37102.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF219141; AAG37102.1; ALT_INIT; mRNA.
EMBL; AK007328; BAB24963.2; -; mRNA.
EMBL; AK013688; BAC25412.1; -; mRNA.
EMBL; AK132695; BAE21306.1; -; mRNA.
EMBL; AK170046; BAE41530.1; -; mRNA.
EMBL; BC082335; AAH82335.1; -; mRNA.
EMBL; BC060633; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS36686.1; -. [Q641K1-1]
CCDS; CCDS36687.1; -. [Q641K1-4]
CCDS; CCDS70470.1; -. [Q641K1-2]
RefSeq; NP_001041473.1; NM_001048008.2. [Q641K1-4]
RefSeq; NP_001271147.1; NM_001284218.1. [Q641K1-4]
RefSeq; NP_001271148.1; NM_001284219.1.
RefSeq; NP_001271150.1; NM_001284221.1. [Q641K1-2]
RefSeq; NP_075817.2; NM_023328.3. [Q641K1-1]
RefSeq; XP_006517398.1; XM_006517335.2. [Q641K1-1]
RefSeq; XP_006517399.1; XM_006517336.3. [Q641K1-1]
RefSeq; XP_006517400.1; XM_006517337.3. [Q641K1-1]
RefSeq; XP_006517401.1; XM_006517338.3. [Q641K1-1]
RefSeq; XP_011242857.1; XM_011244555.2. [Q641K1-2]
UniGene; Mm.153008; -.
ProteinModelPortal; Q641K1; -.
STRING; 10090.ENSMUSP00000022040; -.
iPTMnet; Q641K1; -.
PhosphoSitePlus; Q641K1; -.
EPD; Q641K1; -.
PaxDb; Q641K1; -.
PRIDE; Q641K1; -.
Ensembl; ENSMUST00000022040; ENSMUSP00000022040; ENSMUSG00000021557. [Q641K1-1]
Ensembl; ENSMUST00000109830; ENSMUSP00000105456; ENSMUSG00000021557. [Q641K1-4]
Ensembl; ENSMUST00000164215; ENSMUSP00000130939; ENSMUSG00000021557. [Q641K1-2]
Ensembl; ENSMUST00000170555; ENSMUSP00000128589; ENSMUSG00000021557. [Q641K1-3]
Ensembl; ENSMUST00000171606; ENSMUSP00000132697; ENSMUSG00000021557. [Q641K1-4]
GeneID; 67269; -.
KEGG; mmu:67269; -.
UCSC; uc007qum.1; mouse. [Q641K1-1]
UCSC; uc007quq.2; mouse. [Q641K1-4]
UCSC; uc033gmf.1; mouse. [Q641K1-2]
CTD; 23287; -.
MGI; MGI:2159437; Agtpbp1.
eggNOG; KOG3641; Eukaryota.
eggNOG; COG2866; LUCA.
GeneTree; ENSGT00550000074405; -.
HOVERGEN; HBG107587; -.
InParanoid; Q641K1; -.
OMA; HIAPAFC; -.
OrthoDB; EOG091G01L5; -.
PhylomeDB; Q641K1; -.
TreeFam; TF313794; -.
PRO; PR:Q641K1; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021557; -.
CleanEx; MM_AGTPBP1; -.
ExpressionAtlas; Q641K1; baseline and differential.
Genevisible; Q641K1; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; TAS:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0035609; P:C-terminal protein deglutamylation; IDA:UniProtKB.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:UniProtKB.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0001754; P:eye photoreceptor cell differentiation; IMP:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
GO; GO:0042133; P:neurotransmitter metabolic process; IMP:MGI.
GO; GO:0021772; P:olfactory bulb development; IMP:UniProtKB.
GO; GO:0035610; P:protein side chain deglutamylation; IDA:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
CDD; cd06906; M14_Nna1; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR033852; Cytosolic_aminopeptidase_1.
InterPro; IPR000834; Peptidase_M14.
Pfam; PF00246; Peptidase_M14; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Alternative splicing; Carboxypeptidase; Complete proteome; Cytoplasm;
Disease mutation; Hydrolase; Metal-binding; Metalloprotease;
Mitochondrion; Neurodegeneration; Nucleus; Phosphoprotein; Protease;
Reference proteome; Zinc.
CHAIN 1 1218 Cytosolic carboxypeptidase 1.
/FTId=PRO_0000308691.
ACT_SITE 962 962 Nucleophile. {ECO:0000250}.
METAL 912 912 Zinc. {ECO:0000305}.
METAL 915 915 Zinc. {ECO:0000305}.
METAL 1009 1009 Zinc. {ECO:0000250}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPW5}.
VAR_SEQ 689 1218 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038804.
VAR_SEQ 771 795 GMQPLMYSVQEALNARPWWIRMGTD -> EITSHEAQLPQA
DRRASPTTPSPSP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029045.
VAR_SEQ 771 789 GMQPLMYSVQEALNARPWW -> DGEETCYKMIVVSTICCK
D (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038803.
VAR_SEQ 790 1218 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038805.
VAR_SEQ 796 1218 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029046.
VAR_SEQ 1160 1174 SPTTYVLDEDEPRFL -> RTRGSSELQLFPAVL (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029047.
VAR_SEQ 1175 1218 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029048.
VARIANT 832 832 D -> DD (in pcd; pcd(5J) mutant).
{ECO:0000269|PubMed:16465590}.
MUTAGEN 912 912 H->A: Abolishes ability to rescue
Purkinje cell degeneration in pcd mice
when expressed in a transgene.
{ECO:0000269|PubMed:18602413,
ECO:0000269|PubMed:20620870,
ECO:0000269|PubMed:21074048}.
MUTAGEN 912 912 H->S: Abolishes deglutamylase activity;
when associated with Q-915.
{ECO:0000269|PubMed:18602413,
ECO:0000269|PubMed:20620870,
ECO:0000269|PubMed:21074048}.
MUTAGEN 915 915 E->A: Abolishes ability to rescue
Purkinje cell degeneration in pcd mice
when expressed in a transgene.
{ECO:0000269|PubMed:18602413,
ECO:0000269|PubMed:20620870,
ECO:0000269|PubMed:21074048}.
MUTAGEN 915 915 E->Q: Abolishes deglutamylase activity;
when associated with S-912.
{ECO:0000269|PubMed:18602413,
ECO:0000269|PubMed:20620870,
ECO:0000269|PubMed:21074048}.
MUTAGEN 971 972 NR->AA: Abolishes ability to rescue
Purkinje cell degeneration in pcd mice
when expressed in a transgene.
{ECO:0000269|PubMed:16952463}.
CONFLICT 237 237 A -> V (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 274 274 Q -> R (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 380 380 V -> A (in Ref. 3; BC060633).
{ECO:0000305}.
CONFLICT 542 548 NAGMRKD -> ERRNEEG (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 644 644 F -> S (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 969 969 D -> G (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 1043 1043 D -> G (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 1121 1121 K -> Q (in Ref. 1; AAG37102).
{ECO:0000305}.
CONFLICT 1126 1126 L -> I (in Ref. 2; BAC25412).
{ECO:0000305}.
CONFLICT 1167 1167 D -> G (in Ref. 2; BAB24963).
{ECO:0000305}.
SEQUENCE 1218 AA; 137197 MW; 89917C6897AD9DD5 CRC64;
MSKLKVVGEK SLTNSSRVVG LLAQLEKINT DSTESDTARY VTSKILHLAQ SQEKTRREMT
TKGSTGMEVL LSTLENTKDL QTVLNILSIL IELVSSGGGR RASFLVAKGG SQILLQLLMN
ASKDSPPHEE VMVQTHSILA KIGPKDKKFG VKARVNGALT VTLNLVKQHF QNYRLVLPCL
QLLRVYSTNS VNSVSLGKNG VVELMFKIIG PFSKKNSGLM KVALDTLAAL LKSKTNARRA
VDRGYVQVLL TIYVDWHRHD NRHRNMLIRK GILQSLKSVT NIKLGRKAFI DANGMKILYN
TSQECLAVRT LDPLVNTSSL IMRKCFPKNR LPLPTIKSSF HFQLPIIPVT GPVAQLYSLP
PEVDDVVDES DDNDDIDLEV ENELENEDDL DQSFKNDDIE TDINKLRPQQ VPGRTIEELK
MYEHLFPELV DDFQDYELIS KEPKPFVFEG KARGPIVVPT AGEEVPGNSG SVKKGVVMKE
RASPKGEEAK EDPKGHDRTL PQQLGGQSRV APSAHSFNND LVKALDRITL QNVPSQVASG
LNAGMRKDFG LPLTVLSCTK ACPHVAKCGS TLFEGRTVHL GKLCCTGVET EDDEDTESHS
STEQAPSVEA SDGPTLHDPD LYIEIVKNTK SVPEYSEVAY PDYFGHIPPP FKEPILERPY
GVQRTKIAQD IERLIHQNDI IDRVVYDLDN PTYTTPEEGD TLKFNSKFES GNLRKVIQIR
KSEYDLILNS DINSNHYHQW FYFEVSGMRP GVAYRFNIIN CEKSNSQFNY GMQPLMYSVQ
EALNARPWWI RMGTDICYYK NHFSRSSVAA GGQKGKSYYT ITFTVNFPHK DDVCYFAYHY
PYTYSTLQMH LQKLESAHNP QQIYFRKDVL CETLSGNICP LVTITAMPES NYYEHICQFR
TRPYIFLSAR VHPGETNASW VMKGTLEYLM SNSPTAQSLR ESYIFKIVPM LNPDGVINGN
HRCSLSGEDL NRQWQSPNPE LHPTIYHAKG LLQYLAAVKR LPLVYCDYHG HSRKKNVFMY
GCSIKETVWH THDNSASCDI VEDMGYRTLP KILSHIAPAF CMSSCSFVVE KSKESTARVV
VWREIGVQRS YTMESTLCGC DQGRYKGLQI GTRELEEMGA KFCVGLLRLK RLTSSLEYNL
PSNLLDFEND LIESSCKVTS PTTYVLDEDE PRFLEEVDYS AESNDELDVE LAENTGDYEP
SAQEEALSDS EVSRTHLI


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