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   27-MAR-2024, entry version 165.
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=GK3 {ECO:0000312|HGNC:HGNC:4292}; Synonyms=GK3P, 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: May be involved in the regulation of glycerol uptake and
CC       metabolism. {ECO:0000305}.
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}.
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; 6.
DR   STRING; 9606.ENSP00000489687; -.
DR   iPTMnet; Q14409; -.
DR   PhosphoSitePlus; Q14409; -.
DR   SwissPalm; Q14409; -.
DR   BioMuta; GK3P; -.
DR   DMDM; 215277039; -.
DR   jPOST; Q14409; -.
DR   MassIVE; Q14409; -.
DR   MaxQB; Q14409; -.
DR   PeptideAtlas; Q14409; -.
DR   ProteomicsDB; 59984; -.
DR   Pumba; Q14409; -.
DR   Antibodypedia; 82498; 43 antibodies from 7 providers.
DR   Ensembl; ENST00000505354.3; ENSP00000489687.1; ENSG00000229894.5.
DR   MANE-Select; ENST00000505354.3; ENSP00000489687.1; NM_001395953.1; NP_001382882.1.
DR   AGR; HGNC:4292; -.
DR   GeneCards; GK3; -.
DR   HGNC; HGNC:4292; GK3.
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; VLEATSW; -.
DR   OrthoDB; 2734344at2759; -.
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 male germ line stem cell (sensu Vertebrata) in testis and 26 other cell types or 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: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   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR042018; GK1-3_metazoa.
DR   InterPro; IPR005999; Glycerol_kin.
DR   NCBIfam; TIGR01311; glycerol_kin; 1.
DR   PANTHER; PTHR10196:SF95; GLYCEROL KINASE 3; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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
//