XKR4_PANTR
ID XKR4_PANTR Reviewed; 650 AA.
AC Q49LS4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=XKR4Q5GH76; Synonyms=XRG4 {ECO:0000303|Ref.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen Y.;
RT "A superfamily of XK-related genes (XRG) widely expressed in vertebrates
RT and invertebrates.";
RL Submitted (JUL-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; AY702907; AAV83786.1; -; mRNA.
DR RefSeq; NP_001028208.1; NM_001033036.1.
DR AlphaFoldDB; Q49LS4; -.
DR SMR; Q49LS4; -.
DR STRING; 9598.ENSPTRP00000034691; -.
DR PaxDb; Q49LS4; -.
DR GeneID; 613217; -.
DR KEGG; ptr:613217; -.
DR CTD; 114786; -.
DR eggNOG; KOG4790; Eukaryota.
DR InParanoid; Q49LS4; -.
DR OrthoDB; 1230316at2759; -.
DR Proteomes; UP000002277; Unplaced.
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..650
FT /note="XK-related protein 4"
FT /id="PRO_0000190779"
FT CHAIN 1..567
FT /note="XK-related protein 4, processed form"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
FT /id="PRO_0000453291"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 567..568
FT /note="Cleavage; by caspase-3, caspase-6 and caspase-7"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5GH67"
SQ SEQUENCE 650 AA; 71561 MW; 00FA6AE738BCA0B8 CRC64;
MAAKSDGRLK MKKSSDVAFT PLQNSDHSGS VQGLAPGLPS GSGAEDEEAA GGGCCPDGGG
CSRCCCCCAG SGSSAGSGGS GGVAGPGGGG AGSAALCLRL GREQRRYSLW DCLWILAAVA
VYFADVGTDV WLAVDYYLRG QRWWFGLTLF FVVLGSLSVQ VFSFRWFVHD FSTEDSATAA
AASSCPQPGA DCKTVVGGGS AAGEGEARPS TPQRQASNAS KSNIAAANSG SNSSGATRAS
GKHRSASCSF CIWLLQSLIH IFQLGQIWRY FHTIYLGIRS RQSGENDRWR FYWKMVYEYA
DVSMLHLLAT FLESAPQLVL QLCIIVQTHS LQALQGFTAA ASLVSLAWAL ASYQKALRDS
RDDKKPISYM AVIIQFCWHF FTIAARVITF ALFASVFQLY FGIFIVLHWC IMTFWIVHCE
TEFCITKWEE IVFDMVVGII YIFSWFNVKE GRTRCRLFIY YFVILLENTA LSALWYLYKA
PQIADAFAIP ALCVVFSSFL TGVVFMLMYY AFFHPNGPRF GQSPSCACED PAAAFPLPPD
VATSTLRSIS NNRSVVSDRD QKFAERDGCV PVFQVRPTAP STPSSRPPRI EESVIKIDLF
RNRYPAWERH VLDRSLRKAI LAFECSPSPP RLQYKDDALI QERLEYETTL
