Stromal interaction molecule
STIM1 (Homo sapiens) | ||
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Properties of human protein | ||
Mass / length primary structure | 663 amino acids | |
Secondary to quaternary structure | Membrane protein (ER, plasma membrane) | |
Identifier | ||
Gene name | STIM1 | |
External IDs | ||
Occurrence | ||
Parent taxon | multicellular animals |
STIM2 (Homo sapiens) | ||
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Properties of human protein | ||
Mass / length primary structure | 732 amino acids | |
Secondary to quaternary structure | Membrane protein (ER, plasma membrane) | |
Identifier | ||
Gene name | STIM2 | |
External IDs | ||
Occurrence | ||
Parent taxon | Vertebrates |
The term stromal interaction molecule (abbreviated to STIM ) describes a protein in cell physiology that, as a calcium sensor, plays a key role in maintaining calcium homeostasis or calcium signaling in animals . In vertebrates there are STIM1 and STIM2, which, as homodimers or heterodimers, form the sensory subunit of the CRAC channel . Mutations in STIM1 - gene are the cause of CRAC channel deficiency and consequent immune deficiency syndrome associated with T-cell inactivation (IDTICED2).
There are two subtypes of STIM: STIM1 and STIM2. Both are membrane proteins , each with a transmembrane domain , which are mainly located in the membrane of the endoplasmic reticulum , but to a lesser extent also in the plasma membrane .
Individual evidence
- ↑ a b Orthologist at eggNOG
- ↑ 1.A.52 The Ca2 + Release-activated Ca2 + (CRAC) Channel (CRAC-C) Family. In: TCDB. Saier Lab Bioinformatics, accessed September 26, 2010 .
- ↑ UniProt Q13586