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Protein

Stromal interaction molecule 1

Gene

Stim1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in mediating store-operated Ca2+ entry (SOCE), a 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 ORAI1. Involved in enamel formation. Activated following interaction with TMEM110/STIMATE, leading to promote STIM1 conformational switch.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi76 – 8712By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • activation of store-operated calcium channel activity Source: UniProtKB
  • cation transport Source: MGI
  • detection of calcium ion Source: UniProtKB
  • enamel mineralization Source: UniProtKB
  • myotube differentiation Source: MGI
  • regulation of calcium ion transport Source: UniProtKB
  • store-operated calcium entry Source: MGI
Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-5578775. Ion homeostasis.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromal interaction molecule 1
Gene namesi
Name:Stim1
Synonyms:Sim
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:107476. Stim1.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
  • Sarcoplasmic reticulum By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca2+ and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. Associated with the microtubule network at the growing distal tip of microtubules (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 213191ExtracellularSequence analysisAdd
BLAST
Transmembranei214 – 23421HelicalSequence analysisAdd
BLAST
Topological domaini235 – 685451CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Membrane, Microtubule, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 685663Stromal interaction molecule 1PRO_0000033327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis
Modified residuei257 – 2571PhosphoserineCombined sources
Modified residuei504 – 5041PhosphothreonineCombined sources
Modified residuei512 – 5121PhosphoserineCombined sources
Modified residuei517 – 5171PhosphothreonineBy similarity
Modified residuei519 – 5191PhosphoserineCombined sources
Modified residuei521 – 5211PhosphoserineCombined sources
Modified residuei523 – 5231PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei567 – 5671PhosphoserineCombined sources
Modified residuei575 – 5751PhosphoserineCombined sources
Modified residuei602 – 6021PhosphoserineBy similarity
Modified residuei608 – 6081PhosphoserineBy similarity
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei665 – 6651PhosphothreonineCombined sources
Modified residuei668 – 6681PhosphoserineCombined sources

Post-translational modificationi

Glycosylation is required for cell surface expression.By similarity
Phosphorylated predominantly on Ser residues.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP70302.
MaxQBiP70302.
PaxDbiP70302.
PRIDEiP70302.

PTM databases

iPTMnetiP70302.
PhosphoSiteiP70302.

Expressioni

Tissue specificityi

Expressed in maturation-stage ameloblasts (at protein level). Expressed in all tissues examined and in many cell types, including bone marrow stroma, fibroblast, B-cell precursors, lymphoma and erythroleukemia.2 Publications

Gene expression databases

BgeeiP70302.
CleanExiMM_STIM1.
GenevisibleiP70302. MM.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with STIM2. Interacts (via the transmembrane region and the SOAR/CAD domain) with SPPL3; the interaction promotes the binding of STIM1 to ORAI1. Interacts with ORAI1. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with CRACR2A/EFCAB4B; the interaction is direct and takes place in absence of Ca2+. Forms a complex with CRACR2A/EFCAB4B and ORAI1 at low concentration of Ca2+, the complex dissociates at elevated Ca2+ concentrations. Interacts with SARAF, promoting a slow inactivation of STIM1-dependent SOCE activity, possibly by facilitating the deoligomerization of STIM1. Interacts with ASPH. Interacts with SLC35G1; intracellular Ca2+-dependent. May interact with ATP1A1, ATP2A2, ATP2B1, ATP2B4, KPNB1 and XPO1; through SLC35G1. Interacts with TMEM203. Interacts with TMEM110/STIMATE, promoting STIM1 conformational switch (By similarity). Interacts with TMEM178A (PubMed:26644563).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-48770N.
IntActiP70302. 1 interaction.
MINTiMINT-4135875.
STRINGi10090.ENSMUSP00000033289.

Structurei

3D structure databases

ProteinModelPortaliP70302.
SMRiP70302. Positions 55-201, 247-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 9836EF-handAdd
BLAST
Domaini132 – 20069SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 444111SOAR/CADBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili248 – 442195By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi642 – 6454Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi270 – 33667Glu-richAdd
BLAST
Compositional biasi601 – 62929Pro/Ser-richAdd
BLAST
Compositional biasi672 – 68514Lys-richAdd
BLAST

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity
The STIM1 Orai1-activating region/CRAC-activating domain (SOAR/CAD) mediates interaction with ORAI1 to activate the channel.By similarity

Sequence similaritiesi

Contains 1 EF-hand domain.Curated
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4403. Eukaryota.
ENOG410XRM6. LUCA.
GeneTreeiENSGT00390000000214.
HOGENOMiHOG000261647.
HOVERGENiHBG054652.
InParanoidiP70302.
KOiK16059.
OMAiNGGNRVH.
OrthoDBiEOG7XSTDR.
TreeFamiTF313487.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
IPR032393. SOAR.
IPR030463. STM1.
[Graphical view]
PANTHERiPTHR15136:SF9. PTHR15136:SF9. 1 hit.
PfamiPF07647. SAM_2. 1 hit.
PF16533. SOAR. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVCARLALW LLWGLLLHQG QSLSHSHSEK NTGASSGATS EESTEAEFCR
60 70 80 90 100
IDKPLCHSED EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD
110 120 130 140 150
PTVKHSTFHG EDKLISVEDL WKAWKSSEVY NWTVDEVIQW LITYVELPQY
160 170 180 190 200
EETFRKLQLT GHAMPRLAVT NTTMTGTVLK MTDRSHRQKL QLKALDTVLF
210 220 230 240 250
GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH MKKMMKDLEG
260 270 280 290 300
LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL
310 320 330 340 350
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW
360 370 380 390 400
LQLTHEVEVQ YYNIKKQNAE RQLLVAKEGA EKIKKKRNTL FGTFHVAHSS
410 420 430 440 450
SLDDVDHKIL TAKQALSEVT AALRERLHRW QQIEILCGFQ IVNNPGIHSL
460 470 480 490 500
VAALNIDPSW MGSTRPNPAH FIMTDDVDDM DEEIVSPLSM QSPSLQSSVR
510 520 530 540 550
QRLTEPQLGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM GRAADEALNA
560 570 580 590 600
MPSNGSHRLI EGVHPGSLVE KLPDSPALAK KTFMALNHGL DKAHSLMELN
610 620 630 640 650
PSVPPGGSPL LDSSHSLSPS SPDPDTPSPV GDNRALQGSR NTRIPHLAGK
660 670 680
KAMAEEDNGS IGEETDSSPG RKKFPLKIFK KPLKK
Length:685
Mass (Da):77,567
Last modified:July 27, 2011 - v2
Checksum:iF4DADF67436790FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3311A → S in AAC52715 (PubMed:8707854).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47323 mRNA. Translation: AAC52715.1.
AK041944 mRNA. Translation: BAC31106.1.
CH466531 Genomic DNA. Translation: EDL16597.1.
BC021644 mRNA. Translation: AAH21644.1.
CCDSiCCDS21530.1.
RefSeqiNP_033313.2. NM_009287.4.
UniGeneiMm.645.

Genome annotation databases

EnsembliENSMUST00000033289; ENSMUSP00000033289; ENSMUSG00000030987.
GeneIDi20866.
KEGGimmu:20866.
UCSCiuc009irm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47323 mRNA. Translation: AAC52715.1.
AK041944 mRNA. Translation: BAC31106.1.
CH466531 Genomic DNA. Translation: EDL16597.1.
BC021644 mRNA. Translation: AAH21644.1.
CCDSiCCDS21530.1.
RefSeqiNP_033313.2. NM_009287.4.
UniGeneiMm.645.

3D structure databases

ProteinModelPortaliP70302.
SMRiP70302. Positions 55-201, 247-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48770N.
IntActiP70302. 1 interaction.
MINTiMINT-4135875.
STRINGi10090.ENSMUSP00000033289.

PTM databases

iPTMnetiP70302.
PhosphoSiteiP70302.

Proteomic databases

EPDiP70302.
MaxQBiP70302.
PaxDbiP70302.
PRIDEiP70302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033289; ENSMUSP00000033289; ENSMUSG00000030987.
GeneIDi20866.
KEGGimmu:20866.
UCSCiuc009irm.1. mouse.

Organism-specific databases

CTDi6786.
MGIiMGI:107476. Stim1.

Phylogenomic databases

eggNOGiKOG4403. Eukaryota.
ENOG410XRM6. LUCA.
GeneTreeiENSGT00390000000214.
HOGENOMiHOG000261647.
HOVERGENiHBG054652.
InParanoidiP70302.
KOiK16059.
OMAiNGGNRVH.
OrthoDBiEOG7XSTDR.
TreeFamiTF313487.

Enzyme and pathway databases

ReactomeiR-MMU-5578775. Ion homeostasis.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

ChiTaRSiStim1. mouse.
NextBioi299689.
PROiP70302.
SOURCEiSearch...

Gene expression databases

BgeeiP70302.
CleanExiMM_STIM1.
GenevisibleiP70302. MM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
IPR032393. SOAR.
IPR030463. STM1.
[Graphical view]
PANTHERiPTHR15136:SF9. PTHR15136:SF9. 1 hit.
PfamiPF07647. SAM_2. 1 hit.
PF16533. SOAR. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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: 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504; SER-512 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-504; SER-512; SER-519; SER-521; SER-524; SER-567; SER-575; SER-660; THR-665 AND SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. Cited for: TISSUE SPECIFICITY.
  8. "Tmem178 acts in a novel negative feedback loop targeting NFATc1 to regulate bone mass."
    Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C., Mellins E.D., Novack D.V., Faccio R.
    Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM178A.

Entry informationi

Entry nameiSTIM1_MOUSE
AccessioniPrimary (citable) accession number: P70302
Secondary accession number(s): Q8K1E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: April 13, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.