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Protein

Phospholipid scramblase 3

Gene

Plscr3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.1 Publication

Cofactori

Ca2+By similarity

GO - Molecular functioni

  1. calcium-dependent protein binding Source: MGI

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to lipopolysaccharide Source: UniProtKB
  3. cholesterol homeostasis Source: MGI
  4. glucose homeostasis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid scramblase 3
Short name:
PL scramblase 3
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 3
Gene namesi
Name:Plscr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1917560. Plscr3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 266266CytoplasmicBy similarityAdd
BLAST
Transmembranei267 – 28317HelicalSequence AnalysisAdd
BLAST
Topological domaini284 – 29613ExtracellularBy similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial membrane Source: UniProtKB-SubCell
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Phospholipid scramblase 3PRO_0000100790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi212 – 2121S-palmitoyl cysteineCurated
Lipidationi215 – 2151S-palmitoyl cysteineCurated
Lipidationi217 – 2171S-palmitoyl cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9JIZ9.
PaxDbiQ9JIZ9.
PRIDEiQ9JIZ9.

PTM databases

PhosphoSiteiQ9JIZ9.

Expressioni

Gene expression databases

BgeeiQ9JIZ9.
CleanExiMM_PLSCR3.
ExpressionAtlasiQ9JIZ9. baseline and differential.
GenevestigatoriQ9JIZ9.

Interactioni

Subunit structurei

Interacts with PDCD6 in a calcium-dependent manner.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9JIZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5858Proline-rich domain (PRD)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 159SH3-binding 1Sequence Analysis
Motifi15 – 184WW-bindingSequence Analysis
Motifi21 – 277SH3-binding 2Sequence Analysis
Motifi66 – 716SH3-binding 3Sequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 2110Poly-Pro
Compositional biasi159 – 1668Cys-rich

Domaini

The Proline-rich domain is required for phospholipid scramblase activity.By similarity

Sequence similaritiesi

Belongs to the phospholipid scramblase family.Curated

Keywords - Domaini

Repeat, SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG119855.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiQ9JIZ9.
OMAiLLGWETC.
OrthoDBiEOG77T14X.
PhylomeDBiQ9JIZ9.
TreeFamiTF314939.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9JIZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGYLPPKGY APSPPPPYPV PSGYPEPVAL HPGPGQAPVP TQVPAPAPGF
60 70 80 90 100
ALFPSPGPVA PGPPAPFVPL PGVPPGLEFL VQIDQILIHQ KAERVETFLG
110 120 130 140 150
WETCNMYELR SGTGQQLGQA AEESNCCARL CCGARRPFRI RLADPGDREV
160 170 180 190 200
LRLLRPLHCG CSCCPCGLQE MEVQAPPGTT IGHVLQTWHP FLPKFSILDA
210 220 230 240 250
DRQPVLRVVG PCWTCGCGTD TNFEVKTKDE SRSVGRISKQ WGGLLREALT
260 270 280 290
DADDFGLQFP VDLDVKVKAV LLGATFLIDY MFFEKRGGAG PSAITS
Length:296
Mass (Da):31,803
Last modified:September 30, 2000 - v1
Checksum:iB7F31C29758CFB07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159850 mRNA. Translation: AAF89526.1.
AK011716 mRNA. Translation: BAB27797.1.
AK029154 mRNA. Translation: BAC26329.1.
AK075841 mRNA. Translation: BAC35999.1.
BC020143 mRNA. Translation: AAH20143.1.
CCDSiCCDS24916.1.
RefSeqiNP_001161969.1. NM_001168497.1.
NP_076053.1. NM_023564.4.
XP_006534219.1. XM_006534156.1.
XP_006534220.1. XM_006534157.2.
UniGeneiMm.28874.

Genome annotation databases

EnsembliENSMUST00000019605; ENSMUSP00000019605; ENSMUSG00000019461.
ENSMUST00000108632; ENSMUSP00000104272; ENSMUSG00000019461.
ENSMUST00000108633; ENSMUSP00000104273; ENSMUSG00000019461.
GeneIDi70310.
KEGGimmu:70310.
UCSCiuc007jrz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159850 mRNA. Translation: AAF89526.1.
AK011716 mRNA. Translation: BAB27797.1.
AK029154 mRNA. Translation: BAC26329.1.
AK075841 mRNA. Translation: BAC35999.1.
BC020143 mRNA. Translation: AAH20143.1.
CCDSiCCDS24916.1.
RefSeqiNP_001161969.1. NM_001168497.1.
NP_076053.1. NM_023564.4.
XP_006534219.1. XM_006534156.1.
XP_006534220.1. XM_006534157.2.
UniGeneiMm.28874.

3D structure databases

ProteinModelPortaliQ9JIZ9.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9JIZ9.

Proteomic databases

MaxQBiQ9JIZ9.
PaxDbiQ9JIZ9.
PRIDEiQ9JIZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019605; ENSMUSP00000019605; ENSMUSG00000019461.
ENSMUST00000108632; ENSMUSP00000104272; ENSMUSG00000019461.
ENSMUST00000108633; ENSMUSP00000104273; ENSMUSG00000019461.
GeneIDi70310.
KEGGimmu:70310.
UCSCiuc007jrz.2. mouse.

Organism-specific databases

CTDi57048.
MGIiMGI:1917560. Plscr3.

Phylogenomic databases

eggNOGiNOG119855.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiQ9JIZ9.
OMAiLLGWETC.
OrthoDBiEOG77T14X.
PhylomeDBiQ9JIZ9.
TreeFamiTF314939.

Miscellaneous databases

NextBioi331360.
PROiQ9JIZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIZ9.
CleanExiMM_PLSCR3.
ExpressionAtlasiQ9JIZ9. baseline and differential.
GenevestigatoriQ9JIZ9.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification of three new members of the phospholipid scramblase gene family."
    Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.
    Biochim. Biophys. Acta 1467:244-253(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Skin and Stomach.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Association of protein kinase C delta and phospholipid scramblase 3 in hippocampal mitochondria correlates with neuronal vulnerability to brain ischemia."
    Kowalczyk J.E., Beresewicz M., Gajkowska B., Zablocka B.
    Neurochem. Int. 55:157-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKCD.
    Tissue: Brain.

Entry informationi

Entry nameiPLS3_MOUSE
AccessioniPrimary (citable) accession number: Q9JIZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2001
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.