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Protein

Phospholipid scramblase 1

Gene

PLSCR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation.

Cofactori

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • CD4 receptor binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • epidermal growth factor receptor binding Source: UniProtKB
  • phospholipid scramblase activity Source: UniProtKB
  • SH3 domain binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: UniProtKB

GO - Biological processi

  • acute-phase response Source: UniProtKB
  • apoptotic process Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • phosphatidylserine biosynthetic process Source: UniProtKB
  • phospholipid scrambling Source: UniProtKB
  • platelet activation Source: UniProtKB
  • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of innate immune response Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
  • regulation of mast cell activation Source: UniProtKB
  • response to interferon-beta Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

Calcium, DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-31063-MONOMER.
BRENDAi3.6.99.B1. 2681.
SignaLinkiO15162.
SIGNORiO15162.

Protein family/group databases

TCDBi9.A.36.1.1. the ca(2+)-dependent phospholipid scramblase (scramblase) family.

Chemistry databases

SwissLipidsiSLP:000000332.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid scramblase 1
Short name:
PL scramblase 1
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 1
Erythrocyte phospholipid scramblase
MmTRA1b
Gene namesi
Name:PLSCR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9092. PLSCR1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 288CytoplasmicAdd BLAST288
Transmembranei289 – 305HelicalSequence analysisAdd BLAST17
Topological domaini306 – 318ExtracellularAdd BLAST13

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • membrane raft Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69Y → F: Decrease in phosphorylation. 1
Mutagenesisi74Y → F: Decrease in phosphorylation. 1
Mutagenesisi161T → A: No induction by PKC. 1
Mutagenesisi184 – 189CCCPCC → AAAPAA: No palmitoylation; constitutively localizes in the nucleus. 2 Publications6
Mutagenesisi273D → A: Reduces the Ca(2+)-dependent phospholipid scrambling. 1
Mutagenesisi275D → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling. 1
Mutagenesisi277F → A: Reduces the Ca(2+)-dependent phospholipid scrambling. 1
Mutagenesisi279I → A: Reduces the Ca(2+)-dependent phospholipid scrambling. 1
Mutagenesisi281F → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling. 1
Mutagenesisi284D → A: Reduces the Ca(2+)-dependent phospholipid scrambling. 1

Organism-specific databases

DisGeNETi5359.
OpenTargetsiENSG00000188313.
PharmGKBiPA33419.

Polymorphism and mutation databases

BioMutaiPLSCR1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001007841 – 318Phospholipid scramblase 1Add BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei69Phosphotyrosine; by ABL1 Publication1
Modified residuei74Phosphotyrosine; by ABL1 Publication1
Modified residuei161Phosphothreonine; by PKC1 Publication1
Lipidationi184S-palmitoyl cysteineCurated1
Lipidationi185S-palmitoyl cysteineCurated1
Lipidationi186S-palmitoyl cysteineSequence analysis1
Lipidationi188S-palmitoyl cysteineCurated1
Lipidationi189S-palmitoyl cysteineCurated1

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO15162.
PaxDbiO15162.
PeptideAtlasiO15162.
PRIDEiO15162.

PTM databases

iPTMnetiO15162.
PhosphoSitePlusiO15162.
SwissPalmiO15162.

Expressioni

Tissue specificityi

Expressed in platelets, erythrocyte membranes, lymphocytes, spleen, thymus, prostate, testis, uterus, intestine, colon, heart, placenta, lung, liver, kidney and pancreas. Not detected in brain and skeletal muscle.

Inductioni

By phosphorylation by PKC. Induced by IFNB1/IFN-beta in response to a viral infection.1 Publication

Gene expression databases

BgeeiENSG00000188313.
CleanExiHS_PLSCR1.
ExpressionAtlasiO15162. baseline and differential.
GenevisibleiO15162. HS.

Interactioni

Subunit structurei

Interacts with ABL.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX28EBI-740019,EBI-710918From a different organism.
BCL6BA8KA133EBI-740019,EBI-10174813
CATSPER1Q8NEC53EBI-740019,EBI-744545
CHRDQ9H2X03EBI-740019,EBI-947551
CPSF6Q166302EBI-740019,EBI-358410
CTSZQ9UBR23EBI-740019,EBI-8636823
DAZAP2Q150384EBI-740019,EBI-724310
DEF6Q9H4E73EBI-740019,EBI-745369
DMRT3Q9NQL93EBI-740019,EBI-9679045
DOCK2Q926083EBI-740019,EBI-448771
ESR2Q927313EBI-740019,EBI-78505
EWSR1Q018444EBI-740019,EBI-739737
FRS3O435593EBI-740019,EBI-725515
GDPD5Q9HBR33EBI-740019,EBI-10310206
GLRX3O760034EBI-740019,EBI-374781
Hoxa1P090223EBI-740019,EBI-3957603From a different organism.
ILF3Q9NXX04EBI-740019,EBI-743980
KRTAP10-11P604123EBI-740019,EBI-10217483
KRTAP10-9P604113EBI-740019,EBI-10172052
KRTAP4-11Q9BYQ63EBI-740019,EBI-10302392
KRTAP4-2Q9BYR53EBI-740019,EBI-10172511
KRTAP5-6Q6L8G93EBI-740019,EBI-10250562
KRTAP9-2Q9BYQ43EBI-740019,EBI-1044640
LCE2DQ5TA823EBI-740019,EBI-10246750
LCE4AQ5TA783EBI-740019,EBI-10246358
LGALS9CQ6DKI23EBI-740019,EBI-9088829
NEU4Q8WWR82EBI-740019,EBI-746964
OCLNQ166252EBI-740019,EBI-2903088
P2RY6Q150773EBI-740019,EBI-10235794
PKD2Q135633EBI-740019,EBI-7813714
PRR13Q9NZ813EBI-740019,EBI-740924
RGS3P497963EBI-740019,EBI-2107809
SCNM1Q9BWG63EBI-740019,EBI-748391
SMARCC1Q929223EBI-740019,EBI-355653
SPATA8Q6RVD63EBI-740019,EBI-8635958
STK16O757163EBI-740019,EBI-749295
TFGQ927342EBI-740019,EBI-357061
TRIM42Q8IWZ53EBI-740019,EBI-5235829
VPS37CA5D8V63EBI-740019,EBI-2559305
ZNF417Q8TAU33EBI-740019,EBI-740727
ZNF587Q96SQ53EBI-740019,EBI-6427977

GO - Molecular functioni

  • CD4 receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • epidermal growth factor receptor binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111373. 133 interactors.
IntActiO15162. 136 interactors.
MINTiMINT-201602.
STRINGi9606.ENSP00000345494.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y2AX-ray2.20P257-266[»]
ProteinModelPortaliO15162.
SMRiO15162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15162.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 84Proline-rich domain (PRD)Add BLAST84

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi18 – 26SH3-binding 1Sequence analysis9
Motifi22 – 25WW-binding 1Sequence analysis4
Motifi33 – 36WW-binding 2Sequence analysis4
Motifi42 – 50SH3-binding 2Sequence analysis9
Motifi84 – 92SH3-binding 3Sequence analysis9
Motifi257 – 266Nuclear localization signal1 Publication10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi181 – 189Cys-rich9

Domaini

The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.

Sequence similaritiesi

Belongs to the phospholipid scramblase family.Curated

Keywords - Domaini

Repeat, SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0621. Eukaryota.
ENOG410XSYS. LUCA.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiO15162.
OMAiCVVGKIS.
OrthoDBiEOG091G0CUL.
PhylomeDBiO15162.
TreeFamiTF314939.

Family and domain databases

InterProiIPR005552. Scramblase.
[Graphical view]
PANTHERiPTHR23248. PTHR23248. 1 hit.
PfamiPF03803. Scramblase. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15162-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP
60 70 80 90 100
AGHSGPGPAG FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE
110 120 130 140 150
YLSQIDQILI HQQIELLEVL TGFETNNKYE IKNSFGQRVY FAAEDTDCCT
160 170 180 190 200
RNCCGPSRPF TLRIIDNMGQ EVITLERPLR CSSCCCPCCL QEIEIQAPPG
210 220 230 240 250
VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC GDVDFEIKSL
260 270 280 290 300
DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI
310
DFMFFESTGS QEQKSGVW
Length:318
Mass (Da):35,049
Last modified:January 1, 1998 - v1
Checksum:i9860744DEC40616E
GO
Isoform 2 (identifier: O15162-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MDKQNSQMNASHPETNLPVGYPP → MLLTRKQTCQLGILLSIHRQHSK
     24-104: Missing.

Note: No experimental confirmation available.
Show »
Length:237
Mass (Da):26,825
Checksum:i61B33BDD238A5519
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034388262H → Y.Corresponds to variant rs343320dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0552371 – 23MDKQN…VGYPP → MLLTRKQTCQLGILLSIHRQ HSK in isoform 2. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_05523824 – 104Missing in isoform 2. 1 PublicationAdd BLAST81

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098642 mRNA. Translation: AAC99413.1.
AB006746 mRNA. Translation: BAA32568.1.
AF224492 Genomic DNA. Translation: AAF80593.1.
AK300181 mRNA. Translation: BAG61960.1.
AC069528 Genomic DNA. No translation available.
AC116544 Genomic DNA. No translation available.
AK313377 mRNA. Translation: BAG36175.1.
CH471052 Genomic DNA. Translation: EAW78926.1.
BC021100 mRNA. Translation: AAH21100.1.
BC032718 mRNA. Translation: AAH32718.1.
CCDSiCCDS3135.1. [O15162-1]
PIRiJE0284.
RefSeqiNP_066928.1. NM_021105.2. [O15162-1]
XP_005247595.1. XM_005247538.3. [O15162-2]
XP_011511206.1. XM_011512904.1. [O15162-1]
XP_011511208.1. XM_011512906.2. [O15162-2]
XP_011511209.1. XM_011512907.2. [O15162-2]
XP_016862118.1. XM_017006629.1. [O15162-1]
UniGeneiHs.130759.

Genome annotation databases

EnsembliENST00000342435; ENSP00000345494; ENSG00000188313. [O15162-1]
ENST00000448787; ENSP00000411675; ENSG00000188313. [O15162-2]
GeneIDi5359.
KEGGihsa:5359.
UCSCiuc003evx.5. human. [O15162-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Scramblase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098642 mRNA. Translation: AAC99413.1.
AB006746 mRNA. Translation: BAA32568.1.
AF224492 Genomic DNA. Translation: AAF80593.1.
AK300181 mRNA. Translation: BAG61960.1.
AC069528 Genomic DNA. No translation available.
AC116544 Genomic DNA. No translation available.
AK313377 mRNA. Translation: BAG36175.1.
CH471052 Genomic DNA. Translation: EAW78926.1.
BC021100 mRNA. Translation: AAH21100.1.
BC032718 mRNA. Translation: AAH32718.1.
CCDSiCCDS3135.1. [O15162-1]
PIRiJE0284.
RefSeqiNP_066928.1. NM_021105.2. [O15162-1]
XP_005247595.1. XM_005247538.3. [O15162-2]
XP_011511206.1. XM_011512904.1. [O15162-1]
XP_011511208.1. XM_011512906.2. [O15162-2]
XP_011511209.1. XM_011512907.2. [O15162-2]
XP_016862118.1. XM_017006629.1. [O15162-1]
UniGeneiHs.130759.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y2AX-ray2.20P257-266[»]
ProteinModelPortaliO15162.
SMRiO15162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111373. 133 interactors.
IntActiO15162. 136 interactors.
MINTiMINT-201602.
STRINGi9606.ENSP00000345494.

Chemistry databases

SwissLipidsiSLP:000000332.

Protein family/group databases

TCDBi9.A.36.1.1. the ca(2+)-dependent phospholipid scramblase (scramblase) family.

PTM databases

iPTMnetiO15162.
PhosphoSitePlusiO15162.
SwissPalmiO15162.

Polymorphism and mutation databases

BioMutaiPLSCR1.

Proteomic databases

MaxQBiO15162.
PaxDbiO15162.
PeptideAtlasiO15162.
PRIDEiO15162.

Protocols and materials databases

DNASUi5359.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342435; ENSP00000345494; ENSG00000188313. [O15162-1]
ENST00000448787; ENSP00000411675; ENSG00000188313. [O15162-2]
GeneIDi5359.
KEGGihsa:5359.
UCSCiuc003evx.5. human. [O15162-1]

Organism-specific databases

CTDi5359.
DisGeNETi5359.
GeneCardsiPLSCR1.
HGNCiHGNC:9092. PLSCR1.
MIMi604170. gene.
neXtProtiNX_O15162.
OpenTargetsiENSG00000188313.
PharmGKBiPA33419.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0621. Eukaryota.
ENOG410XSYS. LUCA.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiO15162.
OMAiCVVGKIS.
OrthoDBiEOG091G0CUL.
PhylomeDBiO15162.
TreeFamiTF314939.

Enzyme and pathway databases

BioCyciZFISH:G66-31063-MONOMER.
BRENDAi3.6.99.B1. 2681.
SignaLinkiO15162.
SIGNORiO15162.

Miscellaneous databases

ChiTaRSiPLSCR1. human.
EvolutionaryTraceiO15162.
GeneWikiiPLSCR1.
GenomeRNAii5359.
PROiO15162.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000188313.
CleanExiHS_PLSCR1.
ExpressionAtlasiO15162. baseline and differential.
GenevisibleiO15162. HS.

Family and domain databases

InterProiIPR005552. Scramblase.
[Graphical view]
PANTHERiPTHR23248. PTHR23248. 1 hit.
PfamiPF03803. Scramblase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLS1_HUMAN
AccessioniPrimary (citable) accession number: O15162
Secondary accession number(s): B2R8H8, B4DTE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.