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Protein

Stromal interaction molecule 1

Gene

STIM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 bindingi74 – 8512By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Stromal interaction molecule 1
Gene namesi
Name:STIM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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 – 211189ExtracellularSequence analysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence analysisAdd
BLAST
Topological domaini233 – 683451CytoplasmicSequence 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 – 683661Stromal interaction molecule 1PRO_0000253465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei502 – 5021PhosphothreonineBy similarity
Modified residuei510 – 5101PhosphoserineBy similarity
Modified residuei515 – 5151PhosphothreonineBy similarity
Modified residuei517 – 5171PhosphoserineBy similarity
Modified residuei519 – 5191PhosphoserineBy similarity
Modified residuei521 – 5211PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei573 – 5731PhosphoserineBy similarity
Modified residuei606 – 6061PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei626 – 6261PhosphoserineBy similarity
Modified residuei658 – 6581PhosphoserineBy similarity
Modified residuei663 – 6631PhosphothreonineBy similarity
Modified residuei666 – 6661PhosphoserineBy similarity

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

PaxDbiQ58CP9.
PeptideAtlasiQ58CP9.
PRIDEiQ58CP9.

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. Interacts with TMEM178A.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017425.

Structurei

3D structure databases

ProteinModelPortaliQ58CP9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 9636EF-handAdd
BLAST
Domaini130 – 19869SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni332 – 442111SOAR/CADBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili246 – 440195By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi640 – 6434Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi268 – 33467Glu-richAdd
BLAST
Compositional biasi598 – 62730Pro/Ser-richAdd
BLAST
Compositional biasi670 – 68314Lys-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.
HOGENOMiHOG000261647.
HOVERGENiHBG054652.
InParanoidiQ58CP9.
KOiK16059.

Family and domain databases

CDDicd11722. SOAR. 1 hit.
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.

Q58CP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVCARLALW LLWGLLLHHG QSLSQSHSEK ATGSGANSEE STAAEFCRID
60 70 80 90 100
KPLCHSEDEK LSFDAVRSIH KLMDDDANGD VDVEESDEFL REDLNYHDPT
110 120 130 140 150
VKHSTFHGED KLISVEDLWK AWKSSEVYNW TVDEVVQWLI TYVELPQYEE
160 170 180 190 200
TFRKLQLSGH AMPRLAVTNT TMTGTVLKMT DRSHRQKLQL KALDTVLFGP
210 220 230 240 250
PLLTRHNHLK DFMLVVSIVI GVGGCWFAYI QNRYSKEHMK KMMKDLEGLH
260 270 280 290 300
RAEQSLHDLQ ERLHKAQEEH RTVEVEKVHL EKKLRDEINL AKQEAQRLKE
310 320 330 340 350
LREGTENERS RQKYAEEELE QVREALRKAE KELESHSSWY APEALQKWLQ
360 370 380 390 400
LTHEVEVQYY NIKKQNAEKQ LLVAKEGAEK IKKKRNTLFG TFHVAHSSSL
410 420 430 440 450
DDVDHKILTA KQALSEVTAA LRERLHRWQQ IEILCGFQIV NNPGIHSLVA
460 470 480 490 500
ALNIDPSWMG STRPNPAHFI MTDDVDDMDE EIVSPLSMQS PSLQSSVRQR
510 520 530 540 550
LTEPQHGLGS QRDLTHSDSE SSLHMSDRQR LAPKPPQMIR AADEALSAMT
560 570 580 590 600
SNGSHRLIEG AHPGSLVEKL PDSPALAKKA LLALNHGLDK AHSLMELSSP
610 620 630 640 650
ALPSGSPHLD SSRSHSPSPP DPDTPSPAGD SRALQASRNT RIPHLAGKKA
660 670 680
AAEEDNGSIG EETDSSPGRK KFPLKIFKKP LKK
Length:683
Mass (Da):77,151
Last modified:April 26, 2005 - v1
Checksum:i53938E436B093C69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021898 mRNA. Translation: AAX46745.1.
RefSeqiNP_001030486.1. NM_001035409.1.
UniGeneiBt.31041.

Genome annotation databases

GeneIDi534816.
KEGGibta:534816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021898 mRNA. Translation: AAX46745.1.
RefSeqiNP_001030486.1. NM_001035409.1.
UniGeneiBt.31041.

3D structure databases

ProteinModelPortaliQ58CP9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017425.

Proteomic databases

PaxDbiQ58CP9.
PeptideAtlasiQ58CP9.
PRIDEiQ58CP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi534816.
KEGGibta:534816.

Organism-specific databases

CTDi6786.

Phylogenomic databases

eggNOGiKOG4403. Eukaryota.
ENOG410XRM6. LUCA.
HOGENOMiHOG000261647.
HOVERGENiHBG054652.
InParanoidiQ58CP9.
KOiK16059.

Family and domain databases

CDDicd11722. SOAR. 1 hit.
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...

Entry informationi

Entry nameiSTIM1_BOVIN
AccessioniPrimary (citable) accession number: Q58CP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 26, 2005
Last modified: September 7, 2016
This is version 89 of the entry and version 1 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. 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.