ID PLS4_HUMAN Reviewed; 329 AA. AC Q9NRQ2; A8K2E9; Q2TTR3; Q658L3; Q6ZR73; Q7Z505; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Phospholipid scramblase 4; DE Short=PL scramblase 4; DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 4; DE AltName: Full=Cell growth-inhibiting gene 43 protein; DE AltName: Full=TRA1; GN Name=PLSCR4; ORFNames=GIG43; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-34 AND VAL-155. RC TISSUE=Pancreas; RX PubMed=10930526; DOI=10.1016/s0005-2736(00)00236-4; RA Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.; RT "Identification of three new members of the phospholipid scramblase gene RT family."; RL Biochim. Biophys. Acta 1467:244-253(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-34 AND RP VAL-155. RA Kim J.W.; RT "Identification of a human cell growth inhibiting gene."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Thalamus, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Stomach; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-329 (ISOFORM 1). RA Cui W.C., Yu L., Gao J., Fan Y.X., Xu Y.F., Zhao S.Y.; RT "Cloning and characterization of a novel human cDNA homology to murine TRA1 RT mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP INTERACTION WITH PDCD6. RX PubMed=18256029; DOI=10.1074/jbc.m800717200; RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., RA Maki M.; RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human RT phospholipid scramblase 3: differential binding to an alternatively spliced RT isoform and amino acid-substituted mutants."; RL J. Biol. Chem. 283:9623-9632(2008). RN [10] RP COFACTOR, AND MUTAGENESIS OF ASP-290. RX PubMed=23089641; DOI=10.1515/hsz-2012-0129; RA Francis V.G., Gummadi S.N.; RT "Biochemical and functional characterization of human phospholipid RT scramblase 4 (hPLSCR4)."; RL Biol. Chem. 393:1173-1181(2012). 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; CC Evidence={ECO:0000269|PubMed:23089641}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:23089641}; CC -!- SUBUNIT: Interacts with PDCD6. {ECO:0000269|PubMed:18256029}. CC -!- INTERACTION: CC Q9NRQ2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-769257, EBI-10173507; CC Q9NRQ2; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-769257, EBI-12811889; CC Q9NRQ2; P23141-3: CES1; NbExp=3; IntAct=EBI-769257, EBI-12360993; CC Q9NRQ2; Q9H5F2: CFAP68; NbExp=5; IntAct=EBI-769257, EBI-718615; CC Q9NRQ2; Q16740: CLPP; NbExp=3; IntAct=EBI-769257, EBI-1056029; CC Q9NRQ2; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-769257, EBI-713677; CC Q9NRQ2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-769257, EBI-724310; CC Q9NRQ2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-769257, EBI-742054; CC Q9NRQ2; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-769257, EBI-11977403; CC Q9NRQ2; P15976-2: GATA1; NbExp=3; IntAct=EBI-769257, EBI-9090198; CC Q9NRQ2; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-769257, EBI-745201; CC Q9NRQ2; P49639: HOXA1; NbExp=5; IntAct=EBI-769257, EBI-740785; CC Q9NRQ2; Q5TA45: INTS11; NbExp=3; IntAct=EBI-769257, EBI-748258; CC Q9NRQ2; P16144-2: ITGB4; NbExp=3; IntAct=EBI-769257, EBI-11051601; CC Q9NRQ2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-769257, EBI-6426443; CC Q9NRQ2; Q5T749: KPRP; NbExp=3; IntAct=EBI-769257, EBI-10981970; CC Q9NRQ2; Q9NSB4: KRT82; NbExp=3; IntAct=EBI-769257, EBI-1045341; CC Q9NRQ2; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-769257, EBI-11741292; CC Q9NRQ2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-769257, EBI-10171774; CC Q9NRQ2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-769257, EBI-12811111; CC Q9NRQ2; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-769257, EBI-1048945; CC Q9NRQ2; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-769257, EBI-12805508; CC Q9NRQ2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-769257, EBI-10241353; CC Q9NRQ2; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-769257, EBI-18395721; CC Q9NRQ2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-769257, EBI-9996449; CC Q9NRQ2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-769257, EBI-3957694; CC Q9NRQ2; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-769257, EBI-10172511; CC Q9NRQ2; Q3LI64: KRTAP6-1; NbExp=4; IntAct=EBI-769257, EBI-12111050; CC Q9NRQ2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-769257, EBI-11962084; CC Q9NRQ2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-769257, EBI-10261141; CC Q9NRQ2; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-769257, EBI-11962058; CC Q9NRQ2; Q5T751: LCE1C; NbExp=3; IntAct=EBI-769257, EBI-12224199; CC Q9NRQ2; O14633: LCE2B; NbExp=3; IntAct=EBI-769257, EBI-11478468; CC Q9NRQ2; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-769257, EBI-11955689; CC Q9NRQ2; Q5JR59: MTUS2; NbExp=5; IntAct=EBI-769257, EBI-742948; CC Q9NRQ2; Q8IV28: NID2; NbExp=3; IntAct=EBI-769257, EBI-10261509; CC Q9NRQ2; Q7Z3S9: NOTCH2NLA; NbExp=5; IntAct=EBI-769257, EBI-945833; CC Q9NRQ2; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-769257, EBI-12813389; CC Q9NRQ2; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-769257, EBI-11956269; CC Q9NRQ2; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-769257, EBI-744023; CC Q9NRQ2; P10745: RBP3; NbExp=3; IntAct=EBI-769257, EBI-12806054; CC Q9NRQ2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-769257, EBI-740343; CC Q9NRQ2; P62979: RPS27A; NbExp=3; IntAct=EBI-769257, EBI-357375; CC Q9NRQ2; Q16348: SLC15A2; NbExp=3; IntAct=EBI-769257, EBI-12806032; CC Q9NRQ2; Q96M29: TEKT5; NbExp=3; IntAct=EBI-769257, EBI-10239812; CC Q9NRQ2; Q6N022: TENM4; NbExp=3; IntAct=EBI-769257, EBI-12827077; CC Q9NRQ2; Q8IWZ5: TRIM42; NbExp=5; IntAct=EBI-769257, EBI-5235829; CC Q9NRQ2; Q15645: TRIP13; NbExp=5; IntAct=EBI-769257, EBI-358993; CC Q9NRQ2; O14817: TSPAN4; NbExp=3; IntAct=EBI-769257, EBI-8652667; CC Q9NRQ2; P62987: UBA52; NbExp=3; IntAct=EBI-769257, EBI-357304; CC Q9NRQ2; P0CG47: UBB; NbExp=3; IntAct=EBI-769257, EBI-413034; CC Q9NRQ2; P0CG48: UBC; NbExp=3; IntAct=EBI-769257, EBI-3390054; CC Q9NRQ2; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-769257, EBI-2510804; CC Q9NRQ2; P09022: Hoxa1; Xeno; NbExp=4; IntAct=EBI-769257, EBI-3957603; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NRQ2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NRQ2-2; Sequence=VSP_042931, VSP_042932; CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver, CC kidney, pancreas, spleen, thymus, prostate, testis, uterus, small CC intestine and colon. Not detected in peripheral blood lymphocytes. 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP97186.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF199023; AAF89960.1; -; mRNA. DR EMBL; AY550971; AAT52217.1; -; mRNA. DR EMBL; AK128442; BAC87442.1; -; mRNA. DR EMBL; AK290214; BAF82903.1; -; mRNA. DR EMBL; AL833760; CAH56232.1; -; mRNA. DR EMBL; AC092982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78935.1; -; Genomic_DNA. DR EMBL; BC028354; AAH28354.1; -; mRNA. DR EMBL; AF087887; AAP97186.1; ALT_SEQ; mRNA. DR CCDS; CCDS3133.1; -. [Q9NRQ2-1] DR CCDS; CCDS54651.1; -. [Q9NRQ2-2] DR RefSeq; NP_001121776.1; NM_001128304.1. [Q9NRQ2-1] DR RefSeq; NP_001121777.1; NM_001128305.1. [Q9NRQ2-1] DR RefSeq; NP_001121778.1; NM_001128306.1. DR RefSeq; NP_001170775.1; NM_001177304.1. [Q9NRQ2-2] DR RefSeq; NP_065086.2; NM_020353.2. [Q9NRQ2-1] DR RefSeq; XP_005247711.1; XM_005247654.2. [Q9NRQ2-1] DR RefSeq; XP_005247712.1; XM_005247655.2. [Q9NRQ2-1] DR RefSeq; XP_011511333.1; XM_011513031.2. [Q9NRQ2-1] DR PDB; 3Q5U; X-ray; 2.50 A; B=271-283. DR PDBsum; 3Q5U; -. DR AlphaFoldDB; Q9NRQ2; -. DR SMR; Q9NRQ2; -. DR BioGRID; 121357; 76. DR IntAct; Q9NRQ2; 70. DR MINT; Q9NRQ2; -. DR STRING; 9606.ENSP00000347038; -. DR TCDB; 9.A.36.1.4; the ca(2+)-dependent phospholipid scramblase (scramblase) family. DR iPTMnet; Q9NRQ2; -. DR PhosphoSitePlus; Q9NRQ2; -. DR SwissPalm; Q9NRQ2; -. DR BioMuta; PLSCR4; -. DR DMDM; 212276457; -. DR EPD; Q9NRQ2; -. DR jPOST; Q9NRQ2; -. DR MassIVE; Q9NRQ2; -. DR MaxQB; Q9NRQ2; -. DR PaxDb; 9606-ENSP00000347038; -. DR PeptideAtlas; Q9NRQ2; -. DR ProteomicsDB; 82403; -. [Q9NRQ2-1] DR ProteomicsDB; 82404; -. [Q9NRQ2-2] DR Pumba; Q9NRQ2; -. DR Antibodypedia; 948; 149 antibodies from 26 providers. DR DNASU; 57088; -. DR Ensembl; ENST00000354952.7; ENSP00000347038.2; ENSG00000114698.15. [Q9NRQ2-1] DR Ensembl; ENST00000433593.6; ENSP00000415605.2; ENSG00000114698.15. [Q9NRQ2-2] DR Ensembl; ENST00000446574.6; ENSP00000399315.2; ENSG00000114698.15. [Q9NRQ2-1] DR Ensembl; ENST00000493382.5; ENSP00000419040.1; ENSG00000114698.15. [Q9NRQ2-1] DR GeneID; 57088; -. DR KEGG; hsa:57088; -. DR MANE-Select; ENST00000354952.7; ENSP00000347038.2; NM_020353.3; NP_065086.2. DR UCSC; uc003evt.6; human. [Q9NRQ2-1] DR AGR; HGNC:16497; -. DR CTD; 57088; -. DR DisGeNET; 57088; -. DR GeneCards; PLSCR4; -. DR HGNC; HGNC:16497; PLSCR4. DR HPA; ENSG00000114698; Low tissue specificity. DR MIM; 607612; gene. DR neXtProt; NX_Q9NRQ2; -. DR OpenTargets; ENSG00000114698; -. DR PharmGKB; PA33422; -. DR VEuPathDB; HostDB:ENSG00000114698; -. DR eggNOG; KOG0621; Eukaryota. DR GeneTree; ENSGT00940000161947; -. DR HOGENOM; CLU_053024_0_0_1; -. DR InParanoid; Q9NRQ2; -. DR OMA; MMTSFET; -. DR OrthoDB; 4390at2759; -. DR PhylomeDB; Q9NRQ2; -. DR TreeFam; TF314939; -. DR BRENDA; 7.6.2.1; 2681. DR PathwayCommons; Q9NRQ2; -. DR SignaLink; Q9NRQ2; -. DR BioGRID-ORCS; 57088; 9 hits in 1144 CRISPR screens. DR ChiTaRS; PLSCR4; human. DR GeneWiki; PLSCR4; -. DR GenomeRNAi; 57088; -. DR Pharos; Q9NRQ2; Tbio. DR PRO; PR:Q9NRQ2; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9NRQ2; Protein. DR Bgee; ENSG00000114698; Expressed in germinal epithelium of ovary and 201 other cell types or tissues. DR ExpressionAtlas; Q9NRQ2; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0042609; F:CD4 receptor binding; IPI:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0017128; F:phospholipid scramblase activity; IBA:GO_Central. