XKR9_MOUSE
ID XKR9_MOUSE Reviewed; 373 AA.
AC Q5GH62; B2RWB3;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=XK-related protein 9 {ECO:0000305};
DE Contains:
DE RecName: Full=XK-related protein 9, processed form {ECO:0000305|PubMed:25231987};
GN Name=Xkr9 {ECO:0000303|PubMed:25231987, ECO:0000312|MGI:MGI:2686466};
GN Synonyms=Gm1620 {ECO:0000312|MGI:MGI:2686466}, Xrg9 {ECO:0000303|Ref.1};
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 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC CLEAVAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 354-ASP--ASP-357.
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).
CC -!- FUNCTION: [XK-related protein 9, processed form]: Phospholipid
CC scramblase that promotes phosphatidylserine exposure on apoptotic cell
CC surface (PubMed:25231987). Phosphatidylserine is a specific marker only
CC present at the surface of apoptotic cells and acts as a specific signal
CC for engulfment (PubMed:25231987). {ECO:0000269|PubMed:25231987}.
CC -!- CATALYTIC ACTIVITY: [XK-related protein 9, 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 -!- ACTIVITY REGULATION: Activated upon caspase cleavage to generate the
CC XK-related protein 9, processed form (PubMed:25231987). Does not act
CC prior the onset of apoptosis (PubMed:25231987).
CC {ECO:0000269|PubMed:25231987}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25231987};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the small intestines; weakly
CC expressed in the pancreas, liver, stomach, and large intestines.
CC {ECO:0000269|PubMed:25231987}.
CC -!- PTM: [XK-related protein 9]: Undergoes proteolytic processing by
CC caspase-3 (CASP3), caspase-6 (CASP6) and caspase-7 (CASP7) to generate
CC the XK-related protein 9, processed form, leading to its activation.
CC {ECO:0000269|PubMed:25231987}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000305}.
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DR EMBL; AY534255; AAT07104.1; -; mRNA.
DR EMBL; BC147699; AAI47700.1; -; mRNA.
DR CCDS; CCDS14824.1; -.
DR RefSeq; NP_001011873.1; NM_001011873.2.
DR RefSeq; XP_006495610.1; XM_006495547.3.
DR AlphaFoldDB; Q5GH62; -.
DR SMR; Q5GH62; -.
DR STRING; 10090.ENSMUSP00000085900; -.
DR iPTMnet; Q5GH62; -.
DR PhosphoSitePlus; Q5GH62; -.
DR PaxDb; Q5GH62; -.
DR PRIDE; Q5GH62; -.
DR ProteomicsDB; 300002; -.
DR Antibodypedia; 51209; 7 antibodies from 6 providers.
DR DNASU; 381246; -.
DR Ensembl; ENSMUST00000088542; ENSMUSP00000085900; ENSMUSG00000067813.
DR GeneID; 381246; -.
DR KEGG; mmu:381246; -.
DR UCSC; uc007aiv.1; mouse.
DR CTD; 389668; -.
DR MGI; MGI:2686466; Xkr9.
DR VEuPathDB; HostDB:ENSMUSG00000067813; -.
DR eggNOG; KOG4790; Eukaryota.
DR GeneTree; ENSGT01050000244963; -.
DR HOGENOM; CLU_028534_2_0_1; -.
DR InParanoid; Q5GH62; -.
DR OMA; VSMEFLY; -.
DR OrthoDB; 1230316at2759; -.
DR PhylomeDB; Q5GH62; -.
DR TreeFam; TF316454; -.
DR BioGRID-ORCS; 381246; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q5GH62; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5GH62; protein.
DR Bgee; ENSMUSG00000067813; Expressed in jejunum and 20 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IDA:UniProtKB.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="XK-related protein 9"
FT /id="PRO_0000190797"
FT CHAIN 1..357
FT /note="XK-related protein 9, processed form"
FT /evidence="ECO:0000305|PubMed:25231987"
FT /id="PRO_0000453294"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 357..358
FT /note="Cleavage; by caspase-3, caspase-6 and caspase-7"
FT /evidence="ECO:0000305|PubMed:25231987"
FT MUTAGEN 354..357
FT /note="DETD->AETA: In 2DA mutant; abolished cleavage by
FT caspase, preventing phospholipid scramblase activity."
FT /evidence="ECO:0000269|PubMed:25231987"
SQ SEQUENCE 373 AA; 43271 MW; 8F3C976AB36BE067 CRC64;
MKYTKCNFMM SVLGIIIYVT DLVADIVLSV RYFHDGQYVL GVLTLSFVLC GTLIVHCFSY
SWLKADLEKA GQENERYFLL LHCLQGGVFT RYWFALRTGY HVVFKHSDRK SNFMEEQTDP
HKEAIDMATD LSMLRLFETY LEGCPQLILQ LYAFLECGQA NLSQCMVIMV SCCAISWSTV
DYQIALRKSL PDKNLLRGLW PKLMYLFYKL LTLLSWMLSV VLLLFVDVRV ALLLLLFLWI
TGFIWAFINH TQFCNSVSME FLYRIVVGFI LVFTFFNIKG QNTKCPMSCY YTVRVLGTLG
ILTVFWIYPL SIFNSDYFIP ISATIVLALL LGIIFLGVYY GNFHPNRNVE PQLDETDGKA
PQRDCRIRYF LMD
