CEND_RAT
ID CEND_RAT Reviewed; 149 AA.
AC Q5FVI4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cell cycle exit and neuronal differentiation protein 1;
GN Name=Cend1;
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 [LARGE SCALE MRNA].
RC 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 [2]
RP PROTEIN SEQUENCE OF 17-25; 34-41; 49-61 AND 99-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in neuronal differentiation.
CC {ECO:0000250|UniProtKB:Q9JKC6}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with AHI1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8N111,
CC ECO:0000250|UniProtKB:Q9JKC6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CEND1 family. {ECO:0000305}.
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DR EMBL; BC089963; AAH89963.1; -; mRNA.
DR RefSeq; NP_001014185.1; NM_001014163.1.
DR RefSeq; XP_003749055.1; XM_003749007.4.
DR RefSeq; XP_008772956.1; XM_008774734.2.
DR AlphaFoldDB; Q5FVI4; -.
DR BioGRID; 262868; 2.
DR IntAct; Q5FVI4; 1.
DR MINT; Q5FVI4; -.
DR STRING; 10116.ENSRNOP00000024867; -.
DR iPTMnet; Q5FVI4; -.
DR PhosphoSitePlus; Q5FVI4; -.
DR jPOST; Q5FVI4; -.
DR PaxDb; Q5FVI4; -.
DR PRIDE; Q5FVI4; -.
DR Ensembl; ENSRNOT00000116264; ENSRNOP00000087482; ENSRNOG00000062814.
DR GeneID; 361675; -.
DR KEGG; rno:361675; -.
DR UCSC; RGD:1309401; rat.
DR CTD; 51286; -.
DR RGD; 1309401; Cend1.
DR eggNOG; ENOG502SGTV; Eukaryota.
DR GeneTree; ENSGT00390000012831; -.
DR HOGENOM; CLU_1748972_0_0_1; -.
DR InParanoid; Q5FVI4; -.
DR OMA; FFDNMKP; -.
DR OrthoDB; 1547337at2759; -.
DR PhylomeDB; Q5FVI4; -.
DR TreeFam; TF336209; -.
DR PRO; PR:Q5FVI4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018448; Expressed in cerebellum and 10 other tissues.
DR ExpressionAtlas; Q5FVI4; baseline.
DR Genevisible; Q5FVI4; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0021686; P:cerebellar granular layer maturation; ISO:RGD.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0021933; P:radial glia guided migration of cerebellar granule cell; ISO:RGD.
DR InterPro; IPR020162; Cend1.
DR PANTHER; PTHR36683; PTHR36683; 1.
DR Pfam; PF15677; CEND1; 1.
PE 1: Evidence at protein level;
KW Differentiation; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..149
FT /note="Cell cycle exit and neuronal differentiation protein
FT 1"
FT /id="PRO_0000245465"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKC6"
SQ SEQUENCE 149 AA; 15043 MW; 196D56164631009F CRC64;
MESRGKSASS PKPDTKVPQA TAEAKATPAA DGKAPLTKPV KKDAQAEKQE QPAAPGPATT
KKTPAKADPV LLNNHSNLKP APTVPAAPSS PDTTSEPKGP GDGAEEDESN TGGRGPWPCE
NLTPLLVAGG VAVATIALIL GVAFLARKK
