XKR4_RAT
ID XKR4_RAT Reviewed; 647 AA.
AC Q5GH59;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=XK-related protein 4 {ECO:0000305};
DE Contains:
DE RecName: Full=XK-related protein 4, processed form {ECO:0000250|UniProtKB:Q5GH67};
GN Name=Xkr4 {ECO:0000312|RGD:1549780}; Synonyms=Xrg4 {ECO:0000303|Ref.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
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.
CC -!- FUNCTION: [XK-related protein 4, processed form]: Phospholipid
CC scramblase that promotes phosphatidylserine exposure on apoptotic cell
CC surface. Phosphatidylserine is a specific marker only present at the
CC surface of apoptotic cells and acts as a specific signal for
CC engulfment. {ECO:0000250|UniProtKB:Q5GH67}.
CC -!- CATALYTIC ACTIVITY: [XK-related protein 4, 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:0000250|UniProtKB:Q5GH67};
CC -!- ACTIVITY REGULATION: Phospholipid scramblase activity is activated upon
CC caspase cleavage to generate the XK-related protein 4, processed form.
CC Does not act prior the onset of apoptosis.
CC {ECO:0000250|UniProtKB:Q5GH67}.
CC -!- ACTIVITY REGULATION: [XK-related protein 4, processed form]:
CC Homodimerizes upon caspase cleavage. Phospholipid scramblase activity
CC is activated following interaction with the processed C-terminus of
CC XRCC4 (protein XRCC4, C-terminus). {ECO:0000250|UniProtKB:Q5GH67}.
CC -!- SUBUNIT: [XK-related protein 4, processed form]: Homodimer;
CC homodimerization takes place upon caspase cleavage. Interacts with the
CC processed C-terminus of XRCC4 (protein XRCC4, C-terminus); interaction
CC promotes the phospholipid scramblase activity.
CC {ECO:0000250|UniProtKB:Q5GH67}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5GH67};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: [XK-related protein 4, processed form]: Undergoes proteolytic
CC processing by caspase-3 (CASP3), caspase-6 (CASP6) and caspase-7
CC (CASP7) to generate the XK-related protein 4, processed form, leading
CC to its activation. {ECO:0000250|UniProtKB:Q5GH67}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000305}.
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DR EMBL; AY534258; AAT07107.1; -; mRNA.
DR RefSeq; NP_001011971.1; NM_001011971.1.
DR AlphaFoldDB; Q5GH59; -.
DR SMR; Q5GH59; -.
DR STRING; 10116.ENSRNOP00000029598; -.
DR PhosphoSitePlus; Q5GH59; -.
DR SwissPalm; Q5GH59; -.
DR PaxDb; Q5GH59; -.
DR PRIDE; Q5GH59; -.
DR GeneID; 297801; -.
DR KEGG; rno:297801; -.
DR UCSC; RGD:1549780; rat.
DR CTD; 114786; -.
DR RGD; 1549780; Xkr4.
DR VEuPathDB; HostDB:ENSRNOG00000027276; -.
DR eggNOG; KOG4790; Eukaryota.
DR HOGENOM; CLU_028534_1_0_1; -.
DR InParanoid; Q5GH59; -.
DR OrthoDB; 1230316at2759; -.
DR PhylomeDB; Q5GH59; -.
DR TreeFam; TF316454; -.
DR PRO; PR:Q5GH59; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000027276; Expressed in frontal cortex and 4 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; ISS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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; ISS:UniProtKB.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..647
FT /note="XK-related protein 4"
FT /id="PRO_0000190780"
FT CHAIN 1..564
FT /note="XK-related protein 4, processed form"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
FT /id="PRO_0000453292"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 193..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 564..565
FT /note="Cleavage; by caspase-3, caspase-6 and caspase-7"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
SQ SEQUENCE 647 AA; 72716 MW; C347575AA9456E2E CRC64;
MARPPPLLVQ KPSFLVEACC SPSPATHLAP YHTQPGARTP STIQRDLLFP IPRRCHARSS
PRPPALGGGP TQRLQHAARS AHPIPPSVKE IHPTFSEIPR ARASDCCAAA LGVQHWPARH
PHPPLPSISL AVDYYLLGQR WWFGLTLFFV VLGSLSVQVF SFRWFVHDFS TEDSATTTAS
TCQQPGADCK TVVSSGSAAG EGEARPSTPQ RQASNASKSN IAATNSGSNS NGATRTSGKH
RSASCSFCIW LLQSLIHILQ LGQVWRYLHT IYLGIRSRQS GESSRWRFYW KMVYEYADVS
MLHLLATFLE SAPQLVLQLC IIVQTHSLQA LQGFTAAASL VSLAWALASY QKALRDSRDD
KKPISYMAVI IQFCWHFFTI AARVITFALF ASVFQLYFGI FIVLHWCIMT FWIVHCETEF
CITKWEEIVF DMVVGIIYIF SWFNVKEGRT RCRLFIYYFV ILLENTALSA LWYLYKAPQI
ADAFAIPALC VVFSSFLTGV VFMLMYYAFF HPNGPRFGQS PSCACDDPAT AFSMPPEVAT
STLRSISNNR SVASDRDQKF AERDGCVPVF QVRPTAPPTP SSRPPRIEES VIKIDLFRNR
YPAWERHVLD RSLRKAILAF ECSPSPPRLQ YKDDALIQER LEYETTL