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IBA:GO_Central. DR InterPro; IPR005552; Scramblase. DR PANTHER; PTHR23248:SF28; PHOSPHOLIPID SCRAMBLASE 4; 1. DR PANTHER; PTHR23248; PHOSPHOLIPID SCRAMBLASE-RELATED; 1. DR Pfam; PF03803; Scramblase; 1. DR Genevisible; Q9NRQ2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Lipoprotein; Membrane; KW Palmitate; Phosphoprotein; Reference proteome; Repeat; SH3-binding; KW Transmembrane; Transmembrane helix. FT CHAIN 1..329 FT /note="Phospholipid scramblase 4" FT /id="PRO_0000100792" FT TOPO_DOM 1..303 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 304..320 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 321..329 FT /note="Extracellular" FT /evidence="ECO:0000250" FT REGION 1..98 FT /note="Proline-rich domain (PRD)" FT /evidence="ECO:0000250" FT REGION 1..51 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 98..106 FT /note="SH3-binding 3" FT /evidence="ECO:0000255" FT COMPBIAS 23..51 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 83 FT /note="Phosphotyrosine; by ABL" FT /evidence="ECO:0000250" FT MOD_RES 88 FT /note="Phosphotyrosine; by ABL" FT /evidence="ECO:0000250" 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" FT LIPID 199 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 201 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 202 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT VAR_SEQ 1..15 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042931" FT VAR_SEQ 119..208 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042932" FT VARIANT 34 FT /note="N -> S (in dbSNP:rs3762685)" FT /evidence="ECO:0000269|PubMed:10930526, ECO:0000269|Ref.2" FT /id="VAR_011315" FT VARIANT 155 FT /note="I -> V (in dbSNP:rs1061409)" FT /evidence="ECO:0000269|PubMed:10930526, ECO:0000269|Ref.2" FT /id="VAR_011316" FT MUTAGEN 290 FT /note="D->A: 50% decrease in scramblase activity in FT presence of Ca2+, and 40% decrease in scramblase activity FT in presence of Mg2+." FT /evidence="ECO:0000269|PubMed:23089641" FT CONFLICT 56..57 FT /note="LP -> FL (in Ref. 8; AAP97186)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="P -> S (in Ref. 2; AAT52217)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="S -> L (in Ref. 8; AAP97186)" FT /evidence="ECO:0000305" FT CONFLICT 163 FT /note="F -> V (in Ref. 8; AAP97186)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="V -> G (in Ref. 8; AAP97186)" FT /evidence="ECO:0000305" SQ SEQUENCE 329 AA; 37005 MW; 12BE86728D54F794 CRC64; MSGVVPTAPE QPAGEMENQT KPPDPRPDAP PEYNSHFLPG PPGTAVPPPT GYPGGLPMGY YSPQQPSTFP LYQPVGGIHP VRYQPGKYPM PNQSVPITWM PGPTPMANCP PGLEYLVQLD NIHVLQHFEP LEMMTCFETN NRYDIKNNSD QMVYIVTEDT DDFTRNAYRT LRPFVLRVTD CMGREIMTMQ RPFRCTCCCF CCPSARQELE VQCPPGVTIG FVAEHWNLCR AVYSIQNEKK ENVMRVRGPC STYGCGSDSV FEVKSLDGIS NIGSIIRKWN GLLSAMADAD HFDIHFPLDL DVKMKAMIFG ACFLIDFMYF ERSPPQRSR //