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Q9EPK6

- SIL1_MOUSE

UniProt

Q9EPK6 - SIL1_MOUSE

Protein

Nucleotide exchange factor SIL1

Gene

Sil1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleotide exchange factor SIL1
    Gene namesi
    Name:Sil1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1932040. Sil1.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Mice develop adult-onset ataxia with cerebellar Purkinje cell loss. Affected cells have intracellular protein accumulations in the endoplasmic reticulum and the nucleus.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 465434Nucleotide exchange factor SIL1PRO_0000223355Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9EPK6.
    PaxDbiQ9EPK6.
    PRIDEiQ9EPK6.

    PTM databases

    PhosphoSiteiQ9EPK6.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Developmental stagei

    Expressed in the developing retina and epithelial cells of the lens at E12.5. Expressed in the developing cerebral cortex at E15.5.1 Publication

    Gene expression databases

    BgeeiQ9EPK6.
    GenevestigatoriQ9EPK6.

    Interactioni

    Subunit structurei

    Interacts with HSPA5.1 Publication

    Protein-protein interaction databases

    BioGridi219881. 2 interactions.
    IntActiQ9EPK6. 1 interaction.
    MINTiMINT-4128883.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPK6.
    SMRiQ9EPK6. Positions 199-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 260260Interaction with HSPA5 and localization to the endoplasmic reticulumAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SIL1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG310365.
    GeneTreeiENSGT00510000048102.
    HOGENOMiHOG000154326.
    HOVERGENiHBG093955.
    InParanoidiQ9EPK6.
    KOiK14001.
    OMAiQGWCEIT.
    OrthoDBiEOG72G176.
    PhylomeDBiQ9EPK6.
    TreeFamiTF324307.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9EPK6-1 [UniParc]FASTAAdd to Basket

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    MAPQHLPSTR MASPGMLLGL LLTSCLTLCL SCQNSNNFAL TNPEKSIHQE    50
    SDTKETREEE ELDTEILEVF HPTQEWQTLQ PGQAVPAGSH VRMNLQTGVN 100
    EVKLQQEDKF QNNLKGFKRG RRLDINANTY TSQDLKSALA KFKEGTEMEN 150
    SKDELARQAT VKQLFRPIEE LKKEFDELNV VLETDMQIMV RLINKFNSSS 200
    SSLEEKVAAL FDLEYYVHQM DNAQDLLSFG GLQVVINGLN STEPLVKEYA 250
    AFVLGAAFSS NPKVQVEAIE GGALQKLLVI LATNQPLPAK KKVLFALCSL 300
    LRHFPYAQQQ FLKLGGLQVL RSLVQEKSAK VLAVRVVTLL YDLVTEKMFA 350
    EEEAELTQDS SPEKLQQYRQ VQLLPGLQEQ GWCEITAQLL ALPEHDAREK 400
    VLQTLGALLT TCRDRYRQDL QLSRTLGRLQ AEYQALASLE LQEGEDDGYF 450
    RELLASINSL MKELR 465
    Length:465
    Mass (Da):52,430
    Last modified:February 21, 2006 - v2
    Checksum:iC3E2DB44394F1161
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431K → T in CAC17789. (PubMed:11101517)Curated
    Sequence conflicti152 – 1521K → Q in CAC17789. (PubMed:11101517)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ297884 mRNA. Translation: CAC17789.1.
    AK170415 mRNA. Translation: BAE41781.1.
    BC016119 mRNA. Translation: AAH16119.1.
    BC016466 mRNA. Translation: AAH16466.1.
    CCDSiCCDS29140.1.
    RefSeqiNP_109674.2. NM_030749.2.
    XP_006526428.1. XM_006526365.1.
    XP_006526429.1. XM_006526366.1.
    UniGeneiMm.291482.

    Genome annotation databases

    EnsembliENSMUST00000025215; ENSMUSP00000025215; ENSMUSG00000024357.
    GeneIDi81500.
    KEGGimmu:81500.
    UCSCiuc008emc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ297884 mRNA. Translation: CAC17789.1 .
    AK170415 mRNA. Translation: BAE41781.1 .
    BC016119 mRNA. Translation: AAH16119.1 .
    BC016466 mRNA. Translation: AAH16466.1 .
    CCDSi CCDS29140.1.
    RefSeqi NP_109674.2. NM_030749.2.
    XP_006526428.1. XM_006526365.1.
    XP_006526429.1. XM_006526366.1.
    UniGenei Mm.291482.

    3D structure databases

    ProteinModelPortali Q9EPK6.
    SMRi Q9EPK6. Positions 199-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 219881. 2 interactions.
    IntActi Q9EPK6. 1 interaction.
    MINTi MINT-4128883.

    PTM databases

    PhosphoSitei Q9EPK6.

    Proteomic databases

    MaxQBi Q9EPK6.
    PaxDbi Q9EPK6.
    PRIDEi Q9EPK6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025215 ; ENSMUSP00000025215 ; ENSMUSG00000024357 .
    GeneIDi 81500.
    KEGGi mmu:81500.
    UCSCi uc008emc.2. mouse.

    Organism-specific databases

    CTDi 64374.
    MGIi MGI:1932040. Sil1.

    Phylogenomic databases

    eggNOGi NOG310365.
    GeneTreei ENSGT00510000048102.
    HOGENOMi HOG000154326.
    HOVERGENi HBG093955.
    InParanoidi Q9EPK6.
    KOi K14001.
    OMAi QGWCEIT.
    OrthoDBi EOG72G176.
    PhylomeDBi Q9EPK6.
    TreeFami TF324307.

    Miscellaneous databases

    ChiTaRSi SIL1. mouse.
    NextBioi 350402.
    PROi Q9EPK6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EPK6.
    Genevestigatori Q9EPK6.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    6. Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiSIL1_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPK6
    Secondary accession number(s): Q91V34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3