Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01200
Entry Name
UniProt Accession
Theoretical PI
4.83
Molecular Weight
35049.07
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phospholipid scramblase 1
Protein Synonyms/Alias
PL scramblase 1; Ca(2+)-dependent phospholipid scramblase 1; Erythrocyte phospholipid scramblase; MmTRA1b;
Gene Name
PLSCR1
Gene Synonyms/Alias
Created Date
20-JUN-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
184
Canonical
RPLRCSSCCCPCCLQ
[1]
S-Palmitoylation
185
Canonical
PLRCSSCCCPCCLQE
[1]
S-Palmitoylation
186
Canonical
LRCSSCCCPCCLQEI
[1]
S-Palmitoylation
188
Canonical
CSSCCCPCCLQEIEI
[1]
S-Palmitoylation
189
Canonical
SSCCCPCCLQEIEIQ
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Wiedmer T, Zhao J, Nanjundan M, Sims PJ. Palmitoylation of phospholipidscramblase 1 controls its distribution between nucleus and plasma membrane.Biochemistry. 2003 Feb 11;42(5):1227-33.[PMID:12564925]
Functional Description
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.
Sequence Annotation
Topological domain: 1 288 Cytoplasmic.
Transmembrane: 289 305 Helical.
Topological domain: 306 318 Extracellular.
Region: 1 84 Proline-rich domain (PRD).
Motif: 18 26 SH3-binding 1.
Motif: 22 25 WW-binding 1.
Motif: 33 36 WW-binding 2.
Motif: 42 50 SH3-binding 2.
Motif: 84 92 SH3-binding 3.
Motif: 257 266 Nuclear localization signal.
Modified residue: 69 69 Phosphotyrosine; by ABL.
Modified residue: 74 74 Phosphotyrosine; by ABL.
Modified residue: 161 161 Phosphothreonine; by PKC.
Protein Length
318 AA.
Protein Sequence
(Canonical)
MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP AGHSGPGPAG  60
FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE YLSQIDQILI HQQIELLEVL  120
TGFETNNKYE IKNSFGQRVY FAAEDTDCCT RNCCGPSRPF TLRIIDNMGQ EVITLERPLR  180
CSSCCCPCCL QEIEIQAPPG VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC  240
GDVDFEIKSL DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI  300
DFMFFESTGS QEQKSGVW                                                318
FASTA
(Canonical)
>LipidDB-9606-01200|O15162
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
Gene Ontology
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0031012; C:extracellular matrix; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045121; C:membrane raft; IDA:UniProtKB
GO:0005730; C:nucleolus; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005509; F:calcium ion binding; IDA:UniProtKB
GO:0042609; F:CD4 receptor binding; IPI:UniProtKB
GO:0003677; F:DNA binding; IEA:UniProtKB-KW
GO:0019899; F:enzyme binding; IPI:UniProtKB
GO:0005154; F:epidermal growth factor receptor binding; IPI:UniProtKB
GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB
GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:UniProtKB
GO:0017124; F:SH3 domain binding; IDA:UniProtKB
GO:0006953; P:acute-phase response; ISS:UniProtKB
GO:0006915; P:apoptotic process; IDA:UniProtKB
GO:0051607; P:defense response to virus; IMP:UniProtKB
GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB
GO:0006659; P:phosphatidylserine biosynthetic process; ISS:UniProtKB
GO:0017121; P:phospholipid scrambling; IDA:UniProtKB
GO:0030168; P:platelet activation; NAS:UniProtKB
GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IDA:UniProtKB
GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB
GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB
GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; ISS:UniProtKB
GO:0033003; P:regulation of mast cell activation; ISS:UniProtKB
GO:0035456; P:response to interferon-beta; IMP:UniProtKB
Interpro
InterPro; IPR005552; Scramblase
Pfam
Pfam; PF03803; Scramblase;
SMART
PROSITE
PRINTS