PANK4_HUMAN
ID PANK4_HUMAN Reviewed; 773 AA.
AC Q9NVE7; B9DI84; Q53EU3; Q5TA84; Q7RTX3; Q9H3X5;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000303|PubMed:27322068};
DE EC=3.1.3.- {ECO:0000269|PubMed:27322068};
DE AltName: Full=Inactive pantothenic acid kinase 4 {ECO:0000303|PubMed:30927326};
DE Short=hPanK4;
GN Name=PANK4 {ECO:0000312|HGNC:HGNC:19366};
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 [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-684.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-773, AND VARIANT VAL-547.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11479594; DOI=10.1038/ng572;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-
RT Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-404, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=27322068; DOI=10.1038/nchembio.2108;
RA Huang L., Khusnutdinova A., Nocek B., Brown G., Xu X., Cui H., Petit P.,
RA Flick R., Zallot R., Balmant K., Ziemak M.J., Shanklin J.,
RA de Crecy-Lagard V., Fiehn O., Gregory J.F. III, Joachimiak A.,
RA Savchenko A., Yakunin A.F., Hanson A.D.;
RT "A family of metal-dependent phosphatases implicated in metabolite damage-
RT control.";
RL Nat. Chem. Biol. 12:621-627(2016).
RN [16]
RP LACK OF PANTOTHENATE KINASE ACTIVITY, AND MUTAGENESIS OF VAL-147 AND
RP TRP-211.
RX PubMed=30927326; DOI=10.1002/pro.3611;
RA Yao J., Subramanian C., Rock C.O., Jackowski S.;
RT "Human pantothenate kinase 4 is a pseudo-pantothenate kinase.";
RL Protein Sci. 28:1031-1047(2019).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-475.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP INVOLVEMENT IN CTRCT49, AND TISSUE SPECIFICITY.
RX PubMed=30585370; DOI=10.1002/humu.23696;
RA Sun M., Chen C., Hou S., Li X., Wang H., Zhou J., Chen X., Liu P.,
RA Kijlstra A., Lin S., Ye J.;
RT "A novel mutation of PANK4 causes autosomal dominant congenital posterior
RT cataract.";
RL Hum. Mutat. 40:380-391(2019).
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
CC (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could
CC constitute a directed overflow mechanism to prevent its oxidation to
CC the S-sulfonate, sulfonate, or other forms (PubMed:27322068).
CC Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would
CC forestall their conversion to inactive forms of CoA and acyl carrier
CC protein (PubMed:27322068). May play a role in the physiological
CC regulation of CoA intracellular levels (Probable).
CC {ECO:0000269|PubMed:27322068, ECO:0000305|PubMed:27322068}.
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:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000305|PubMed:27322068};
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:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000305|PubMed:27322068};
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:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68341;
CC Evidence={ECO:0000305|PubMed:27322068};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:27322068};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:27322068};
CC Note=Phosphatase activity is strongly promoted by several divalent
CC cation ions but is it suggested that Mn(2+) and possibly Ni(2+)
CC represent biologically relevant metal ion cofactors for damage-control
CC phosphatases. {ECO:0000269|PubMed:27322068};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by Co(2+), Ni(2+),
CC Mg(2+) and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA
CC (PubMed:27322068). {ECO:0000269|PubMed:27322068}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1920 uM for p-nitrophenylphosphate {ECO:0000269|PubMed:27322068};
CC KM=150 uM for D-pantetheine 4'-phosphate
CC {ECO:0000269|PubMed:27322068};
CC KM=3.90 uM for D-pantetheine 4'-phosphate-sulfonate
CC {ECO:0000269|PubMed:27322068};
CC Note=kcat is 0.17 sec(-1) with p-nitrophenylphosphate as substrate.
CC kcat is 0.71 sec(-1) with D-pantetheine 4'-phosphate as substrate.
