| IED ID |
IndEnz0002009513 |
| Enzyme Type ID |
protease009513 |
| Protein Name |
Stromal interaction molecule 1
|
| Gene Name |
Stim1 Sim |
| Organism |
Mus musculus (Mouse) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Mus
Mus
Mus musculus (Mouse)
|
| Enzyme Sequence |
MDVCARLALWLLWGLLLHQGQSLSHSHSEKNTGASSGATSEESTEAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVIQWLITYVELPQYEETFRKLQLTGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAERQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQLGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMGRAADEALNAMPSNGSHRLIEGVHPGSLVEKLPDSPALAKKTFMALNHGLDKAHSLMELNPSVPPGGSPLLDSSHSLSPSSPDPDTPSPVGDNRALQGSRNTRIPHLAGKKAMAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK |
| Enzyme Length |
685 |
| Uniprot Accession Number |
P70302 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
CA_BIND 76..87; /evidence=ECO:0000250 |
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch. {ECO:0000250|UniProtKB:Q13586}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Glycosylation (2); Modified residue (18); Motif (1); Region (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords |
Calcium;Calcium transport;Cell membrane;Coiled coil;Cytoplasm;Cytoskeleton;Endoplasmic reticulum;Glycoprotein;Ion transport;Membrane;Metal-binding;Microtubule;Phosphoprotein;Reference proteome;Sarcoplasmic reticulum;Signal;Transmembrane;Transmembrane helix;Transport |
| Interact With |
Itself |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13586}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13586}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q13586}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13586}. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca(2+) 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. Colocalizes with ORAI1 at the cell membrane. Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:Q13586}. |
| Modified Residue |
MOD_RES 257; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17208939, ECO:0007744|PubMed:21183079"; MOD_RES 504; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 512; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 517; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 521; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 523; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 524; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 567; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 575; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 602; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 608; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 618; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 621; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 628; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q13586"; MOD_RES 660; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 665; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 668; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
| Post Translational Modification |
PTM: Glycosylation is required for cell surface expression. {ECO:0000250|UniProtKB:Q13586}.; PTM: Phosphorylated predominantly on Ser residues. {ECO:0000250|UniProtKB:Q13586}. |
| Signal Peptide |
SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
11463338;
11698278;
12466851;
12520002;
12904583;
14610273;
16615898;
17075073;
17224452;
17343823;
17647013;
17965774;
18059272;
18327260;
18452988;
18488020;
18559454;
18569867;
18772199;
18941110;
19013491;
19111578;
19172794;
19185847;
19265116;
19289460;
19332490;
19754898;
19765991;
19843959;
20028655;
20037597;
20048759;
20418871;
20427714;
20519511;
20739625;
20801505;
21061435;
21160048;
21267068;
21418512;
21441934;
21530328;
21663969;
21746875;
21810664;
21848641;
21941299;
22053056;
22084246;
22110130;
22210847;
22298426;
22298778;
22384096;
22411552;
22546859;
22609200;
22645307;
22785116;
22896585;
22904194;
23014880;
23034388;
23041196;
23076152;
23159931;
23206701;
23348743;
23424198;
23499491;
23625915;
23668188;
23840669;
23851458;
23922331;
23939929;
24077737;
24424349;
24493668;
24556214;
24558039;
24585777;
24650897;
24811382;
24965067;
24990931;
25157823;
25304289;
25471906;
25736291;
25737585;
25788524;
25837581;
25912155;
25938788;
26199344;
26236206;
26241845;
26261328;
26424448;
26454179;
26522985;
26673135;
26764049;
26916731;
26936863;
27150728;
27161229;
27261277;
27336410;
27399837;
27470514;
27601731;
27721237;
27913207;
28003364;
28132808;
28218251;
28258168;
28294127;
28341841;
28352661;
28385807;
28656279;
28707074;
28724541;
28732182;
28794231;
28821659;
29030115;
29054597;
29145451;
29158474;
29176619;
29227474;
29243589;
29305862;
29335300;
29360991;
29604963;
29611835;
29705071;
29709426;
29745808;
29912163;
30131394;
30154209;
30208327;
30224062;
30382093;
30390422;
30504131;
30520731;
30563862;
30575437;
30576443;
30607017;
30643259;
30773462;
30784343;
30862784;
30910863;
30967512;
30975919;
31064875;
31113852;
31308393;
31329049;
31541223;
31637311;
31664108;
31666234;
31722977;
31726860;
31785581;
31844136;
32014794;
32222458;
32295816;
32321939;
32609955;
32867798;
33127885;
33130308;
33737457;
34359900;
34654752;
34685684;
34715400;
8921403;
9680387;
|
| Motif |
MOTIF 642..645; /note=Microtubule tip localization signal |
| Gene Encoded By |
|
| Mass |
77,567 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|