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Q9JJ00 (PLS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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 1

Short name=PL scramblase 1
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 1
Transplantability-associated protein 1
Short name=NOR1
Short name=TRA1
Gene names
Name:Plscr1
Synonyms:Tra1b, Tras1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Ref.4

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. Ref.4

Cofactor

Calcium By similarity.

Subcellular location

Membrane By similarity; Single-pass type II membrane protein. Membrane; Lipid-anchor By similarity; Cytoplasmic side. Nucleus By similarity.

Tissue specificity

Highly expressed in kidney, lung, liver and bone marrow, slightly in spleen, heart and macrophage.

Induction

Up-regulated by SCF/KITL and GCSF/CSF3. Ref.4

Domain

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

Involvement in disease

Participates in a chromosomal translocation that produces MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude mice.

Miscellaneous

Knockout newborn mice display a reduced granulocyte production. Hematopoietic precursor cell from knockout mice display defective colony formation and impaired differentiation to mature granulocytes as stimulated by SCF/KITL and GCSF/CSF3.

Sequence similarities

Belongs to the phospholipid scramblase family.

Sequence caution

The sequence BAA23663.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA23664.1 differs from that shown. Reason: Frameshift at position 92.

Ontologies

Keywords
   Biological processAntiviral defense
   Cellular componentMembrane
Nucleus
   Coding sequence diversityChromosomal rearrangement
   DomainRepeat
SH3-binding
Transmembrane
Transmembrane helix
   LigandCalcium
DNA-binding
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from expression pattern PubMed 17590392. Source: UniProtKB

cellular response to cytokine stimulus

Inferred from expression pattern PubMed 17590392. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 17590392. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype PubMed 15308695. Source: UniProtKB

intrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 15863367. Source: UniProtKB

myeloid cell differentiation

Inferred from mutant phenotype PubMed 15328404. Source: MGI

negative regulation of protein binding

Inferred from direct assay PubMed 16611984. Source: MGI

negative regulation of viral genome replication

Inferred from mutant phenotype PubMed 15308695. Source: UniProtKB

phosphatidylserine biosynthetic process

Inferred from direct assay PubMed 12509439. Source: UniProtKB

phosphatidylserine exposure on apoptotic cell surface

Inferred from direct assay PubMed 12509439. Source: MGI

phospholipid scrambling

Inferred from direct assay PubMed 12509439. Source: UniProtKB

positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 16611984. Source: MGI

positive regulation of innate immune response

Inferred from mutant phenotype PubMed 15308695. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 12509439. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mast cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-alpha

Inferred from mutant phenotype PubMed 15308695. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 17590392. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17590392. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12509439. Source: UniProtKB

   Molecular_functionCD4 receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from sequence or structural similarity. Source: UniProtKB

SH3 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipid scramblase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Phospholipid scramblase 1
PRO_0000100785

Regions

Topological domain1 – 297297Cytoplasmic By similarity
Transmembrane298 – 31417Helical; Potential
Topological domain315 – 32814Extracellular By similarity
Region1 – 9393Proline-rich domain (PRD) By similarity
Motif18 – 269SH3-binding 1 Potential
Motif22 – 254WW-binding Potential
Motif56 – 649SH3-binding 2 Potential
Motif93 – 1019SH3-binding 3 Potential
Motif269 – 2757Nuclear localization signal By similarity
Compositional bias96 – 1016Poly-Pro
Compositional bias190 – 1989Cys-rich

Sites

Site127 – 1282Breakpoint for translocation to form MMTRA1A

Amino acid modifications

Modified residue831Phosphotyrosine; by ABL By similarity
Modified residue1701Phosphothreonine; by PKC By similarity
Lipidation1931S-palmitoyl cysteine By similarity
Lipidation1941S-palmitoyl cysteine By similarity
Lipidation1971S-palmitoyl cysteine By similarity
Lipidation1981S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict24 – 274PYPP → GLCV Ref.3
Sequence conflict1301T → A in BAB22897. Ref.2
Sequence conflict2671K → R in BAB22897. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JJ00 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6CA35DF8DBF72ACF

FASTA32835,914
        10         20         30         40         50         60 
MENHSKQTEA PHPGTYMPAG YPPPYPPAAF QGPSDHAAYP IPQAGYQGPP GPYPGPQPGY 

        70         80         90        100        110        120 
PVPPGGYAGG GPSGFPVQNQ PAYNHPGGPG GTPWMPAPPP PLNCPPGLEY LAQIDQLLVH 

       130        140        150        160        170        180 
QQIELLEVLT GFETNNKYEI KNSLGQRVYF AVEDTDCCTR NCCGASRPFT LRILDNLGRE 

       190        200        210        220        230        240 
VMTLERPLRC SSCCFPCCLQ EIEIQAPPGV PVGYVTQTWH PCLPKFTLQN EKKQDVLKVV 

       250        260        270        280        290        300 
GPCVVCSCCS DIDFELKSLD EESVVGKISK QWSGFVREAF TDADNFGIQF PLDLDVKMKA 

       310        320 
VMLGACFLID FMFFERTGNE EQRSGAWQ 

« 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.
[3]"TRA1, a novel mRNA highly expressed in leukemogenic mouse monocytic sublines but not in nonleukemogenic sublines."
Kasukabe T., Okabe-Kado J., Honma Y.
Blood 89:2975-2985(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-328, CHROMOSOMAL TRANSLOCATION.
Strain: BALB/c.
Tissue: Kidney.
[4]"Normal hemostasis but defective hematopoietic response to growth factors in mice deficient in phospholipid scramblase 1."
Zhou Q., Zhao J., Wiedmer T., Sims P.J.
Blood 99:4030-4038(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF159593 mRNA. Translation: AAF77076.1.
AK003628 mRNA. Translation: BAB22897.1.
D78354 mRNA. Translation: BAA23663.1. Different initiation.
D78355 mRNA. Translation: BAA23664.1. Frameshift.
CCDSCCDS52886.1.
RefSeqNP_035766.2. NM_011636.2.
XP_006511115.1. XM_006511052.1.
UniGeneMm.421956.
Mm.441702.

3D structure databases

ProteinModelPortalQ9JJ00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JJ00. 1 interaction.
STRING10090.ENSMUSP00000108671.

PTM databases

PhosphoSiteQ9JJ00.

Proteomic databases

MaxQBQ9JJ00.
PaxDbQ9JJ00.
PRIDEQ9JJ00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000093801; ENSMUSP00000091318; ENSMUSG00000032369.
GeneID22038.
KEGGmmu:22038.
UCSCuc009ram.2. mouse.

Organism-specific databases

CTD5359.
MGIMGI:893575. Plscr1.

Phylogenomic databases

eggNOGNOG119855.
GeneTreeENSGT00390000002884.
HOGENOMHOG000237356.
HOVERGENHBG019157.
OMAFFESTGS.
OrthoDBEOG77T14X.
TreeFamTF314939.

Gene expression databases

ArrayExpressQ9JJ00.
BgeeQ9JJ00.
CleanExMM_PLSCR1.
GenevestigatorQ9JJ00.

Family and domain databases

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

Other

NextBio301814.
PROQ9JJ00.
SOURCESearch...

Entry information

Entry namePLS1_MOUSE
AccessionPrimary (citable) accession number: Q9JJ00
Secondary accession number(s): O54730, O54731, Q9D1F8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 112 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