GLPK3_HUMAN
ID GLPK3_HUMAN Reviewed; 553 AA.
AC Q14409; Q6NXP9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Glycerol kinase 3 {ECO:0000305};
DE Short=GK 3;
DE Short=Glycerokinase 3;
DE EC=2.7.1.30;
DE AltName: Full=ATP:glycerol 3-phosphotransferase 3;
DE AltName: Full=Glycerol kinase 3 pseudogene {ECO:0000312|HGNC:HGNC:4292};
DE AltName: Full=Glycerol kinase, testis specific 1;
GN Name=GK3P {ECO:0000312|HGNC:HGNC:4292}; Synonyms=GKP3, GKTB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7987308; DOI=10.1093/hmg/3.8.1317;
RA Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.;
RT "The glycerol kinase gene family: structure of the Xp gene, and related
RT intronless retroposons.";
RL Hum. Mol. Genet. 3:1317-1324(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC EC=2.7.1.30;
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=In sperm the majority of
CC the enzyme is bound to mitochondria. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; X78711; CAA55364.1; -; mRNA.
DR EMBL; AC107059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066960; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q14409; -.
DR SMR; Q14409; -.
DR IntAct; Q14409; 5.
DR iPTMnet; Q14409; -.
DR PhosphoSitePlus; Q14409; -.
DR BioMuta; GK3P; -.
DR DMDM; 215277039; -.
DR jPOST; Q14409; -.
DR MassIVE; Q14409; -.
DR MaxQB; Q14409; -.
DR PaxDb; Q14409; -.
DR PeptideAtlas; Q14409; -.
DR PRIDE; Q14409; -.
DR ProteomicsDB; 59984; -.
DR Antibodypedia; 82498; 15 antibodies from 5 providers.
DR Ensembl; ENST00000505354.2; ENSP00000489687.1; ENSG00000229894.4.
DR MANE-Select; ENST00000505354.3; ENSP00000489687.1; NM_001395953.1; NP_001382882.1.
DR GeneCards; GK3P; -.
DR HGNC; HGNC:4292; GK3P.
DR HPA; ENSG00000229894; Tissue enriched (testis).
DR MIM; 600149; gene.
DR neXtProt; NX_Q14409; -.
DR OpenTargets; ENSG00000229894; -.
DR PharmGKB; PA28703; -.
DR VEuPathDB; HostDB:ENSG00000229894; -.
DR GeneTree; ENSGT01000000214434; -.
DR InParanoid; Q14409; -.
DR OMA; TTIVWNS; -.
DR PhylomeDB; Q14409; -.
DR PathwayCommons; Q14409; -.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SignaLink; Q14409; -.
DR UniPathway; UPA00618; UER00672.
DR Pharos; Q14409; Tdark.
DR PRO; PR:Q14409; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14409; protein.
DR Bgee; ENSG00000229894; Expressed in left testis and 25 other tissues.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IBA:GO_Central.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR CDD; cd07792; FGGY_GK1-3_metazoa; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR042018; GK1-3_metazoa.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycerol metabolism; Kinase; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..553
FT /note="Glycerol kinase 3"
FT /id="PRO_0000059537"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 427..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 99
FT /note="V -> A (in Ref. 1; CAA55364)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="E -> K (in Ref. 3; BC066960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 60598 MW; 1D6A197F32A921FB CRC64;
MAASKKAVLG PLVGAVDQGT SSTRFLVFNS RTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LHSVYECIEK TCEKLGQLNI GISNIKAIGV SNQRETTVVW DKITGEPLYN AVVWLDLRTQ
STVESLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VRKVQKAVEE KRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PHVRSSSEIY
GLMKAGALEG VPISGCLGDQ SAALVGQMCF QIGQAKNTYG TGCFLLCNTG HKCVFSDHGL
LTTVAYKLGR DKPVYYALEG SVAIAGAVIR WLRDNLGIIK TSEEIEKLAK EVGTSYGCYF
VPAFSGLYAP YWEPSARGII CGLTQFTNKC HIAFAALEAV CFQTREILDA MNRDCGIPLS
HLQVDGGMTS NKILMQLQAD ILYIPVVKPL MPETTALGAA MAAGAAEGVD VWSLEPEDLS
AVTMERFEPQ INAEESEIRY STWKKAVMKS MGWVTTQSPE GGDPSVFCSL PLGFFIVSSM
AMLIGARYIS GIP
