8.A.27.1.5 CDC50A or TMEM30A of 361 aas and 2 TMSs. Required for targetting of the ATP11C ATPase (3.A.3.8.14) and probably several other phospholipid flipping ATPases to the plasma membrane, and possibly also for their activities (Segawa et al. 2014). Forms a heterodimer with ATP8B1 (van der Mark et al. 2014). Signaling networks are regulated by TMEM30A during cell migration, reflecting the regulatory mechanisms underlying tumor migration (Wang et al. 2017). TMEM30A deficiency leads to intrahepatic cholestasis in mice by impairing the expression and localization of bile salt transporters and the expression of related nuclear receptors (Liu et al. 2017). The 3-D strcutures of 6 distinct intermediates (2.6 - 3.3 Å resolution) of the complex of this protein with ATP8A1 (TC# 3.A.3.8.13) have been solved, revealing the transport cycle for lipid flipping (Hiraizumi et al. 2019). TMEM30A maintains the asymmetric distribution of phosphatidylserine, an 'eat-me' signal recognized by macrophages. TMEM30A loss-of-function mutations drive lymphomagenesis and confer therapeutically exploitable vulnerability in B-cell lymphoma (Ennishi et al. 2020).
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Accession Number: | Q9NV96 |
Protein Name: | Cell cycle control protein 50A |
Length: | 361 |
Molecular Weight: | 40684.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 2 |
Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
Substrate |
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1: MAMNYNAKDE VDGGPPCAPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV LPIFFIIGLI
61: FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT PCFCTINFTL EKSFEGNVFM
121: YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN
181: DTLELFLIGN DSYPIPIALK KKGIAWWTDK NVKFRNPPGG DNLEERFKGT TKPVNWLKPV
241: YMLDSDPDNN GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP
301: VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY RNSSNTADIT
361: I