CEMIP

CEMIP (Cell Migration Inducing Hyaluronan Binding Protein) is a protein coding gene. Diseases associated with CEMIP include Nonsyndromic Deafness. Among its related pathways are Glycosaminoglycan metabolism and Metabolism. Gene Ontology annotations related to this gene include hyaluronic acid binding and clathrin heavy chain binding. An important paralog of this gene is TMEM2.

Cell Migration Inducing Hyaluronan Binding Protein

Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing.

Hyaluronan biosynthetic process Source: Reactome
Hyaluronan catabolic process Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
Positive regulation of protein kinase C activity Source: UniProtKB
Positive regulation of protein targeting to membrane Source: UniProtKB
Positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
Sensory perception of sound Source: UniProtKB

Secreted; Nucleus; Cytoplasm; Cell membrane; Endoplasmic reticulum; Clathrin-coated pit. Retained in the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Colocalized with clathrin heavy chain/CLTC in clathrin-coated vesicles. Strongly detected in the cytoplasm of breast carcinoma cells, whereas poorly detected in adjacent normal epithelial cells, stromal cells, or benign breast tissues. Localized in the nucleus and cytoplasm of colon adenocarcinomas.

N-glycosylated; glycosylation is not necessary for HA-binding.