Q8R3J5 (CHAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cation transport regulator-like protein 1

Alternative name(s):
Blocks Notch protein
Short name=Botch

Gene names

Name:	Chac1
Synonyms:	Botch

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Notch in an immature inactive form, thereby promoting neurogenesis in embryos. May also act as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. Ref.4
Subunit structure	Interacts with NOTCH1 (via extracellular region). Ref.4
Subcellular location	Cytoplasm › cytosol By similarity. Golgi apparatus › trans-Golgi network Ref.4.
Tissue specificity	Widely expressed, with high expression in forebrain and anterior spinal cord. Expressed at intermediate level in the dorsal aorta and heart. Present throughout adult brain (at protein level). Ref.4
Sequence similarities	Belongs to the chaC family.

Ontologies

Keywords
Biological process	Apoptosis Neurogenesis Notch signaling pathway Unfolded protein response
Cellular component	Cytoplasm Golgi apparatus
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of Notch signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein processing Inferred from sequence or structural similarity. Source: UniProtKB neurogenesis Inferred from mutant phenotype Ref.4. Source: UniProtKB response to unfolded protein Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB trans-Golgi network Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	Notch binding Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 223	223	Cation transport regulator-like protein 1		PRO_0000239011
Experimental info
	Sequence conflict	25	1	S → F in AAH25169. Ref.3
	Sequence conflict	89	1	R → H in AAH25169. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8R3J5 [UniParc]. Last modified June 13, 2012. Version 2. Checksum: 2DF793150C1C3B67	FASTA	223	24,547
	10 20 30 40 50 60 MKQESASQST PPPSLSPAPS SAQPSWGDGD PQALWIFGYG SLVWKPDFAY SDSRVGFVRG 70 80 90 100 110 120 YSRRFWQGDT FHRGSDKMPG RVVTLLEDRE GCTWGVAYQV RGEQVNEALK YLNVREAVLG 130 140 150 160 170 180 GYDTKEVTFY PQDTPDQPLT ALAYVATPQN PGYLGPAPEE VIATQILACR GFSGHNLEYL 190 200 210 220 LRLADFMQLC GPQAQDEHLE AIVDAVGTLL PCSYLPEQPL ALT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Olfactory bulb and Pancreas.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Botch promotes neurogenesis by antagonizing Notch." Chi Z., Zhang J., Tokunaga A., Harraz M.M., Byrne S.T., Dolinko A., Xu J., Blackshaw S., Gaiano N., Dawson T.M., Dawson V.L. Dev. Cell 22:707-720(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NOTCH1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK007378 mRNA. Translation: BAB24997.1. AK032218 mRNA. Translation: BAC27764.1. AL929318 Genomic DNA. Translation: CAM25343.1. BC025169 mRNA. Translation: AAH25169.1.
IPI	IPI00387471. IPI00828928.
RefSeq	NP_081205.1. NM_026929.4.
UniGene	Mm.35083.
3D structure databases
ProteinModelPortal	Q8R3J5.
ModBase	Search...
PTM databases
PhosphoSite	Q8R3J5.
Proteomic databases
PRIDE	Q8R3J5.
Protocols and materials databases
DNASU	69065.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028780; ENSMUSP00000028780; ENSMUSG00000027313.
GeneID	69065.
KEGG	mmu:69065.
Organism-specific databases
CTD	79094.
MGI	MGI:1916315. Chac1.
Phylogenomic databases
eggNOG	COG3703.
GeneTree	ENSGT00390000003855.
HOGENOM	HOG000264264.
HOVERGEN	HBG056733.
InParanoid	Q8R3J5.
KO	K07232.
OMA	GDPQALW.
OrthoDB	EOG40CHJ2.
Gene expression databases
ArrayExpress	Q8R3J5.
Bgee	Q8R3J5.
CleanEx	MM_CHAC1.
Genevestigator	Q8R3J5.
GermOnline	ENSMUSG00000027313. Mus musculus.
Family and domain databases
Gene3D	3.10.490.10. 1 hit.
InterPro	IPR013024. Butirosin_synth_BtrG-like. IPR006840. ChaC. [Graphical view]
PANTHER	PTHR12192. PTHR12192. 1 hit.
Pfam	PF04752. ChaC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	328512.
SOURCE	Search...

Entry information

Entry name

CHAC1_MOUSE

Accession

Primary (citable) accession number: Q8R3J5
Secondary accession number(s): A2AV63, Q9D944

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	June 13, 2012
Last modified:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program