PANK4_RAT
ID PANK4_RAT Reviewed; 773 AA.
AC Q923S8;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000250|UniProtKB:Q9NVE7};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9NVE7};
DE AltName: Full=Inactive pantothenic acid kinase 4 {ECO:0000250|UniProtKB:Q9NVE7};
DE Short=rPanK4 {ECO:0000303|PubMed:16132722};
GN Name=Pank4 {ECO:0000312|RGD:628857}; Synonyms=Fang1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PKM.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=16132722; DOI=10.1007/s11010-005-5535-1;
RA Li Y., Chang Y., Zhang L., Feng Q., Liu Z., Zhang Y., Zuo J., Meng Y.,
RA Fang F.;
RT "High glucose upregulates pantothenate kinase 4 (PanK4) and thus affects
RT M2-type pyruvate kinase (Pkm2).";
RL Mol. Cell. Biochem. 277:117-125(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Phosphatase which shows a preference for 4'-
CC phosphopantetheine and its oxidatively damaged forms (sulfonate or S-
CC sulfonate), providing strong indirect evidence that the phosphatase
CC activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing
CC excess 4'-phosphopantetheine could constitute a directed overflow
CC mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or
CC other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate
CC would forestall their conversion to inactive forms of CoA and acyl
CC carrier protein. May play a role in the physiological regulation of CoA
CC intracellular levels. {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate;
CC Xref=Rhea:RHEA:68328, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61723;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine
CC sulfonate + phosphate; Xref=Rhea:RHEA:68336, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:177300, ChEBI:CHEBI:177301;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-
CC sulfopantetheine + phosphate; Xref=Rhea:RHEA:68340,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177302,
CC ChEBI:CHEBI:177303; Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68341;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by Co(2+), Ni(2+),
CC Mg(2+) and Mn(2+). Activity is inhibited by EDTA.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- SUBUNIT: Homodimer. Interacts with PKM. {ECO:0000269|PubMed:16132722}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16132722}.
CC -!- INDUCTION: By glucose. {ECO:0000269|PubMed:16132722}.
CC -!- DOMAIN: Subfamily II proteins have an EGMGR motif about 50 residues
CC from the C-terminus (By similarity). This motif lies near the metal-
CC binding residues in the putative substrate-binding cleft 2 (By
CC similarity). Subfamily II proteins occur only in eukaryotes, in two
CC forms: as a stand-alone unit in plants, and as a C-terminal domain of
CC pantothenate kinases in plants, animals, and chytrid fungi (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4K6}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the type II
CC pantothenate kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the damage-control
CC phosphatase family. Phosphopantetheine phosphatase (II) subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Despite belonging to the type II pantothenate kinase family,
CC the pantothenate kinase domain contains a Val residue at position 147
CC and a Trp residue at position 211 instead of the two conserved active
CC site residues, Glu and Arg. Lacks pantothenate kinase activity.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
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DR EMBL; AF399873; AAK94009.1; -; mRNA.
DR RefSeq; NP_598215.1; NM_133531.2.
DR AlphaFoldDB; Q923S8; -.
DR SMR; Q923S8; -.
DR BioGRID; 251070; 2.
DR IntAct; Q923S8; 1.
DR STRING; 10116.ENSRNOP00000019028; -.
DR iPTMnet; Q923S8; -.
DR PhosphoSitePlus; Q923S8; -.
DR PaxDb; Q923S8; -.
DR PRIDE; Q923S8; -.
DR GeneID; 171053; -.
DR KEGG; rno:171053; -.
DR CTD; 55229; -.
DR RGD; 628857; Pank4.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR InParanoid; Q923S8; -.
DR OrthoDB; 865329at2759; -.
DR BRENDA; 2.7.1.33; 5301.
DR Reactome; R-RNO-196783; Coenzyme A biosynthesis.
DR SABIO-RK; Q923S8; -.
DR PRO; PR:Q923S8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.1700.10; -; 1.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR InterPro; IPR035073; At2g17340_3_helix_bundle.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR015844; PanK_long.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 2.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036939; PanK_long; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Hydrolase;
KW Manganese; Metal-binding; Nickel; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT CHAIN 2..773
FT /note="4'-phosphopantetheine phosphatase"
FT /id="PRO_0000161807"
FT REGION 2..402
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT REGION 403..773
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOTIF 724..728
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT BINDING 196
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 624
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 659
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 320
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80YV4"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 773 AA; 86243 MW; E566662F29616B40 CRC64;
MAECRASGGG SGGDSLDKSI TLPPDEIFRN LENAKRFAID IGGSLTKLAY YSTVQHKVAK
VRSFDHPGKD AEQDHEPPYE ISVQEEITAR LHFIKFENTY MEACLDFIRD HLVNTETKVI
QATGGGAYKF KDLIEEKLRL KVDKEDVMTC LIKGCNFVLK NIPHEAFMYQ KDSDPEFRFQ
TNHPNIFPYL LVNIGSGVSI VKVETEDRFE WIGGSSIGGG TFWGLGALLT KTKKFDELLQ
LASRGRHANV DMLVQDIYGG AHQTLGLSGN LIASSFGKSA TADREFSKED MAKSLLHMIS
NDIGQLACLY AKLHGLDRVY FGGFFIRGHP VTMRTITYSI NFFSKGEVQA LFLRHEGYLG
AIGAFLKGAE QDNPNQYSWG ENYAASSGLM STAPELCPTQ RARSGTFDLL EMDRLERPLV
NLPLLLDPSS YVPDTVDLTD DALARQYWLT CFEEALDGVV KRAVASQPES VDAAERAEKF
RQKYWGKLQT LRHQPFAYGT LTVRSLLDTR EHCLNEFNFP DPYSKVKQKE NGLALKCFQS
VTRSLDSLGW EERQLALVKG LLAGNVFDWG AKAVSDVLES DPQFGFEEAK RKLQERPWLV
DSYTKWLQRL KGPPHKCALI FADNSGIDII LGVFPFVREL LCRGIEVILA CNSGPALNDV
TYSESLIVAE RIAAMDPIIC TALREDRLLL VQTGSSPPCL DLSRLDKGLA VLVRERGADL
VVIEGMGRAV HTNYHALLRC ESLKLAVVKN AWLAERLGGQ LFSVIFKYEV PAE
