GCKR_XENLA
ID GCKR_XENLA Reviewed; 619 AA.
AC Q91754; Q6PAX3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Glucokinase regulatory protein {ECO:0000303|PubMed:7925465};
DE Short=GKRP {ECO:0000303|PubMed:23733961};
DE Short=Glucokinase regulator {ECO:0000250|UniProtKB:Q14397};
GN Name=gckr {ECO:0000250|UniProtKB:Q14397};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7925465; DOI=10.1111/j.1432-1033.1994.00043.x;
RA Veiga-Da-Cunha M., Detheux M., Watelet N., van Schaftingen E.;
RT "Cloning and expression of a Xenopus liver cDNA encoding a fructose-
RT phosphate-insensitive regulatory protein of glucokinase.";
RL Eur. J. Biochem. 225:43-51(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:3W0L}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH GCK AND
RP KETO-D-FRUCTOSE 6-PHOSPHATE, FUNCTION, AND INTERACTION WITH GCK.
RX PubMed=23733961; DOI=10.1073/pnas.1300457110;
RA Choi J.M., Seo M.H., Kyeong H.H., Kim E., Kim H.S.;
RT "Molecular basis for the role of glucokinase regulatory protein as the
RT allosteric switch for glucokinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10171-10176(2013).
CC -!- FUNCTION: Regulates glucokinase (gck) by forming an inactive complex
CC with this enzyme (PubMed:23733961). The affinity of gckr for gck is
CC modulated by fructose metabolites: gckr with bound fructose 6-phosphate
CC has increased affinity for gck, while gckr with bound fructose 1-
CC phosphate has strongly decreased affinity for gck and does not inhibit
CC gck activity (PubMed:23733961). {ECO:0000269|PubMed:23733961}.
CC -!- SUBUNIT: Interacts (fructose 6-phosphate bound form) with gck.
CC {ECO:0000269|PubMed:23733961}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14397}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14397}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q07071}.
CC -!- DOMAIN: Fructose 1-phosphate and fructose 6-phosphate compete for the
CC same binding site. {ECO:0000269|PubMed:23733961}.
CC -!- SIMILARITY: Belongs to the GCKR family. {ECO:0000305}.
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DR EMBL; X80901; CAA56863.1; -; mRNA.
DR EMBL; BC060011; AAH60011.1; -; mRNA.
DR PIR; S48729; S48729.
DR RefSeq; NP_001083276.1; NM_001089807.1.
DR PDB; 3W0L; X-ray; 2.92 A; B/D=1-619.
DR PDBsum; 3W0L; -.
DR AlphaFoldDB; Q91754; -.
DR SMR; Q91754; -.
DR GeneID; 398839; -.
DR KEGG; xla:398839; -.
DR CTD; 398839; -.
DR Xenbase; XB-GENE-6255160; gckr.L.
DR OrthoDB; 858819at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398839; Expressed in kidney and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0070095; F:fructose-6-phosphate binding; ISS:UniProtKB.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; ISS:UniProtKB.
DR InterPro; IPR005486; Glucokinase_regulatory_CS.
DR InterPro; IPR040190; MURQ/GCKR.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10088; PTHR10088; 3.
DR SUPFAM; SSF53697; SSF53697; 2.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Mitochondrion; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..619
FT /note="Glucokinase regulatory protein"
FT /id="PRO_0000214828"
FT DOMAIN 90..283
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 319..498
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT REGION 462..464
FT /note="Essential for interaction with GCK"
FT /evidence="ECO:0000269|PubMed:23733961"
FT BINDING 107..109
FT /ligand="keto-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57579"
FT /evidence="ECO:0000269|PubMed:23733961,
FT ECO:0007744|PDB:3W0L"
FT BINDING 109..110
FT /ligand="beta-D-fructose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:138881"
FT /evidence="ECO:0000250|UniProtKB:Q14397"
FT BINDING 153
FT /ligand="beta-D-fructose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:138881"
FT /evidence="ECO:0000250|UniProtKB:Q14397"
FT BINDING 179..183
FT /ligand="keto-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57579"
FT /evidence="ECO:0000269|PubMed:23733961,
FT ECO:0007744|PDB:3W0L"
FT BINDING 179..181
FT /ligand="beta-D-fructose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:138881"
FT /evidence="ECO:0000250|UniProtKB:Q14397"
FT BINDING 347
FT /ligand="beta-D-fructose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:138881"
FT /evidence="ECO:0000250|UniProtKB:Q14397"
FT BINDING 347
FT /ligand="keto-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57579"
FT /evidence="ECO:0000269|PubMed:23733961,
FT ECO:0007744|PDB:3W0L"
FT BINDING 513
FT /ligand="beta-D-fructose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:138881"
FT /evidence="ECO:0000250|UniProtKB:Q14397"
FT BINDING 513
FT /ligand="keto-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57579"
FT /evidence="ECO:0000269|PubMed:23733961,
FT ECO:0007744|PDB:3W0L"
FT CONFLICT 530
FT /note="H -> Q (in Ref. 2; AAH60011)"
FT /evidence="ECO:0000305"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 261..279
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 309..324
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 446..451
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 452..460
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 469..495
FT /evidence="ECO:0007829|PDB:3W0L"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 512..525
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 530..542
FT /evidence="ECO:0007829|PDB:3W0L"
FT TURN 550..553
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 556..563
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 569..578
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 583..591
FT /evidence="ECO:0007829|PDB:3W0L"
FT HELIX 596..604
FT /evidence="ECO:0007829|PDB:3W0L"
SQ SEQUENCE 619 AA; 68739 MW; 41B72C1981D1BA52 CRC64;
MRGTRKYQHV IETPDPGKWE LAGYEESLPI SEKSNPMTRE LDKADPSQLV QLLRDCDAEI
FQEEDENLIH YHRLYSESVL KTMGDVAKRV QEVLKNPDDS LVVLSGCGTS GRLALLLANS
FNGLLKGLHK TPCYCYIMSG GDRSIVTSQE SSEDNPQLGA QELEKVCEGK KNVLFIGISC
GLSAPFIAGQ LDFCMRHLDV YLPVLVGFNP VSMARNERIE GWHSSFRQVA ERLQTLHDSQ
KGFILNPAVG PEGVSGSSRM KGGSATKILL ETLLLVAHKA ESNVPVTEKC LLEILRTYER
AHKVTYSQSK KIAALMKQTA TSLQKKGHLY ILGWGTLGLV GIMDAVECVP TYQADWRDVR
GFITGGYHSI ENKEGDLSSL GPQFSISHED FVKNVLPSVS ETDTVLLIFT LDDDLNQIEK
LVALVKEKTS NIQVICHATA GQYLPNSLKK TIPSIIGLTW PILFLEYEGA FIQKFQRELS
TKWILDTVTS GAYTLRGKIF RNFMVDFKIN NSKLFHRATS VLQRLTGQSH QRCTEVLLQS
IYGEQTLSEQ IRNTTIAGHV EAAASQDKVL PVAIVSLLRS CTIQDSRSRI NSSLSIRSAI
ESSMNVPGRK RGAEDSESR
