PLS4_HUMAN
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 03-AUG-2022, entry version 182.
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; Q9H5F2: C11orf1; NbExp=5; IntAct=EBI-769257, EBI-718615;
CC Q9NRQ2; P23141-3: CES1; NbExp=3; IntAct=EBI-769257, EBI-12360993;
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};
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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; 75.
DR IntAct; Q9NRQ2; 73.
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; Q9NRQ2; -.
DR PeptideAtlas; Q9NRQ2; -.
DR PRIDE; Q9NRQ2; -.
DR ProteomicsDB; 82403; -. [Q9NRQ2-1]
DR ProteomicsDB; 82404; -. [Q9NRQ2-2]
DR Antibodypedia; 948; 131 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 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; TDYMGRE; -.
DR OrthoDB; 1015148at2759; -.
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 1066 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 199 other tissues.
DR ExpressionAtlas; Q9NRQ2; baseline and differential.
DR Genevisible; Q9NRQ2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
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
