Q9EPK6 (SIL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleotide exchange factor SIL1

Gene names

Name:

Sil1

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	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5 By similarity.
Subunit structure	Interacts with HSPA5. Ref.4
Subcellular location	Endoplasmic reticulum lumen Ref.4.
Tissue specificity	Expressed in several areas of the brain including the cerebellum, cerebral cortex, cortical neurons, glial cells of white matter, hippocampus, olfactory bulb, Purkinje cells, inferior olive and the choroids plexus. Also expressed in the eye and skeletal muscle. Ref.4 Ref.5 Ref.6
Developmental stage	Expressed in the developing retina and epithelial cells of the lens at E12.5. Expressed in the developing cerebral cortex at E15.5. Ref.5
Post-translational modification	N-glycosylated By similarity.
Disruption phenotype	Mice develop adult-onset ataxia with cerebellar Purkinje cell loss. Affected cells have intracellular protein accumulations in the endoplasmic reticulum and the nucleus. Ref.5
Sequence similarities	Belongs to the SIL1 family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Endoplasmic reticulum
Domain	Signal
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.4. Source: MGI endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 465	434	Nucleotide exchange factor SIL1		PRO_0000223355
Regions
	Region	1 – 260	260	Interaction with HSPA5 and localization to the endoplasmic reticulum
Amino acid modifications
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	240	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	143	1	K → T in CAC17789. Ref.1
	Sequence conflict	152	1	K → Q in CAC17789. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9EPK6 [UniParc]. Last modified February 21, 2006. Version 2. Checksum: C3E2DB44394F1161	FASTA	465	52,430
	10 20 30 40 50 60 MAPQHLPSTR MASPGMLLGL LLTSCLTLCL SCQNSNNFAL TNPEKSIHQE SDTKETREEE 70 80 90 100 110 120 ELDTEILEVF HPTQEWQTLQ PGQAVPAGSH VRMNLQTGVN EVKLQQEDKF QNNLKGFKRG 130 140 150 160 170 180 RRLDINANTY TSQDLKSALA KFKEGTEMEN SKDELARQAT VKQLFRPIEE LKKEFDELNV 190 200 210 220 230 240 VLETDMQIMV RLINKFNSSS SSLEEKVAAL FDLEYYVHQM DNAQDLLSFG GLQVVINGLN 250 260 270 280 290 300 STEPLVKEYA AFVLGAAFSS NPKVQVEAIE GGALQKLLVI LATNQPLPAK KKVLFALCSL 310 320 330 340 350 360 LRHFPYAQQQ FLKLGGLQVL RSLVQEKSAK VLAVRVVTLL YDLVTEKMFA EEEAELTQDS 370 380 390 400 410 420 SPEKLQQYRQ VQLLPGLQEQ GWCEITAQLL ALPEHDAREK VLQTLGALLT TCRDRYRQDL 430 440 450 460 QLSRTLGRLQ AEYQALASLE LQEGEDDGYF RELLASINSL MKELR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum." Tyson J.R., Stirling C.J. EMBO J. 19:6440-6452(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[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]	"Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP." Zhao L., Longo-Guess C., Harris B.S., Lee J.-W., Ackerman S.L. Nat. Genet. 37:974-979(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"The gene disrupted in Marinesco-Sjoegren syndrome encodes SIL1, an HSPA5 cochaperone." Anttonen A.-K., Mahjneh I., Haemaelaeinen R.H., Lagier-Tourenne C., Kopra O., Waris L., Anttonen M., Joensuu T., Kalimo H., Paetau A., Tranebjaerg L., Chaigne D., Koenig M., Eeg-Olofsson O., Udd B., Somer M., Somer H., Lehesjoki A.-E. Nat. Genet. 37:1309-1311(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[6]	"Mutations in SIL1 cause Marinesco-Sjoegren syndrome, a cerebellar ataxia with cataract and myopathy." Senderek J., Krieger M., Stendel C., Bergmann C., Moser M., Breitbach-Faller N., Rudnik-Schoeneborn S., Blaschek A., Wolf N.I., Harting I., North K., Smith J., Muntoni F., Brockington M., Quijano-Roy S., Renault F., Herrmann R., Hendershot L.M. , Schroeder J.M., Lochmueller H., Topaloglu H., Voit T., Weis J., Ebinger F., Zerres K. Nat. Genet. 37:1312-1314(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ297884 mRNA. Translation: CAC17789.1. AK170415 mRNA. Translation: BAE41781.1. BC016119 mRNA. Translation: AAH16119.1. BC016466 mRNA. Translation: AAH16466.1.
IPI	IPI00338561.
RefSeq	NP_109674.2. NM_030749.2.
UniGene	Mm.291482.
3D structure databases
ProteinModelPortal	Q9EPK6.
SMR	Q9EPK6. Positions 188-303.
ModBase	Search...
PTM databases
PhosphoSite	Q9EPK6.
Proteomic databases
PaxDb	Q9EPK6.
PRIDE	Q9EPK6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025215; ENSMUSP00000025215; ENSMUSG00000024357.
GeneID	81500.
KEGG	mmu:81500.
UCSC	uc008emc.2. mouse.
Organism-specific databases
CTD	64374.
MGI	MGI:1932040. Sil1.
Phylogenomic databases
eggNOG	NOG310365.
GeneTree	ENSGT00510000048102.
HOGENOM	HOG000154326.
HOVERGEN	HBG093955.
InParanoid	Q9EPK6.
KO	K14001.
OMA	EHDAREK.
OrthoDB	EOG47H5QQ.
Gene expression databases
Bgee	Q9EPK6.
Genevestigator	Q9EPK6.
GermOnline	ENSMUSG00000024357. Mus musculus.
Family and domain databases
Gene3D	1.25.10.10. 1 hit.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SIL1. mouse.
NextBio	350402.
SOURCE	Search...

Entry information

Entry name

SIL1_MOUSE

Accession

Primary (citable) accession number: Q9EPK6
Secondary accession number(s): Q91V34

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	February 21, 2006
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program