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Ca+2-activated chloride channel regulator 2 (Ca+2-activated chloride channel family member 2, hCLCA2, hCaCC-3, [contains: Ca+2-activated chloride channel regulator 2, 109 kD form], CLCA2, CaCC3)
Function:
- role in modulating chloride current across the plasma membrane (Ca+2-dependent)
- cell adhesion involved in basal cell adhesion &/or stratification of squamous epithelia
- may act as a tumor suppressor in breast & colorectal cancer
Structure:
- 141 kD mature form is shed producing a 109 kD form & a 35 kD form
- N-glycosylated
- belongs to the CLCR family
- contains 1 VWFA domain
Compartment:
- cell surface, basal cell membrane, cell junction
- 109 kD form: secreted, remains membrane-associated until an unidentified event triggers release
Expression:
- expressed in cornea, skin, vagina, esophagus, & larynx (at protein level)
- expressed in trachea & mammary gland
- weakly expressed in testis & kidney
- highly expressed in corneal epithelium, colon & trachea
- moderately expressed in brain, urogenital organs, bladder, uterus & prostate
- expression greater in tissues containing stratified epithelium than in tissues containing epithelial monolayers: cornea, esophagus, larynx, skin & vagina
- highly expressed during epithelial stratification
- expressed in normal breast epithelium but not in breast cancer
- expressed in endothelial cells of lung
- expressed selectively in endothelia of small pulmonary arteries, arterioles, & subpleural & interlobular venules
Pathology:
- role for cell adhesion in the beginning stages of lung matastasis via the binding to ITGB4
- significantly down-regulated in breast cancer & colorectal cancer
General
glycoprotein
membrane protein
Properties
SIZE: entity length = 943 aa
MW = 104 kD
COMPARTMENT: plasma membrane
MOTIF: signal sequence {1-31}
N-glycosylation site {N74}
N-glycosylation site {N150}
N-glycosylation site {N231}
VWFA domain {311-483}
N-glycosylation site {N522}
N-glycosylation site {N822}
transmembrane domain {902-922}
Database Correlations
OMIM 604003
UniProt Q9UQC9
PFAM correlations
References
UniProt :accession Q9UQC9