PLS4_MOUSE
ID PLS4_MOUSE Reviewed; 326 AA.
AC P58196; Q3TMI2; Q8BH62;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phospholipid scramblase 4;
DE Short=PL scramblase 4;
DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 4;
GN Name=Plscr4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hippocampus, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
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 Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with PDCD6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
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; AK035919; BAC29242.1; -; mRNA.
DR EMBL; AK082330; BAC38468.1; -; mRNA.
DR EMBL; AK141580; BAE24748.1; -; mRNA.
DR EMBL; AK165919; BAE38460.1; -; mRNA.
DR EMBL; BC052067; AAH52067.1; -; mRNA.
DR CCDS; CCDS23407.1; -.
DR RefSeq; NP_848826.1; NM_178711.3.
DR AlphaFoldDB; P58196; -.
DR STRING; 10090.ENSMUSP00000034941; -.
DR PhosphoSitePlus; P58196; -.
DR SwissPalm; P58196; -.
DR MaxQB; P58196; -.
DR PaxDb; P58196; -.
DR PeptideAtlas; P58196; -.
DR PRIDE; P58196; -.
DR ProteomicsDB; 289626; -.
DR Antibodypedia; 948; 131 antibodies from 26 providers.
DR DNASU; 235527; -.
DR Ensembl; ENSMUST00000034941; ENSMUSP00000034941; ENSMUSG00000032377.
DR GeneID; 235527; -.
DR KEGG; mmu:235527; -.
DR UCSC; uc009ras.1; mouse.
DR CTD; 57088; -.
DR MGI; MGI:2143267; Plscr4.
DR VEuPathDB; HostDB:ENSMUSG00000032377; -.
DR eggNOG; KOG0621; Eukaryota.
DR GeneTree; ENSGT00940000161947; -.
DR HOGENOM; CLU_053024_0_0_1; -.
DR InParanoid; P58196; -.
DR OMA; TDYMGRE; -.
DR OrthoDB; 1015148at2759; -.
DR PhylomeDB; P58196; -.
DR TreeFam; TF314939; -.
DR BRENDA; 7.6.2.1; 3474.
DR BioGRID-ORCS; 235527; 4 hits in 75 CRISPR screens.
DR PRO; PR:P58196; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58196; protein.
DR Bgee; ENSMUSG00000032377; Expressed in sciatic nerve and 149 other tissues.
DR Genevisible; P58196; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0017128; F:phospholipid scramblase activity; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IBA:GO_Central.
DR InterPro; IPR005552; Scramblase.
DR PANTHER; PTHR23248; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
PE 2: Evidence at transcript level;
KW Calcium; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Phospholipid scramblase 4"
FT /id="PRO_0000100793"
FT TOPO_DOM 1..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..326
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT REGION 1..94
FT /note="Proline-rich domain (PRD)"
FT /evidence="ECO:0000250"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 18..25
FT /note="SH3-binding 1"
FT /evidence="ECO:0000255"
FT MOTIF 30..33
FT /note="PPxY motif"
FT /evidence="ECO:0000255"
FT MOTIF 41..49
FT /note="SH3-binding 2"
FT /evidence="ECO:0000255"
FT MOTIF 94..102
FT /note="SH3-binding 3"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 194
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 195
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 197
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
FT LIPID 198
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O15162"
SQ SEQUENCE 326 AA; 36579 MW; 4798174B69DD7555 CRC64;
MSGLVPTAPE QPTEEMENQI KSPTAVPDAP PDYNSHFAPG PAGPVASPSA GLPMGYYIPQ
QPGAIPLYHP TGGTHPIQYQ PGKYPVTNQP APIMWMAGPA PVPNCPPGLE YLAQLDNIHV
LQHVEPLELM TRFETNNRYD IKNNIDQMVY IVTEDTDDFT RNAYRNLRPF VLRVTDCLGR
EIMTMQRPFR CTCCCFCCPC ARQELEVQCP PGVTIGFVAE HWNLCRASYS IQNEKKESMM
RVRGPCATYG CGSDSVFEIN SLDGVSNIGS IIRKWNGFLS TMVNADHFEI RFPLALDVKM
KAMIFGSCFL IDFMYFERPP PRRMSR
