BioPAX pathway converted from "ARV1 transports CHOL from ER membrane to plasma membrane" in the Reactome database.ARV1 transports CHOL from ER membrane to plasma membraneARV1 transports CHOL from ER membrane to plasma membraneThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1933841endoplasmic reticulum membraneGO0005789cholesterol [ChEBI:16113]cholesterolcholest-5-en-3beta-olReactomehttp://www.reactome.orgChEBI16113Reactome DB_ID: 1710951plasma membraneGO0005886PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10154112UniProt:F1RGS6ARV1Sus scrofaNCBI Taxonomy9823UniProtF1RGS6Chain Coordinates1EQUAL271EQUALGO0015248GO molecular functionReactome Database ID Release 7510154113Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10154113Reactome Database ID Release 7510154115Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10154115ReactomeR-SSC-52505311Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5250531.1Sterols such as cholesterol (CHOL) synthesised in the endoplasmic reticulum (ER) need to be efficiently transported to the plasma membrane, where 90% of the free sterol pool resides. Conversely, sterols taken up from outside the cell need to be transported back to the ER for esterification to sterol esters. The mechanisms that control this bi-directional movement of sterols are still poorly understood but a likely candidate is protein ARV1 (ARV1). Studies with mutant yeast Arv1 indicate altered intracellular sterol distribution and subsequent defects in sphingolipid metabolism. Human ARV1, a predicted sequence ortholog of yeast Arv1, complements the defects seen associated with deletion of yeast Arv1 (Tinkelenberg et al. 2000, Swain et al. 2002).11063737Pubmed2000Mutations in yeast ARV1 alter intracellular sterol distribution and are complemented by human ARV1Tinkelenberg, A HLiu, YAlcantara, FKhan, SGuo, ZBard, MSturley, S LJ. Biol. Chem. 275:40667-7012145310Pubmed2002Yeast cells lacking the ARV1 gene harbor defects in sphingolipid metabolism. Complementation by human ARV1Swain, EvelynStukey, JosephMcDonough, VirginiaGermann, MelodyLiu, YingSturley, Stephen LNickels, Joseph TJ. Biol. Chem. 277:36152-60inferred by electronic annotationIEAGOIEA