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CERK1_MOUSE
ID   CERK1_MOUSE             Reviewed;         531 AA.
AC   Q8K4Q7; Q52KP2;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Ceramide kinase;
DE            Short=mCERK;
DE            EC=2.7.1.138 {ECO:0000269|PubMed:16269826};
DE   AltName: Full=Acylsphingosine kinase;
GN   Name=Cerk;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=11956206; DOI=10.1074/jbc.m201535200;
RA   Sugiura M., Kono K., Liu H., Shimizugawa T., Minekura H., Spiegel S.,
RA   Kohama T.;
RT   "Ceramide kinase, a novel lipid kinase. Molecular cloning and functional
RT   characterization.";
RL   J. Biol. Chem. 277:23294-23300(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
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 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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=16269826; DOI=10.1194/jlr.m500321-jlr200;
RA   Van Overloop H., Gijsbers S., Van Veldhoven P.P.;
RT   "Further characterization of mammalian ceramide kinase: substrate delivery
RT   and (stereo)specificity, tissue distribution, and subcellular localization
RT   studies.";
RL   J. Lipid Res. 47:268-283(2006).
CC   -!- FUNCTION: Catalyzes specifically the phosphorylation of ceramide to
CC       form ceramide 1-phosphate (PubMed:16269826). Acts efficiently on
CC       natural and analog ceramides (C6, C8, C16 ceramides, and C8-
CC       dihydroceramide), to a lesser extent on C2-ceramide and C6-
CC       dihydroceramide, but not on other lipids, such as various sphingosines
CC       (PubMed:16269826). Shows a greater preference for D-erythro isomer of
CC       ceramides (By similarity). Binds phosphoinositides (By similarity).
CC       {ECO:0000250|UniProtKB:Q8TCT0, ECO:0000269|PubMed:16269826}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine
CC         1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674,
CC         ChEBI:CHEBI:456216; EC=2.7.1.138;
CC         Evidence={ECO:0000269|PubMed:16269826};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930;
CC         Evidence={ECO:0000305|PubMed:16269826};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-
CC         hexanoylsphing-4-enine 1-phosphate; Xref=Rhea:RHEA:43312,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63867,
CC         ChEBI:CHEBI:82959, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-(acetyl)-sphing-4-enine = ADP + H(+) + N-(acetyl)-
CC         sphing-4-enine-1-phosphate; Xref=Rhea:RHEA:47904, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:46979, ChEBI:CHEBI:85375,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47905;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-hexadecanoylsphing-4-enine = ADP + H(+) + N-
CC         (hexadecanoyl)-sphing-4-enine-1-phosphate; Xref=Rhea:RHEA:46340,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72959,
CC         ChEBI:CHEBI:72963, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46341;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-hexanoyl-(4R)-hydroxysphinganine = ADP + H(+) + N-
CC         hexanoyl-(4R)-hydroxysphinganine-1-phosphate; Xref=Rhea:RHEA:47916,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:88095,
CC         ChEBI:CHEBI:88096, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47917;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT0};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCT0}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8TCT0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8TCT0}.
CC   -!- TISSUE SPECIFICITY: High level expression in heart, brain, testis and
CC       pancreas; low expression in spleen, liver and lung; not detected in
CC       skeletal muscle. {ECO:0000269|PubMed:11956206,
CC       ECO:0000269|PubMed:16269826}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at 7 dpc and decreases rapidly
CC       thereafter. {ECO:0000269|PubMed:11956206}.
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DR   EMBL; AB079067; BAC01155.1; -; mRNA.
DR   EMBL; AK042077; BAC31157.1; -; mRNA.
DR   EMBL; AK052269; BAC34908.1; -; mRNA.
DR   EMBL; AK169528; BAE41212.1; -; mRNA.
DR   EMBL; BC094253; AAH94253.1; -; mRNA.
DR   CCDS; CCDS27728.1; -.
DR   RefSeq; NP_663450.3; NM_145475.4.
DR   AlphaFoldDB; Q8K4Q7; -.
DR   SMR; Q8K4Q7; -.
DR   BioGRID; 230189; 2.
DR   STRING; 10090.ENSMUSP00000038203; -.
DR   PhosphoSitePlus; Q8K4Q7; -.
DR   MaxQB; Q8K4Q7; -.
DR   PaxDb; Q8K4Q7; -.
DR   PRIDE; Q8K4Q7; -.
DR   ProteomicsDB; 281382; -.
DR   Antibodypedia; 326; 325 antibodies from 29 providers.
DR   DNASU; 223753; -.
DR   Ensembl; ENSMUST00000044332; ENSMUSP00000038203; ENSMUSG00000035891.
DR   GeneID; 223753; -.
DR   KEGG; mmu:223753; -.
DR   UCSC; uc007xdx.2; mouse.
DR   CTD; 64781; -.
DR   MGI; MGI:2386052; Cerk.
DR   VEuPathDB; HostDB:ENSMUSG00000035891; -.
DR   eggNOG; KOG1115; Eukaryota.
DR   GeneTree; ENSGT00940000156976; -.
DR   HOGENOM; CLU_013399_2_2_1; -.
DR   InParanoid; Q8K4Q7; -.
DR   OMA; HHKTTAF; -.
DR   OrthoDB; 681139at2759; -.
DR   PhylomeDB; Q8K4Q7; -.
DR   TreeFam; TF314514; -.
DR   BRENDA; 2.7.1.138; 3474.
DR   Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR   BioGRID-ORCS; 223753; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Cerk; mouse.
DR   PRO; PR:Q8K4Q7; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8K4Q7; protein.
DR   Bgee; ENSMUSG00000035891; Expressed in cerebellum lobe and 221 other tissues.
DR   ExpressionAtlas; Q8K4Q7; baseline and differential.
DR   Genevisible; Q8K4Q7; MM.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001729; F:ceramide kinase activity; IDA:UniProtKB.
DR   GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR045363; CERK_C.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   Pfam; PF19280; CERK_C; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell membrane; Cytoplasm; Kinase; Lipid metabolism;
KW   Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..531
FT                   /note="Ceramide kinase"
FT                   /id="PRO_0000181355"
FT   DOMAIN          128..278
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   REGION          1..125
FT                   /note="Required for binding to sulfatide and
FT                   phosphoinositides"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT0"
FT   REGION          1..115
FT                   /note="Essential for enzyme activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT0"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYA1"
FT   BINDING         138..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         170..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         195..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYA1"
FT   BINDING         202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         239..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         502..504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT0"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT0"
FT   CONFLICT        378
FT                   /note="M -> V (in Ref. 1; BAC01155)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="D -> Y (in Ref. 2; BAC34908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   531 AA;  59843 MW;  C5A030D422E3AA10 CRC64;
     MGAMGAAEPL HSVLWVKRRR CAVSLEPARA LLRWWRSPEP GPSAPGADAR SVLVSEIIAV
     EEKDDCEKHA SSGRWHKMEN PFAFTVHRVK RVRHHRWKWA RVTFWSADEQ LCHLWLQTLR
     GLLESLTSRP KHLLVFINPF GGKGQGKRIY EKTVAPLFTL ASITTEIIIT EHANQAKETL
     YEINTDSYDG IVCVGGDGMF SEVLHGVIGR TQQSAGIDPN HPRAVLVPST LRIGIIPAGS
     TDCVCYSTVG TNDAETSALH IIIGDSLAID VSSVHYHNTL LRYSVSLLGY GFYGDLIKDS
     EKKRWMGLVR YDFSGLKTFL SHQYYEGTLS FLPAQHTVGS PRDNKPCRAG CFVCRQSKQQ
     LEEEEKKALY GLENAEEMEE WQVTCGKFLA INATNMSCAC PRSPGGLSPF AHLGDGSSDL
     ILIRKCSRFN FLRFLIRHTN QEDQFDFTFV EVYRVKKFHF TSKHVEDEDN DSKEQEKQKF
     GKICKDRPSC TCSASRSSWN CDGEVMHSPA IEVRVHCQLV RLFARGIEEE S
 
 
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