CC kcat is 0.09 sec(-1) with D-pantetheine 4'-phosphate-sulfonate as
CC substrate. {ECO:0000269|PubMed:27322068};
CC -!- SUBUNIT: Homodimer. Interacts with PKM. {ECO:0000250|UniProtKB:Q923S8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q923S8}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high expression in the muscle
CC (PubMed:11479594). Expressed in the retina and lens epithelium, mainly
CC in ganglion cell layer, outer plexiform layer and retinal pigment layer
CC (at protein level) (PubMed:30585370). {ECO:0000269|PubMed:11479594,
CC ECO:0000269|PubMed:30585370}.
CC -!- DOMAIN: Subfamily II proteins have an EGMGR motif about 50 residues
CC from the C-terminus (Probable). This motif lies near the metal-binding
CC residues in the putative substrate-binding cleft 2 (Probable).
CC Subfamily II proteins occur only in eukaryotes, in two forms: as a
CC stand-alone unit in plants, and as a C-terminal domain of pantothenate
CC kinases in plants, animals, and chytrid fungi (Probable).
CC {ECO:0000305|PubMed:27322068}.
CC -!- DISEASE: Cataract 49 (CTRCT49) [MIM:619593]: A form of cataract, an
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT49 is
CC an autosomal dominant form characterized by congenital cataract located
CC in the posterior region of the lens. Visual impairment has onset in
CC early childhood. {ECO:0000269|PubMed:30585370}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
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:0000269|PubMed:30927326}.
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DR EMBL; AK001644; BAA91805.1; -; mRNA.
DR EMBL; AK223546; BAD97266.1; -; mRNA.
DR EMBL; AL139246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56097.1; -; Genomic_DNA.
DR EMBL; BC043496; AAH43496.1; -; mRNA.
DR EMBL; AL442072; CAC09438.1; -; mRNA.
DR EMBL; BK000012; DAA00006.1; -; Genomic_DNA.
DR CCDS; CCDS42.2; -.
DR RefSeq; NP_060686.2; NM_018216.2.
DR AlphaFoldDB; Q9NVE7; -.
DR SMR; Q9NVE7; -.
DR BioGRID; 120524; 65.
DR IntAct; Q9NVE7; 8.
DR MINT; Q9NVE7; -.
DR STRING; 9606.ENSP00000367727; -.
DR iPTMnet; Q9NVE7; -.
DR MetOSite; Q9NVE7; -.
DR PhosphoSitePlus; Q9NVE7; -.
DR SwissPalm; Q9NVE7; -.
DR BioMuta; PANK4; -.
DR DMDM; 27805669; -.
DR EPD; Q9NVE7; -.
DR jPOST; Q9NVE7; -.
DR MassIVE; Q9NVE7; -.
DR MaxQB; Q9NVE7; -.
DR PaxDb; Q9NVE7; -.
DR PeptideAtlas; Q9NVE7; -.
DR PRIDE; Q9NVE7; -.
DR ProteomicsDB; 82788; -.
DR Antibodypedia; 1627; 140 antibodies from 21 providers.
DR DNASU; 55229; -.
DR Ensembl; ENST00000378466.9; ENSP00000367727.5; ENSG00000157881.16.
DR Ensembl; ENST00000615291.3; ENSP00000478189.1; ENSG00000273494.3.
DR GeneID; 55229; -.
DR KEGG; hsa:55229; -.
DR MANE-Select; ENST00000378466.9; ENSP00000367727.5; NM_018216.4; NP_060686.3.
DR UCSC; uc001ajm.2; human.
DR CTD; 55229; -.
DR DisGeNET; 55229; -.
DR GeneCards; PANK4; -.
DR GeneReviews; PANK4; -.
DR HGNC; HGNC:19366; PANK4.
DR HPA; ENSG00000157881; Low tissue specificity.
DR MalaCards; PANK4; -.
DR MIM; 606162; gene.
DR MIM; 619593; phenotype.
DR neXtProt; NX_Q9NVE7; -.
DR OpenTargets; ENSG00000157881; -.
DR Orphanet; 98993; Early-onset posterior polar cataract.
DR PharmGKB; PA134887214; -.
DR VEuPathDB; HostDB:ENSG00000157881; -.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR GeneTree; ENSGT00940000158896; -.
DR HOGENOM; CLU_012496_1_1_1; -.
DR InParanoid; Q9NVE7; -.
DR OMA; NHPLSMH; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; Q9NVE7; -.
DR TreeFam; TF342917; -.
DR BioCyc; MetaCyc:HS08249-MON; -.
DR PathwayCommons; Q9NVE7; -.
DR Reactome; R-HSA-196783; Coenzyme A biosynthesis.
DR SignaLink; Q9NVE7; -.
DR BioGRID-ORCS; 55229; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; PANK4; human.
DR GeneWiki; PANK4; -.
DR GenomeRNAi; 55229; -.
DR Pharos; Q9NVE7; Tbio.
DR PRO; PR:Q9NVE7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NVE7; protein.
DR Bgee; ENSG00000157881; Expressed in apex of heart and 92 other tissues.
DR ExpressionAtlas; Q9NVE7; baseline and differential.
DR Genevisible; Q9NVE7; HS.
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: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; Cataract; Coenzyme A biosynthesis; Cytoplasm;
KW Hydrolase; Manganese; Metal-binding; Nickel; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..773
FT /note="4'-phosphopantetheine phosphatase"
FT /id="PRO_0000161806"
FT REGION 2..402
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000305|PubMed:27322068"
FT REGION 403..773
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000305|PubMed:27322068"
FT MOTIF 724..728
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000305|PubMed:27322068"
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:0007744|PubMed:19413330"
FT MOD_RES 320
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80YV4"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80YV4"
FT VARIANT 475
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs966358882)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035470"
FT VARIANT 547
FT /note="A -> V (in dbSNP:rs7535528)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_027409"
FT VARIANT 684
FT /note="Q -> R (in dbSNP:rs2494620)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_015170"
FT MUTAGEN 147
FT /note="V->E: Does not induce acetyl-CoA production.
FT Restores a moderate increase in acetyl-CoA production; when
FT associated with R-211."
FT /evidence="ECO:0000269|PubMed:30927326"
FT MUTAGEN 211
FT /note="W->R: Does not induce acetyl-CoA production.
FT Restores a moderate increase in acetyl-CoA production; when
FT associated with E-147."
FT /evidence="ECO:0000269|PubMed:30927326"
SQ SEQUENCE 773 AA; 85991 MW; D55027171A85E8B6 CRC64;
MAECGASGSG SSGDSLDKSI TLPPDEIFRN LENAKRFAID IGGSLTKLAY YSTVQHKVAK
VRSFDHSGKD TEREHEPPYE ISVQEEITAR LHFIKFENTY IEACLDFIKD HLVNTETKVI
QATGGGAYKF KDLIEEKLRL KVDKEDVMTC LIKGCNFVLK NIPHEAFVYQ KDSDPEFRFQ
TNHPHIFPYL LVNIGSGVSI VKVETEDRFE WVGGSSIGGG TFWGLGALLT KTKKFDELLH
LASRGQHSNV DMLVRDVYGG AHQTLGLSGN LIASSFGKSA TADQEFSKED MAKSLLHMIS
NDIGQLACLH ARLHSLDRVY FGGFFIRGHP VTMRTITYSI NFFSKGEVQA LFLRHEGYLG
AIGAFLKGAE QDNPNQYSWG ENYAGSSGLM SASPELGPAQ RARSGTFDLL EMDRLERPLV
DLPLLLDPPS YVPDTVDLTD DALARKYWLT CFEEALDGVV KRAVASQPDS VDAAERAEKF
RQKYWNKLQT LRQQPFAYGT LTVRSLLDTR EHCLNEFNFP DPYSKVKQRE NGVALRCFPG
VVRSLDALGW EERQLALVKG LLAGNVFDWG AKAVSAVLES DPYFGFEEAK RKLQERPWLV
DSYSEWLQRL KGPPHKCALI FADNSGIDII LGVFPFVREL LLRGTEVILA CNSGPALNDV
THSESLIVAE RIAGMDPVVH SALQEERLLL VQTGSSSPCL DLSRLDKGLA ALVRERGADL
VVIEGMGRAV HTNYHAALRC ESLKLAVIKN AWLAERLGGR LFSVIFKYEV PAE
