Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00776
Entry Name
UniProt Accession
Theoretical PI
6.22
Molecular Weight
31648.42
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phospholipid scramblase 3
Protein Synonyms/Alias
PL scramblase 3; Ca(2+)-dependent phospholipid scramblase 3;
Gene Name
PLSCR3
Gene Synonyms/Alias
Created Date
20-JUN-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
126
Canonical
AAEESNCCARLCCGA
[1]
S-Palmitoylation
130
Canonical
SNCCARLCCGARRPL
[1]
S-Palmitoylation
162
Canonical
PLHCGCSCCPCGLQE
[1]
S-Palmitoylation
163
Canonical
LHCGCSCCPCGLQEM
[1]
S-Palmitoylation
165
Canonical
CGCSCCPCGLQEMEV
[1]
S-Palmitoylation
211
Canonical
VLRVVGPCWTCGCGT
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
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. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages.
Sequence Annotation
Topological domain: 1 265 Cytoplasmic.
Transmembrane: 266 282 Helical.
Topological domain: 283 295 Extracellular.
Region: 1 57 Proline-rich domain (PRD).
Motif: 7 15 SH3-binding 1.
Motif: 15 18 WW-binding.
Motif: 21 27 SH3-binding 2.
Motif: 65 70 SH3-binding 3.
Modified residue: 21 21 Phosphothreonine; by PKC/PRKCD.
Protein Length
295 AA.
Protein Sequence
(Canonical)
MAGYLPPKGY APSPPPPYPV TPGYPEPALH PGPGQAPVPA QVPAPAPGFA LFPSPGPVAL  60
GSAAPFLPLP GVPSGLEFLV QIDQILIHQK AERVETFLGW ETCNRYELRS GAGQPLGQAA  120
EESNCCARLC CGARRPLRVR LADPGDREVL RLLRPLHCGC SCCPCGLQEM EVQAPPGTTI  180
GHVLQTWHPF LPKFSIQDAD RQTVLRVVGP CWTCGCGTDT NFEVKTRDES RSVGRISKQW  240
GGLVREALTD ADDFGLQFPL DLDVRVKAVL LGATFLIDYM FFEKRGGAGP SAVTS       295
FASTA
(Canonical)
>LipidDB-9606-00776|Q9NRY6
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005739; C:mitochondrion; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005509; F:calcium ion binding; NAS:UniProtKB
GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB
GO:0017128; F:phospholipid scramblase activity; NAS:UniProtKB
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW
GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl
GO:0042632; P:cholesterol homeostasis; IEA:Ensembl
GO:0042593; P:glucose homeostasis; IEA:Ensembl
GO:0017121; P:phospholipid scrambling; NAS:UniProtKB
Interpro
InterPro; IPR005552; Scramblase
Pfam
Pfam; PF03803; Scramblase;
SMART
PROSITE
PRINTS