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9.A.36.1.1
Erythrocyte Ca2+-dependent phospholipid scramblase 1, PLSCR1, of 318 aas and 1 or 2 C-terminal TMSs.  The C-terminal helix (CTH) inserts into the membrane via charge interactions but does not oligomerize in the membrane. The CTH is thus required for membrane insertion, Ca2+ coordination and the functional conformational changes that result in lipid scrambling (Francis et al. 2013).  The C-terminal region binds cholesterol (Posada et al. 2014). The role of this protein in phospholipid scrambling has been questioned (Sahu et al. 2007; Sivagnanam et al. 2017).

Accession Number:O15162
Protein Name:Scramblase 1
Length:318
Molecular Weight:35049.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Membrane1 / Single-pass type II membrane protein2
Substrate Ca2+

Cross database links:

Genevestigator: O15162
eggNOG: prNOG15180
HEGENOM: HBG452824
RefSeq: NP_066928.1   
Entrez Gene ID: 5359   
Pfam: PF03803   
OMIM: 604170  gene
KEGG: hsa:5359   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005509 F:calcium ion binding
GO:0017128 F:phospholipid scramblase activity
GO:0017124 F:SH3 domain binding
GO:0017121 P:phospholipid scrambling
GO:0030168 P:platelet activation
GO:0009615 P:response to virus

References (11)

[1] “Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids.”  Zhou Q.et.al.   9218461
[2] “Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene.”  Kasukabe T.et.al.   9712717
[3] “Identification of three new members of the phospholipid scramblase gene family.”  Wiedmer T.et.al.   10930526
[4] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid.”  Basse F.et.al.   8663431
[7] “Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta.”  Frasch S.C.et.al.   10770950
[8] “c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1.”  Sun J.et.al.   11390389
[9] “Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids.”  Zhao J.et.al.   9572851
[10] “Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids.”  Zhou Q.et.al.   9485382
[11] “Phospholipid scramblase 1 potentiates the antiviral activity of interferon.”  Dong B.et.al.   15308695
Structure:
1Y2A     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP AGHSGPGPAG 
61:	FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE YLSQIDQILI HQQIELLEVL 
121:	TGFETNNKYE IKNSFGQRVY FAAEDTDCCT RNCCGPSRPF TLRIIDNMGQ EVITLERPLR 
181:	CSSCCCPCCL QEIEIQAPPG VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC 
241:	GDVDFEIKSL DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI 
301:	DFMFFESTGS QEQKSGVW