Small integral membrane protein 14 (SMIM14)

Small integral membrane protein 14 (SMIM14) is a type I transmembrane protein encoded by the SMIM14 gene on chromosome 4p14[1][2]. The protein is typically 99 amino acids in length and contains a single transmembrane domain spanning residues 51–70, positioning its N-terminus outside the cell and its C-terminus in the cytosol[1]. SMIM14 is mainly localized to the endoplasmic reticulum, and its transmembrane domain is thought to facilitate ER retention, although it does not possess a classical ER retention signal[1]. The protein contains motifs that may be involved in protein sorting to endosomes and lysosomes, as well as potential posttranslational modification sites (palmitoylation, glycosaminoglycan addition, phosphorylation)[1]. It is highly expressed in liver, adrenal gland, colon, and prostate, but under-expressed in blood lymphocytes, skeletal muscle, and heart[1]. Present evidence does not indicate a well-established molecular function, drug interactions, or therapeutic targeting; its disease involvement is limited to genetic associations with certain hereditary disorders[2][4]. It has predicted protein-protein interactions, including with FATE1 (involved in ER-mitochondria calcium transfer for apoptosis regulation) and LSM4[1].

Other names

C4orf34FLJ13289small integral membrane protein 14SMIM14