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P84903 (STIM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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. Ref.2 UniProtKB Q13586

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. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasm › cytoskeleton. Note: Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium. Associated with the microtubule network at the growing distal tip of microtubules By similarity. Ref.2 UniProtKB Q13586

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. UniProtKB Q13586

Phosphorylated predominantly on Ser residues By similarity.

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_0000248270

Regions

Topological domain23 – 213191Extracellular Potential
Transmembrane214 – 23421Helical; Potential
Topological domain235 – 685451Cytoplasmic Potential
Domain63 – 9836EF-hand
Domain132 – 19059SAM
Calcium binding76 – 8712 Potential
Coiled coil248 – 388141 Potential
Motif642 – 6454Microtubule tip localization signal

Amino acid modifications

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

Experimental info

Mutagenesis761D → A: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.2
Mutagenesis781D → A: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.2
Mutagenesis871E → Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P84903 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: FD2DA28427D2E41E

FASTA68577,449
        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 
WKAWKASEVY 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 QRLTEPQHGL GSQRDLTHSD SESSLHTSDR QRVAPKPPQM 

       550        560        570        580        590        600 
GRAADEALNA TSSNGSHRLI EGVHPGSLVE KLPDSPALAK KTILALNHGL DKAHSLMELN 

       610        620        630        640        650        660 
PSVPPGGSPL LDSSHSHSPS SPDPDTPSPV GDSRALQGSR NTRIPHLAGK KAMAEEDNGS 

       670        680 
IGEETDSSPG RKKFPLKIFK KPLKK

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane."
Zhang S.L., Yu Y., Roos J., Kozak J.A., Deerinck T.J., Ellisman M.H., Stauderman K.A., Cahalan M.D.
Nature 437:902-905(2005) [PubMed: 16208375] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-76; ASP-78 AND GLU-87.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03000423 Genomic DNA. No translation available.
AABR03002698 Genomic DNA. No translation available.
IPIIPI00365792.
RefSeqNP_001101966.2. NM_001108496.2.
UniGeneRn.106771.

3D structure databases

ProteinModelPortalP84903.
ModBaseSearch...

Protein-protein interaction databases

STRINGP84903.

PTM databases

PhosphoSiteP84903.

Proteomic databases

PRIDEP84903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027685; ENSRNOP00000027685; ENSRNOG00000020425.
GeneID361618.
KEGGrno:361618.
NMPDRfig|10116.3.peg.2474.

Organism-specific databases

CTD6786.
RGD1306831. Stim1.

Phylogenomic databases

eggNOGmaNOG09088.
GeneTreeENSGT00390000000214.
HOVERGENHBG054652.
InParanoidP84903.
OMAQMDDDAN.
OrthoDBEOG4F4S9M.
PhylomeDBP84903.

Gene expression databases

ArrayExpressP84903.
GenevestigatorP84903.

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

NextBio676948.

Entry information

Entry nameSTIM1_RAT
AccessionPrimary (citable) accession number: P84903
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: September 21, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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