IED Industry Enzyme Database

Detail Information for IndEnz0002009037
IED ID IndEnz0002009037
Enzyme Type ID protease009037
Protein Name Stromal interaction molecule 1
Gene Name STIM1 GOK
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK
Enzyme Length 685
Uniprot Accession Number Q13586
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding CA_BIND 76..87
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 (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19249086, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:26322679, PubMed:25326555, PubMed:28219928). 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 (PubMed:16208375, PubMed:16537481). Involved in enamel formation (PubMed:24621671). Activated following interaction with STIMATE, leading to promote STIM1 conformational switch (PubMed:26322679). {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:28219928}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Beta strand (2); Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Glycosylation (2); Helix (17); Modified residue (18); Motif (1); Mutagenesis (16); Natural variant (14); Region (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2)
Keywords 3D-structure;Alternative splicing;Calcium;Calcium transport;Cell membrane;Coiled coil;Cytoplasm;Cytoskeleton;Disease variant;Endoplasmic reticulum;Glycoprotein;Ion transport;Membrane;Metal-binding;Microtubule;Phosphoprotein;Reference proteome;Sarcoplasmic reticulum;Signal;Transmembrane;Transmembrane helix;Transport
Interact With Q9BSW2; Q8N7U6; P22607; Q14957; Q5SUL5; P01112; P15260; Q9Y5U4; Q92993; Q8TAP4-4; Q96CV9; Q96D31; P30101; P62937-2; P23284; Q9UI14; Q96BY9; Q15047-2; P30825; Itself; Q9P246; P48995; Q9UMX0; P61981; Q9Y649; P62157
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:28219928}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:27185316}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19632184}. Sarcoplasmic reticulum {ECO:0000269|PubMed:25326555}. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane (PubMed:19249086, PubMed:16005298, PubMed:16208375, PubMed:18854159). Associated with the microtubule network at the growing distal tip of microtubules (PubMed:19632184). Colocalizes with ORAI1 at the cell membrane (PubMed:27185316). Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (PubMed:27185316). {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:27185316}.
Modified Residue MOD_RES 257; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:23186163"; MOD_RES 504; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P70302"; MOD_RES 512; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 517; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 521; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 523; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 524; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P70302"; MOD_RES 567; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 575; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 602; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 608; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 618; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 621; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 628; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 660; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 665; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 668; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
Post Translational Modification PTM: Glycosylation is required for cell surface expression. {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:11983428, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218}.; PTM: Phosphorylated predominantly on Ser residues. {ECO:0000269|PubMed:11004585}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (4); X-ray crystallography (2)
Cross Reference PDB 2K60; 2MAJ; 2MAK; 3TEQ; 4O9B; 6YEL;
Mapped Pubmed ID 11901194; 14582397; 16860747; 16870612; 16906149; 16921385; 16966422; 16987424; 17020874; 17045966; 17158173; 17218358; 17224452; 17283081; 17298947; 17299780; 17360414; 17452328; 17486119; 17517596; 17684017; 17702753; 17925382; 18166150; 18187424; 18190941; 18249114; 18250319; 18326500; 18337467; 18403424; 18420269; 18430726; 18448669; 18484746; 18506892; 18542992; 18569867; 18596693; 18635545; 18644792; 18768920; 18778263; 18802022; 18820677; 18832420; 18843204; 18845811; 18995841; 19019825; 19052075; 19088073; 19111578; 19171672; 19182790; 19185847; 19189966; 19260825; 19272522; 19287379; 19307462; 19327826; 19332491; 19403622; 19429662; 19433061; 19433064; 19447651; 19487696; 19506081; 19622747; 19626660; 19631699; 19706554; 19754898; 19765994; 19843011; 19881501; 19897728; 19906989; 20073506; 20194530; 20375143; 20436167; 20534587; 20562859; 20587595; 20629634; 20679432; 20736304; 20808796; 20876309; 20887894; 20926378; 20929812; 20976103; 21081754; 21126331; 21193399; 21217057; 21220431; 21239714; 21255618; 21321120; 21408196; 21427704; 21432868; 21499266; 21540881; 21640715; 21724845; 21788372; 21790973; 21876174; 21880734; 21906591; 21941299; 22031597; 22110130; 22210847; 22246182; 22260675; 22278058; 22298426; 22298778; 22381755; 22384096; 22438918; 22498042; 22549787; 22592407; 22748319; 22842488; 22914293; 22984609; 23022228; 23043102; 23049826; 23068106; 23108404; 23184982; 23203806; 23203809; 23212906; 23272049; 23320111; 23378028; 23395841; 23447534; 23512987; 23512989; 23515871; 23572507; 23578185; 23625915; 23668188; 23687376; 23690558; 23698468; 23700407; 23713409; 23714431; 23798062; 23800047; 23816623; 23871111; 23943619; 23994313; 24044355; 24095720; 24114840; 24308967; 24463606; 24464579; 24492416; 24556214; 24583265; 24603752; 24672054; 24681268; 24755083; 24806964; 24811382; 24842273; 24845346; 24954132; 24957221; 24996186; 25015419; 25016017; 25044882; 25057023; 25088676; 25190815; 25296861; 25342749; 25381814; 25404747; 25447552; 25504574; 25517631; 25531324; 25533457; 25562429; 25609649; 25645930; 25712868; 25736291; 25788524; 25805497; 25832866; 25840641; 25884983; 25915399; 25918394; 25935105; 26166565; 26184105; 26232624; 26257076; 26351694; 26399906; 26453325; 26454179; 26455959; 26469693; 26543234; 26546674; 26560041; 26576490; 26638075; 26643254; 26644574; 26670474; 26738614; 26775216; 26809794; 26826124; 26911279; 26919241; 27035326; 27068144; 27068962; 27069021; 27414851; 27431311; 27459950; 27506849; 27528628; 27601731; 27753099; 27793015; 27847114; 27863410; 27879676; 28058752; 28108672; 28145580; 28151650; 28185894; 28218251; 28220789; 28231751; 28326487; 28341841; 28385807; 28479254; 28534934; 28600435; 28624464; 28713917; 28724757; 28851859; 28866365; 28869106; 28912430; 29048678; 29093564; 29237734; 29242293; 29284605; 29298434; 29326165; 29414068; 29483506; 29563214; 29581306; 29661937; 29677491; 29705071; 29709426; 29748135; 29954946; 30088035; 30114708; 30131394; 30185837; 30241943; 30243034; 30317585; 30408546; 30414508; 30444880; 30475382; 30508734; 30530091; 30576443; 30589833; 30630032; 30643259; 30807904; 30831274; 30850711; 30902388; 30975919; 31018906; 31064875; 31366337; 31493399; 31564210; 31744929; 31818466; 31831524; 31838437; 31843504; 31844136; 32038646; 32056202; 32098964; 32118726; 32176842; 32330125; 32575830; 32589186; 32601188; 32641503; 32764353; 32795540; 32867798; 32879390; 32916960; 33073872; 33106661; 33124982; 33278394; 33361160; 33414420; 33430308; 33436389; 33468626; 33473127; 33649206; 33713955; 33733462; 33760103; 33802838; 33859736; 33907089; 34155535; 34498097; 34653219; 34705029; 34819389; 34939697;
Motif MOTIF 642..645; /note=Microtubule tip localization signal
Gene Encoded By
Mass 77,423
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda