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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
 
 
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