GLPK2_MACFA
ID GLPK2_MACFA Reviewed; 553 AA.
AC Q4R4D5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Glycerol kinase 2;
DE Short=GK 2;
DE Short=Glycerokinase 2;
DE EC=2.7.1.30;
DE AltName: Full=ATP:glycerol 3-phosphotransferase 2;
DE AltName: Full=Glycerol kinase, testis specific 2;
GN Name=GK2; ORFNames=QtsA-10839;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism. Essential for male fertility and sperm mitochondrial sheath
CC formation (By similarity). Required for proper arrangement of crescent-
CC like mitochondria to form the mitochondrial sheath during
CC spermatogenesis (By similarity). Can induce mitochondrial clustering
CC through interactions with PLD6 and up-regulation of phosphatidic acid
CC synthesis in the mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:Q9WU65}.
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 -!- SUBUNIT: Interacts with ARMC12 and PLD6.
CC {ECO:0000250|UniProtKB:Q9WU65}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9WU65}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9WU65}. Cytoplasm {ECO:0000250}. Note=In sperm
CC the majority of the enzyme is bound to mitochondria.
CC {ECO:0000250|UniProtKB:Q9WU65}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB178979; BAE02030.1; -; mRNA.
DR RefSeq; NP_001270487.1; NM_001283558.1.
DR AlphaFoldDB; Q4R4D5; -.
DR SMR; Q4R4D5; -.
DR STRING; 9541.XP_005555022.1; -.
DR PRIDE; Q4R4D5; -.
DR GeneID; 101865283; -.
DR CTD; 2712; -.
DR eggNOG; KOG2517; Eukaryota.
DR OrthoDB; 519426at2759; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0097226; C:sperm mitochondrial sheath; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0120317; P:sperm mitochondrial sheath assembly; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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; Differentiation; Glycerol metabolism; Kinase;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Spermatogenesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..553
FT /note="Glycerol kinase 2"
FT /id="PRO_0000343677"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 553 AA; 60705 MW; 8A6567D268217EF0 CRC64;
MADPKTAAVG PLVGAVVQGT DSTRFLVFSS KTAELLSHHK VELTQEFPKE GWVEQDPKEI
LQSVYECIAR TCEKLDEMNI DISNIKAVGI SNQRETTVIW DKLTGEPLYN AVVWLDLRTQ
TTVEDLSKKI PGNSNFVKSK TGLPLSTYFS AVKLRWMLDN VRHVQKAVEE GRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKELC DFFEIPMDLL PNVFSSSEIY
GLIKTGALEG VPISGCLGDQ CAALVGQMCF QEGQAKNTYG TGCFLLCNTG RKCVFSEHGL
LTTIAYKLGK EKPAYYALEG SVAIAGAVIR WLRDNLGIIE TSGDIEKLAK EVGTSYGCYF
VPAFSGLYAP YWEPSARGIL CGLTQFTNKC HIAFAALEAV CFQTREILEA MNRDCGIPLR
HLQVDGGMTN NKVLMQLQAD ILHIPVIKPF MPETTALGAA MAAGAAEGVS VWSLEPQALS
VLRMERFEPQ IQATESEIRY ATWKKAVMKS MGWVTSQSPE SGDPSIFSSM PLGFFIVSSM
VMLIGARYIS GMP
