PLS2_MOUSE
ID PLS2_MOUSE Reviewed; 307 AA.
AC Q9DCW2; O70233; Q921P6;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Phospholipid scramblase 2;
DE Short=PL scramblase 2;
DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 2;
GN Name=Plscr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=9485382; DOI=10.1021/bi972625o;
RA Zhou Q., Sims P.J., Wiedmer T.;
RT "Identity of a conserved motif in phospholipid scramblase that is required
RT for Ca2+-accelerated transbilayer movement of membrane phospholipids.";
RL Biochemistry 37:2356-2360(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May mediate accelerated ATP-independent bidirectional
CC transbilayer migration of phospholipids upon binding calcium ions that
CC results in a loss of phospholipid asymmetry in the plasma membrane. May
CC play a central role in the initiation of fibrin clot formation, in the
CC activation of mast cells and in the recognition of apoptotic and
CC injured cells by the reticuloendothelial system.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in erythrocyte membranes, blood
CC platelets, blood leukocytes, T- and B-lymphocytes, vascular
CC endothelium, spleen, thymus, prostate, testis, uterus, intestine and
CC colon.
CC -!- DOMAIN: The N-terminal proline-rich domain (PRD) is required for
CC phospholipid scramblase activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phospholipid scramblase family.
CC {ECO:0000305}.
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DR EMBL; AF015790; AAC40053.1; -; mRNA.
DR EMBL; AK002410; BAB22079.1; -; mRNA.
DR EMBL; CH466560; EDL20918.1; -; Genomic_DNA.
DR EMBL; BC002012; AAH02012.1; -; mRNA.
DR EMBL; BC011299; AAH11299.1; -; mRNA.
DR CCDS; CCDS23405.1; -.
DR RefSeq; NP_001182013.1; NM_001195084.1.
DR RefSeq; NP_032906.2; NM_008880.3.
DR AlphaFoldDB; Q9DCW2; -.
DR IntAct; Q9DCW2; 1.
DR MINT; Q9DCW2; -.
DR STRING; 10090.ENSMUSP00000034932; -.
DR iPTMnet; Q9DCW2; -.
DR PhosphoSitePlus; Q9DCW2; -.
DR SwissPalm; Q9DCW2; -.
DR jPOST; Q9DCW2; -.
DR MaxQB; Q9DCW2; -.
DR PaxDb; Q9DCW2; -.
DR PRIDE; Q9DCW2; -.
DR ProteomicsDB; 289455; -.
DR DNASU; 18828; -.
DR Ensembl; ENSMUST00000034932; ENSMUSP00000034932; ENSMUSG00000032372.
DR Ensembl; ENSMUST00000180154; ENSMUSP00000136481; ENSMUSG00000032372.
DR GeneID; 18828; -.
DR KEGG; mmu:18828; -.
DR UCSC; uc009rao.2; mouse.
DR CTD; 57047; -.
DR MGI; MGI:1270860; Plscr2.
DR VEuPathDB; HostDB:ENSMUSG00000032372; -.
DR eggNOG; KOG0621; Eukaryota.
DR GeneTree; ENSGT00940000154435; -.
DR HOGENOM; CLU_053024_1_1_1; -.
DR InParanoid; Q9DCW2; -.
DR OMA; NCWAVCC; -.
DR OrthoDB; 1015148at2759; -.
DR PhylomeDB; Q9DCW2; -.
DR TreeFam; TF314939; -.
DR BioGRID-ORCS; 18828; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Plscr2; mouse.
DR PRO; PR:Q9DCW2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCW2; protein.
DR Bgee; ENSMUSG00000032372; Expressed in right kidney and 147 other tissues.
DR ExpressionAtlas; Q9DCW2; baseline and differential.
DR Genevisible; Q9DCW2; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0032791; F:lead ion binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR GO; GO:0004518; F:nuclease activity; ISO:MGI.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IBA:GO_Central.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; ISO:MGI.
DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; ISO:MGI.
DR GO; GO:0033003; P:regulation of mast cell activation; ISO:MGI.
DR InterPro; IPR005552; Scramblase.
DR PANTHER; PTHR23248; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
PE 1: Evidence at protein level;
KW Calcium; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; SH3-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Phospholipid scramblase 2"
FT /id="PRO_0000100788"
FT TOPO_DOM 1..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 287..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..307
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT REGION 1..82
FT /note="Proline-rich domain (PRD)"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..20
FT /note="SH3-binding 1"
FT /evidence="ECO:0000255"
FT MOTIF 82..89
FT /note="SH3-binding 2"
FT /evidence="ECO:0000255"
FT MOD_RES 159
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT LIPID 182
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 183
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 186
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 187
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT CONFLICT 178
FT /note="K -> R (in Ref. 1; AAC40053 and 4; AAH02012)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="P -> S (in Ref. 2; BAB22079)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="W -> S (in Ref. 2; BAB22079)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="K -> M (in Ref. 2; BAB22079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 34052 MW; 4B7D9CE9C2476E63 CRC64;
MEAPRSGTYL PAGYAPQYPP AAVQGPPEHT GRPTFQTNYQ VPQSGYPGPQ ASYTVSTSGH
EGYAATRLPI QNNQTIVLAN TQWMPAPPPI LNCPPGLEYL NQIDQLLIHQ QVELLEVLTG
FETNNKFEIK NSLGQMVYVA VEDTDCCTRN CCEASRPFTL RILDHLGQEV MTLERPLKCS
SCCFPCCLQE IEIQAPPGVP IGYVTQTWHP CLPKLTLQND KRENVLKVVG PCVACTCCSD
IDFEIKSLDE VTRIGKITKQ WSGCVKEAFT DSDNFGIQFP LDLEVKMKAV TLGACFLIDY
MFFEGCE
