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Q9JIZ9 (PLS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid scramblase 3

Short name=PL scramblase 3
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 3
Gene names
Name:Plscr3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Cofactor

Calcium By similarity.

Subunit structure

Interacts with PDCD6 in a calcium-dependent manner By similarity. Ref.4

Subcellular location

Mitochondrion membrane; Single-pass type II membrane protein By similarity Ref.4.

Domain

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

Sequence similarities

Belongs to the phospholipid scramblase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Phospholipid scramblase 3
PRO_0000100790

Regions

Topological domain1 – 266266Cytoplasmic By similarity
Transmembrane267 – 28317Helical; Potential
Topological domain284 – 29613Extracellular By similarity
Region1 – 5858Proline-rich domain (PRD) By similarity
Motif7 – 159SH3-binding 1 Potential
Motif15 – 184WW-binding Potential
Motif21 – 277SH3-binding 2 Potential
Motif66 – 716SH3-binding 3 Potential
Compositional bias12 – 2110Poly-Pro
Compositional bias159 – 1668Cys-rich

Amino acid modifications

Lipidation2121S-palmitoyl cysteine Probable
Lipidation2151S-palmitoyl cysteine Probable
Lipidation2171S-palmitoyl cysteine Probable

Sequences

Sequence LengthMass (Da)Tools
Q9JIZ9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B7F31C29758CFB07

FASTA29631,803
        10         20         30         40         50         60 
MAGYLPPKGY APSPPPPYPV PSGYPEPVAL HPGPGQAPVP TQVPAPAPGF ALFPSPGPVA 

        70         80         90        100        110        120 
PGPPAPFVPL PGVPPGLEFL VQIDQILIHQ KAERVETFLG WETCNMYELR SGTGQQLGQA 

       130        140        150        160        170        180 
AEESNCCARL CCGARRPFRI RLADPGDREV LRLLRPLHCG CSCCPCGLQE MEVQAPPGTT 

       190        200        210        220        230        240 
IGHVLQTWHP FLPKFSILDA DRQPVLRVVG PCWTCGCGTD TNFEVKTKDE SRSVGRISKQ 

       250        260        270        280        290 
WGGLLREALT DADDFGLQFP VDLDVKVKAV LLGATFLIDY MFFEKRGGAG PSAITS 

« Hide

References

« Hide 'large scale' references
[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(2000) [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. expand/collapse author list , 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(2005) [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(2004) [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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKCD.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS24916.1.
RefSeqNP_001161969.1. NM_001168497.1.
NP_076053.1. NM_023564.4.
XP_006534219.1. XM_006534156.1.
XP_006534220.1. XM_006534157.1.
UniGeneMm.28874.

3D structure databases

ProteinModelPortalQ9JIZ9.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9JIZ9.

Proteomic databases

PaxDbQ9JIZ9.
PRIDEQ9JIZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019605; ENSMUSP00000019605; ENSMUSG00000019461.
ENSMUST00000108632; ENSMUSP00000104272; ENSMUSG00000019461.
ENSMUST00000108633; ENSMUSP00000104273; ENSMUSG00000019461.
GeneID70310.
KEGGmmu:70310.
UCSCuc007jrz.2. mouse.

Organism-specific databases

CTD57048.
MGIMGI:1917560. Plscr3.

Phylogenomic databases

eggNOGNOG119855.
GeneTreeENSGT00390000002884.
HOGENOMHOG000237356.
HOVERGENHBG019157.
InParanoidQ9JIZ9.
OMAVTPGYPE.
OrthoDBEOG77T14X.
PhylomeDBQ9JIZ9.
TreeFamTF314939.

Gene expression databases

ArrayExpressQ9JIZ9.
BgeeQ9JIZ9.
CleanExMM_PLSCR3.
GenevestigatorQ9JIZ9.

Family and domain databases

InterProIPR005552. Scramblase.
[Graphical view]
PANTHERPTHR23248. PTHR23248. 1 hit.
PfamPF03803. Scramblase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331360.
PROQ9JIZ9.
SOURCESearch...

Entry information

Entry namePLS3_MOUSE
AccessionPrimary (citable) accession number: Q9JIZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot