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FCSK_MOUSE
ID   FCSK_MOUSE              Reviewed;        1090 AA.
AC   Q7TMC8; Q7TSB1; Q8C7W3; Q8CI18;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=L-fucose kinase {ECO:0000305};
DE            Short=Fucokinase {ECO:0000312|MGI:MGI:1916071};
DE            EC=2.7.1.52 {ECO:0000269|PubMed:14686921};
GN   Name=Fcsk; Synonyms=Fuk {ECO:0000312|MGI:MGI:1916071};
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] {ECO:0000312|EMBL:CAD59135.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ {ECO:0000312|EMBL:CAD59135.1};
RX   PubMed=14686921; DOI=10.1046/j.1432-1033.2003.03904.x;
RA   Niittymaki J., Mattila P., Roos C., Huopaniemi L., Sjoblom S., Renkonen R.;
RT   "Cloning and expression of murine enzymes involved in the salvage pathway
RT   of GDP-L-fucose.";
RL   Eur. J. Biochem. 271:78-86(2004).
RN   [2] {ECO:0000312|EMBL:AAP20647.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP20647.1};
RA   Jang J.S., Ackerman S.L.;
RT   "cDNA sequences of L-fucose kinase.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0000312|EMBL:EDL11475.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000312|EMBL:AAH37698.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N {ECO:0000312|EMBL:AAH37698.1};
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:AAH37698.1};
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   [6] {ECO:0000312|EMBL:BAC33572.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-1090 (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33572.1};
RC   TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAC33572.1};
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Takes part in the salvage pathway for reutilization of fucose
CC       from the degradation of oligosaccharides.
CC       {ECO:0000305|PubMed:14686921}.
CC   -!- FUNCTION: [Isoform 1]: Has strong fucokinase activity.
CC       {ECO:0000269|PubMed:14686921}.
CC   -!- FUNCTION: [Isoform 2]: Has very weak fucokinase activity.
CC       {ECO:0000269|PubMed:14686921}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-fucose = ADP + beta-L-fucose 1-phosphate + H(+);
CC         Xref=Rhea:RHEA:13241, ChEBI:CHEBI:2181, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57268, ChEBI:CHEBI:456216;
CC         EC=2.7.1.52; Evidence={ECO:0000269|PubMed:14686921};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TMC8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TMC8-2; Sequence=VSP_058365;
CC   -!- TISSUE SPECIFICITY: Isoform 1: Expressed strongly in brain, ovary and
CC       testis, moderately in kidney and liver, and weakly in lung, spleen and
CC       heart. Isoform 2: Expressed very strongly in brain, strongly in ovary,
CC       testis and kidney, moderately in lung and liver, and weakly in heart
CC       and spleen. {ECO:0000269|PubMed:14686921}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family.
CC       {ECO:0000255|RuleBase:RU004209}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37698.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ534942; CAD59135.1; -; mRNA.
DR   EMBL; AJ297482; CAC82178.4; -; mRNA.
DR   EMBL; AY223865; AAP20647.1; -; mRNA.
DR   EMBL; AC132945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466525; EDL11475.1; -; Genomic_DNA.
DR   EMBL; BC037698; AAH37698.1; ALT_INIT; mRNA.
DR   EMBL; AK049153; BAC33572.1; -; mRNA.
DR   CCDS; CCDS22666.1; -. [Q7TMC8-1]
DR   RefSeq; NP_758487.2; NM_172283.3. [Q7TMC8-1]
DR   AlphaFoldDB; Q7TMC8; -.
DR   STRING; 10090.ENSMUSP00000039271; -.
DR   iPTMnet; Q7TMC8; -.
DR   PhosphoSitePlus; Q7TMC8; -.
DR   EPD; Q7TMC8; -.
DR   MaxQB; Q7TMC8; -.
DR   PaxDb; Q7TMC8; -.
DR   PeptideAtlas; Q7TMC8; -.
DR   PRIDE; Q7TMC8; -.
DR   ProteomicsDB; 271611; -. [Q7TMC8-1]
DR   ProteomicsDB; 271612; -. [Q7TMC8-2]
DR   Antibodypedia; 29979; 160 antibodies from 27 providers.
DR   DNASU; 234730; -.
DR   Ensembl; ENSMUST00000041382; ENSMUSP00000039271; ENSMUSG00000033703. [Q7TMC8-1]
DR   GeneID; 234730; -.
DR   KEGG; mmu:234730; -.
DR   UCSC; uc009nlg.2; mouse. [Q7TMC8-1]
DR   CTD; 197258; -.
DR   MGI; MGI:1916071; Fcsk.
DR   VEuPathDB; HostDB:ENSMUSG00000033703; -.
DR   eggNOG; KOG4644; Eukaryota.
DR   GeneTree; ENSGT00390000002251; -.
DR   HOGENOM; CLU_006983_0_0_1; -.
DR   InParanoid; Q7TMC8; -.
DR   OMA; QRWREAW; -.
DR   OrthoDB; 135001at2759; -.
DR   PhylomeDB; Q7TMC8; -.
DR   TreeFam; TF314554; -.
DR   BRENDA; 2.7.1.52; 3474.
DR   Reactome; R-MMU-6787639; GDP-fucose biosynthesis.
DR   BioGRID-ORCS; 234730; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q7TMC8; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q7TMC8; protein.
DR   Bgee; ENSMUSG00000033703; Expressed in paneth cell and 222 other tissues.
DR   ExpressionAtlas; Q7TMC8; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050201; F:fucokinase activity; IDA:UniProtKB.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR   GO; GO:0042352; P:GDP-L-fucose salvage; ISS:UniProtKB.
DR   GO; GO:1903350; P:response to dopamine; IEA:Ensembl.
DR   InterPro; IPR012887; Fucokinase.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF07959; Fucokinase; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1090
FT                   /note="L-fucose kinase"
FT                   /id="PRO_0000436383"
FT   BINDING         834..845
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         923..993
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058365"
SQ   SEQUENCE   1090 AA;  119267 MW;  46A1FA0750424B9E CRC64;
     MEQSEGVNWT VIILTCQYKD SVQVFQRELE VRQRREQIPA GTMLLAVEDP QTRVGSGGAT
     LNALLVAAEH LSARAGFTVV TSDVLHSAWI LILHMGRDFP FDDCGRAFTC LPVENPQAPV
     EALVCNLDCL LDIMTHRLGP GSPPGVWVCS TDMLLSVPPN PGISWDGFRG ARVIAFPGSL
     AYALNHGVYL TDSQGLVLDI YYQGTKAEIQ RCVGPDGLVP LVSGVVFFSV ETAEHLLATH
     VSPPLDACTY MGLDSGAQPV QLSLFFDILL CMARNMSREN FLAGRPPELG QGDMDVASYL
     KGARAQLWRE LRDQPLTMVY VPDGGYSYMT TDATEFLHRL TMPGVAVAQI VHSQVEEPQL
     LEATCSVVSC LLEGPVHLGP RSVLQHCHLR GPIRIGAGCF VSGLDTAHSE ALHGLELHDV
     ILQGHHVRLH GSLSRVFTLA GRLDSWERQG AGMYLNMSWN EFFKKTGIRD WDLWDPDTPP
     SDRCLLTARL FPVLHPTRAL GPQDVLWMLH PRKHRGEALR AWRASWRLSW EQLQPCVDRA
     ATLDFRRDLF FCQALQKARH VLEARQDLCL RPLIRAAVGE GCSGPLLATL DKVAAGAEDP
     GVAARALACV ADVLGCMAEG RGGLRSGPAA NPEWIQPFSY LECGDLMRGV EALAQEREKW
     LTRPALLVRA ARHYEGAEQI LIRQAVMTAR HFVSTQPVEL PAPGQWVVTE CPARVDFSGG
     WSDTPPIAYE LGGAVLGLAV RVDGRRPIGA KARRIPEPEL WLAVGPRQDE MTMRIVCRSL
     DDLRDYCQPH APGALLKAAF ICAGIVHLHS ELPLLEQLLH SFNGGFELHT WSELPHGSGL
     GTSSILAGAA LAALQRAAGR AVGTEALIHA VLHLEQVLTT GGGWQDQVSG LMPGIKVGRS
     RAQLPLKVEV EEITVPEGFV QKINDHLLLV YTGKTRLARN LLQDVLRNWY ARLPVVVQNA
     RRLVRQTEKC AEAFRQGNLP LLGQYLTSYW EQKKLMAPGC EPLAVQRMMD VLAPYAYGQS
     LAGAGGGGFL YLLTKEPRQK ETLEAVLAKA EGLGNYSVHL VEVDPQGLSL QLLGHDTRLC
     GAGPSEVGTT
 
 
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