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P70302 (STIM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromal interaction molecule 1
Gene names
Name:Stim1
Synonyms:Sim
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in mediating Ca2+ influx following depletion of intracellular Ca2+ stores. Acts as Ca2+ sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca2+ depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca2+ release-activated Ca2+ (CRAC) channel subunit, TMEM142A/ORAI1 By similarity.

Subunit structure

Forms homooligomers and heterooligomers with STIM2. Interacts with ORAI1. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with EFCAB4B/CRACR2A; the interaction is direct and takes place in absence of Ca2+. Forms a complex with EFCAB4B/CRACR2A and ORAI1 at low concentration of Ca2+, the complex dissociates at elevated Ca2+ concentrations By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Cytoplasm › cytoskeleton By similarity. Note: Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca2+. Associated with the microtubule network at the growing distal tip of microtubules By similarity. Ref.1

Tissue specificity

Expressed in all tissues examined and in many cell types, including bone marrow stroma, fibroblast, B-cell precursors, lymphoma and erythroleukemia. Ref.1

Domain

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends By similarity.

Post-translational modification

Glycosylation is required for cell surface expression By similarity.

Phosphorylated predominantly on Ser residues By similarity. Ref.5 Ref.6 Ref.7 Ref.8

Sequence similarities

Contains 1 EF-hand domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 685663Stromal interaction molecule 1
PRO_0000033327

Regions

Topological domain23 – 213191Extracellular Potential
Transmembrane214 – 23421Helical; Potential
Topological domain235 – 685451Cytoplasmic Potential
Domain63 – 9836EF-hand
Domain132 – 20069SAM
Calcium binding76 – 8712 Potential
Coiled coil248 – 388141 Potential
Motif642 – 6454Microtubule tip localization signal
Compositional bias270 – 33667Glu-rich
Compositional bias601 – 62929Pro/Ser-rich
Compositional bias672 – 68514Lys-rich

Amino acid modifications

Modified residue2571Phosphoserine Ref.6 Ref.8
Modified residue4201Phosphothreonine By similarity
Modified residue5191Phosphoserine Ref.7 Ref.8
Modified residue5241Phosphoserine Ref.7
Modified residue5751Phosphoserine By similarity
Modified residue6081Phosphoserine By similarity
Modified residue6601Phosphoserine By similarity
Modified residue6651Phosphothreonine Ref.5
Modified residue6681Phosphoserine Ref.5
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3311A → S in AAC52715. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70302 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F4DADF67436790FD

FASTA68577,567
        10         20         30         40         50         60 
MDVCARLALW LLWGLLLHQG QSLSHSHSEK NTGASSGATS EESTEAEFCR IDKPLCHSED 

        70         80         90        100        110        120 
EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL 

       130        140        150        160        170        180 
WKAWKSSEVY NWTVDEVIQW LITYVELPQY EETFRKLQLT GHAMPRLAVT NTTMTGTVLK 

       190        200        210        220        230        240 
MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH 

       250        260        270        280        290        300 
MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL 

       310        320        330        340        350        360 
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW LQLTHEVEVQ 

       370        380        390        400        410        420 
YYNIKKQNAE RQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT 

       430        440        450        460        470        480 
AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM 

       490        500        510        520        530        540 
DEEIVSPLSM QSPSLQSSVR QRLTEPQLGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM 

       550        560        570        580        590        600 
GRAADEALNA MPSNGSHRLI EGVHPGSLVE KLPDSPALAK KTFMALNHGL DKAHSLMELN 

       610        620        630        640        650        660 
PSVPPGGSPL LDSSHSLSPS SPDPDTPSPV GDNRALQGSR NTRIPHLAGK KAMAEEDNGS 

       670        680 
IGEETDSSPG RKKFPLKIFK KPLKK

« Hide

References

« Hide 'large scale' references
[1]"Identification of stromal cell products that interact with pre-B cells."
Oritani K., Kincade P.W.
J. Cell Biol. 134:771-782(1996) [PubMed: 8707854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6 X DBA/2.
Tissue: Bone marrow stroma.
[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-665 AND SER-668, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-524, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-519, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U47323 mRNA. Translation: AAC52715.1.
AK041944 mRNA. Translation: BAC31106.1.
CH466531 Genomic DNA. Translation: EDL16597.1.
BC021644 mRNA. Translation: AAH21644.1.
IPIIPI00108041.
RefSeqNP_033313.2. NM_009287.4.
UniGeneMm.645.

3D structure databases

ProteinModelPortalP70302.
SMRP70302. Positions 55-201.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48770N.
STRINGP70302.

PTM databases

PhosphoSiteP70302.

Proteomic databases

PRIDEP70302.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033289; ENSMUSP00000033289; ENSMUSG00000030987.
GeneID20866.
KEGGmmu:20866.

Organism-specific databases

CTD6786.
MGIMGI:107476. Stim1.

Phylogenomic databases

eggNOGroNOG13590.
GeneTreeENSGT00390000000214.
HOGENOMHBG714829.
HOVERGENHBG054652.
InParanoidP70302.
OrthoDBEOG4F4S9M.

Gene expression databases

ArrayExpressP70302.
BgeeP70302.
CleanExMM_STIM1.
GenevestigatorP70302.
GermOnlineENSMUSG00000030987. Mus musculus.

Family and domain databases

InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
Gene3DG3DSA:1.10.150.50. SAM_type. 1 hit.
PfamPF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SAM_homology. 1 hit.
PROSITEPS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. False negative.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio458901.
SOURCESearch...

Entry information

Entry nameSTIM1_MOUSE
AccessionPrimary (citable) accession number: P70302
Secondary accession number(s): Q8K1E1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents