XKR8_MOUSE
ID XKR8_MOUSE Reviewed; 401 AA.
AC Q8C0T0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=XK-related protein 8 {ECO:0000305};
DE Short=mXkr8 {ECO:0000303|PubMed:23845944};
DE Contains:
DE RecName: Full=XK-related protein 8, processed form {ECO:0000250|UniProtKB:Q9H6D3};
GN Name=Xkr8 {ECO:0000303|PubMed:23845944, ECO:0000312|MGI:MGI:2685877};
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 STRAIN=C57BL/6J;
RA Huang C.-H., Chen Y.;
RT "A superfamily of XK-related genes (XRG) widely expressed in vertebrates
RT and invertebrates.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
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).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23845944; DOI=10.1126/science.1236758;
RA Suzuki J., Denning D.P., Imanishi E., Horvitz H.R., Nagata S.;
RT "Xk-Related protein 8 and CED-8 promote phosphatidylserine exposure in
RT apoptotic cells.";
RL Science 341:403-406(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE,
RP AND MUTAGENESIS OF VAL-35; ALA-46; SER-64; GLY-94; GLU-141; LEU-150;
RP GLN-163; SER-184; ILE-215; GLY-248; ASP-295; VAL-305 AND THR-309.
RX PubMed=25231987; DOI=10.1074/jbc.m114.583419;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Exposure of phosphatidylserine by Xk-related protein family members during
RT apoptosis.";
RL J. Biol. Chem. 289:30257-30267(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH BSG AND NPTN.
RX PubMed=27503893; DOI=10.1073/pnas.1610403113;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine
RT exposure.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9509-9514(2016).
RN [9]
RP FUNCTION.
RX PubMed=28881496; DOI=10.1111/febs.14261;
RA Kim G.W., Nam G.H., Kim I.S., Park S.Y.;
RT "Xk-related protein 8 regulates myoblast differentiation and survival.";
RL FEBS J. 284:3575-3588(2017).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30559640; DOI=10.3389/fnins.2018.00876;
RA Kautzman A.G., Keeley P.W., Ackley C.R., Leong S., Whitney I.E.,
RA Reese B.E.;
RT "Xkr8 modulates bipolar cell number in the mouse retina.";
RL Front. Neurosci. 12:876-876(2018).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29440417; DOI=10.1073/pnas.1720732115;
RA Kawano M., Nagata S.;
RT "Lupus-like autoimmune disease caused by a lack of Xkr8, a caspase-
RT dependent phospholipid scramblase.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2132-2137(2018).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT
RP THR-356; SER-361 AND THR-375, AND MUTAGENESIS OF 351-ASP--ASP-354; THR-356;
RP SER-361 AND THR-375.
RX PubMed=30718401; DOI=10.1073/pnas.1820499116;
RA Sakuragi T., Kosako H., Nagata S.;
RT "Phosphorylation-mediated activation of mouse Xkr8 scramblase for
RT phosphatidylserine exposure.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:2907-2912(2019).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31712393; DOI=10.1128/mcb.00402-19;
RA Yamashita Y., Suzuki C., Uchiyama Y., Nagata S.;
RT "Infertility caused by inefficient apoptotic germ cell clearance in Xkr8-
RT deficient male mice.";
RL Mol. Cell. Biol. 40:0-0(2020).
CC -!- FUNCTION: [XK-related protein 8, processed form]: Phospholipid
CC scramblase that promotes phosphatidylserine exposure on apoptotic cell
CC surface (PubMed:23845944, PubMed:25231987, PubMed:27503893,
CC PubMed:29440417, PubMed:30718401). Phosphatidylserine is a specific
CC marker only present at the surface of apoptotic cells and acts as a
CC specific signal for engulfment (PubMed:23845944, PubMed:29440417,
CC PubMed:30718401, PubMed:31712393). Required for the clearance of
CC apoptotic cells, such as engulfment of apoptotic germ cells by Sertoli
CC cells, clearance of senescent neutrophils or regulation of bipolar cell
CC numbers in the retina (PubMed:30559640, PubMed:29440417,
CC PubMed:31712393). Has no effect on calcium-induced exposure of
CC phosphatidylserine (By similarity). Promotes myoblast differentiation
CC and survival (PubMed:28881496). {ECO:0000250|UniProtKB:Q9H6D3,
CC ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:25231987,
CC ECO:0000269|PubMed:27503893, ECO:0000269|PubMed:28881496,
CC ECO:0000269|PubMed:29440417, ECO:0000269|PubMed:30559640,
CC ECO:0000269|PubMed:30718401, ECO:0000269|PubMed:31712393}.
CC -!- CATALYTIC ACTIVITY: [XK-related protein 8, processed form]:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000305|PubMed:25231987,
CC ECO:0000305|PubMed:30718401};
CC -!- ACTIVITY REGULATION: Activated upon caspase cleavage to generate the
CC XK-related protein 8, processed form (By similarity). Does not act
CC prior the onset of apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6D3}.
CC -!- SUBUNIT: Interacts with BSG and NPTN; which act as chaperones to
CC localize XKR8 at the cell membrane. {ECO:0000269|PubMed:27503893}.
CC -!- SUBUNIT: [XK-related protein 8, processed form]: Homodimer.
CC {ECO:0000250|UniProtKB:Q9H6D3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25231987};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:Q9H6D3}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in testis
CC (PubMed:23845944). Expressed in the bone marrow and mononuclear
CC leukocytes in the blood; highly expressed in thymocytes and lymphocytes
CC (PubMed:29440417). Expressed in the mature retina (PubMed:30559640).
CC {ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:29440417,
CC ECO:0000269|PubMed:30559640}.
CC -!- PTM: Undergoes proteolytic processing by caspase-3 (CASP3), leading to
CC its activation. {ECO:0000269|PubMed:25231987,
CC ECO:0000269|PubMed:30718401}.
CC -!- PTM: Phosphorylation at Thr-375 activates the phospholipid scramblase
CC activity. {ECO:0000269|PubMed:30718401}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice show defects in
CC phosphatidylserine exposure following apoptosis, leading to defects in
CC engulfment of apoptotic cells (PubMed:23845944, PubMed:29440417). Mice
CC on the MRL background develop a lupus-like autoimmune disease caused by
CC impaired clearance of apoptotic lymphocytes and aged neutrophils
CC (PubMed:29440417). Male mice are infertile due to reduced sperm counts
CC in their epididymides: defects are caused by inefficient clearance of
CC apoptotic germ cells by Sertoli cells in testes (PubMed:31712393).
CC {ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:29440417,
CC ECO:0000269|PubMed:31712393}.
CC -!- SIMILARITY: Belongs to the XK family. {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; AY534254; AAT07103.1; -; mRNA.
DR EMBL; AK029920; BAC26677.1; -; mRNA.
DR EMBL; AL627130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30093.1; -; Genomic_DNA.
DR EMBL; BC057035; AAH57035.1; -; mRNA.
DR CCDS; CCDS18732.1; -.
DR RefSeq; NP_958756.1; NM_201368.1.
DR AlphaFoldDB; Q8C0T0; -.
DR SMR; Q8C0T0; -.
DR STRING; 10090.ENSMUSP00000041205; -.
DR TCDB; 2.A.112.1.3; the kx blood-group antigen (kxa) family.
DR PaxDb; Q8C0T0; -.
DR PRIDE; Q8C0T0; -.
DR ProteomicsDB; 299712; -.
DR Antibodypedia; 55125; 80 antibodies from 19 providers.
DR DNASU; 381560; -.
DR Ensembl; ENSMUST00000045550; ENSMUSP00000041205; ENSMUSG00000037752.
DR GeneID; 381560; -.
DR KEGG; mmu:381560; -.
DR UCSC; uc008vbr.1; mouse.
DR CTD; 55113; -.
DR MGI; MGI:2685877; Xkr8.
DR VEuPathDB; HostDB:ENSMUSG00000037752; -.
DR eggNOG; KOG4790; Eukaryota.
DR GeneTree; ENSGT01050000244963; -.
DR HOGENOM; CLU_028534_2_1_1; -.
DR InParanoid; Q8C0T0; -.
DR OMA; GYLYRCL; -.
DR OrthoDB; 1230316at2759; -.
DR PhylomeDB; Q8C0T0; -.
DR TreeFam; TF316454; -.
DR BioGRID-ORCS; 381560; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q8C0T0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8C0T0; protein.
DR Bgee; ENSMUSG00000037752; Expressed in spermatocyte and 161 other tissues.
DR Genevisible; Q8C0T0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB.
DR GO; GO:1902742; P:apoptotic process involved in development; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0097350; P:neutrophil clearance; IMP:UniProtKB.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IDA:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0002513; P:tolerance induction to self antigen; IMP:MGI.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="XK-related protein 8"
FT /id="PRO_0000415854"
FT CHAIN 1..354
FT /note="XK-related protein 8, processed form"
FT /evidence="ECO:0000250|UniProtKB:Q9H6D3"
FT /id="PRO_0000423985"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 354..355
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q9H6D3"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30718401"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30718401"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 35
FT /note="V->A: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 46
FT /note="A->E: Abolished ability to promote
FT phosphatidylserine exposure. Promotes localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 64
FT /note="S->L: Abolished ability to promote
FT phosphatidylserine exposure. Promotes localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 94
FT /note="G->R: Abolished ability to promote
FT phosphatidylserine exposure. Promotes localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 141
FT /note="E->R: Abolished ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 150
FT /note="L->E: Abolished ability to promote
FT phosphatidylserine exposure. Promotes localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 163
FT /note="Q->T: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 184
FT /note="S->V: Abolished ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 215
FT /note="I->T: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 248
FT /note="G->T: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 295
FT /note="D->K: Abolished ability to promote
FT phosphatidylserine exposure. Promotes localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 305
FT /note="V->S: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 309
FT /note="T->F: Does not affect ability to promote
FT phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:25231987"
FT MUTAGEN 351..354
FT /note="DLVD->ALVA: In 2DA mutant; abolished cleavage by
FT CASP3 and ability to promote phosphatidylserine exposure."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 356
FT /note="T->A: Decreased phosphorylation; does not affect the
FT phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 356
FT /note="T->D: Mimics phosphorylation status; does not affect
FT the phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 361
FT /note="S->A: Decreased phosphorylation; does not affect the
FT phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 361
FT /note="S->D: Mimics phosphorylation status; does not affect
FT the phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 375
FT /note="T->A: Decreased phosphorylation; impairs the
FT phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
FT MUTAGEN 375
FT /note="T->D: Mimics phosphorylation status; activation of
FT the phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:30718401"
SQ SEQUENCE 401 AA; 45563 MW; F34F237653D6FCF9 CRC64;
MPLSVHHHVA LDVVVGLVSI LSFLLDLVAD LWAVVQYVLL GRYLWAALVL VLLGQASVLL
QLFSWLWLTA DPTELHHSQL SRPFLALLHL LQLGYLYRCL HGMHQGLSMC YQEMPSECDL
AYADFLSLDI SMLKLFESFL EATPQLTLVL AIVLQNGQAE YYQWFGISSS FLGISWALLD
YHRSLRTCLP SKPRLGRSSS AIYFLWNLLL LGPRICAIAL FSAVFPYYVA LHFFSLWLVL
LFWIWLQGTN FMPDSKGEWL YRVTMALILY FSWFNVSGGR TRGRAVIHLI FIFSDSVLLV
TTSWVTHGTW LPSGISLLMW VTIGGACFFL GLALRVIYYL WLHPSCSWDP DLVDGTLGLL
SPHRPPKLIY NRRATLLAEN FFAKAKARAV LTEEVQLNGV L
