HZG_DROME
ID HZG_DROME Reviewed; 352 AA.
AC M9PFN0; Q7YU53; Q9VUX0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Phosphatase Herzog {ECO:0000303|PubMed:31491385, ECO:0000312|FlyBase:FBgn0036556};
DE EC=3.1.3.16 {ECO:0000269|PubMed:31491385};
GN Name=hzg {ECO:0000303|PubMed:31491385, ECO:0000312|FlyBase:FBgn0036556};
GN Synonyms=24664944 {ECO:0000312|FlyBase:FBgn0036556};
GN ORFNames=CG5830 {ECO:0000312|FlyBase:FBgn0036556};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAQ22453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22453.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:ACJ13154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, INTERACTION WITH BABO; DAH; IRK1; PCH2; RAS64B; SAX
RP AND SRC64B, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 118-ASP--ASP-120.
RX PubMed=31491385; DOI=10.1016/j.cell.2019.08.019;
RA Nil Z., Hervas R., Gerbich T., Leal P., Yu Z., Saraf A., Sardiu M.,
RA Lange J.J., Yi K., Unruh J., Slaughter B., Si K.;
RT "Amyloid-like Assembly Activates a Phosphatase in the Developing Drosophila
RT Embryo.";
RL Cell 178:1403-1420.E21(2019).
CC -!- FUNCTION: Prion-like membrane-associated phosphatase (PubMed:31491385).
CC Phosphatase activity depends on amyloid-like assembly at the membrane
CC (PubMed:31491385). Might have a role in establishment of segment
CC polarity in embryos (PubMed:31491385). {ECO:0000269|PubMed:31491385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:31491385};
CC -!- ACTIVITY REGULATION: Phosphatase activity requires amyloid-like
CC aggregation on the membrane. {ECO:0000269|PubMed:31491385}.
CC -!- SUBUNIT: Monomer (PubMed:31491385). Forms higher-order protein
CC aggregates with amyloid-like features during gastrulation
CC (PubMed:31491385). Interacts with babo, dah, Irk1, pch2, Ras64B, sax
CC and Src64B (PubMed:31491385). {ECO:0000269|PubMed:31491385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31491385};
CC Peripheral membrane protein {ECO:0000269|PubMed:31491385}. Note=During
CC embryonic development shows diffuse localization between stages 1-5 and
CC then shows foci formation at the cell membrane that persist till later
CC stages. {ECO:0000269|PubMed:31491385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0036556};
CC IsoId=M9PFN0-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0036556};
CC IsoId=M9PFN0-2; Sequence=VSP_060469;
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout embryonic
CC development (at protein level). {ECO:0000269|PubMed:31491385}.
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DR EMBL; AE014296; AGB94605.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49553.2; -; Genomic_DNA.
DR EMBL; BT009984; AAQ22453.1; -; mRNA.
DR EMBL; BT050447; ACJ13154.1; -; mRNA.
DR RefSeq; NP_001261912.1; NM_001274983.2. [M9PFN0-1]
DR RefSeq; NP_648825.1; NM_140568.3. [M9PFN0-2]
DR AlphaFoldDB; M9PFN0; -.
DR SMR; M9PFN0; -.
DR IntAct; M9PFN0; 14.
DR STRING; 7227.FBpp0305756; -.
DR PaxDb; M9PFN0; -.
DR PRIDE; M9PFN0; -.
DR DNASU; 39748; -.
DR EnsemblMetazoa; FBtr0075521; FBpp0075276; FBgn0036556. [M9PFN0-2]
DR EnsemblMetazoa; FBtr0333579; FBpp0305756; FBgn0036556. [M9PFN0-1]
DR GeneID; 39748; -.
DR KEGG; dme:Dmel_CG5830; -.
DR UCSC; CG5830-RA; d. melanogaster.
DR CTD; 39748; -.
DR FlyBase; FBgn0036556; hzg.
DR VEuPathDB; VectorBase:FBgn0036556; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_4_0_1; -.
DR OMA; CLCHDES; -.
DR OrthoDB; 1176152at2759; -.
DR BioGRID-ORCS; 39748; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39748; -.
DR PRO; PR:M9PFN0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036556; Expressed in adult Malpighian tubule (Drosophila) and 25 other tissues.
DR ExpressionAtlas; M9PFN0; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IMP:FlyBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:FlyBase.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISS:FlyBase.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Hydrolase; Membrane;
KW Reference proteome.
FT CHAIN 1..352
FT /note="Phosphatase Herzog"
FT /id="PRO_0000448931"
FT DOMAIN 108..266
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..102
FT /note="Prion-like domain necessary for both protein
FT assembly and membrane targeting"
FT /evidence="ECO:0000269|PubMed:31491385"
FT REGION 103..267
FT /note="Mediates substrate recognition"
FT /evidence="ECO:0000269|PubMed:31491385"
FT REGION 284..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 29..51
FT /note="Missing (in isoform A)"
FT /id="VSP_060469"
FT MUTAGEN 118..120
FT /note="DLD->ELN: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:31491385"
FT CONFLICT 11
FT /note="S -> F (in Ref. 3; AAQ22453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40326 MW; 4A2E9BB01C3F948F CRC64;
MDATSIITQV SRDDEQLNVY PSYPNDKDAW LGFSGSVWLP DCPADHAQLT HDVDRLKPQK
RGLFHSLLCC WRRNRTKTNQ NGTQIDGSTT PPPLPDQQRY LLPQVRLTDM HRKCMVIDLD
ETLVHSSFKP IPNADFIVPV EIDGTVHQVY VLKRPHVDEF LQKMGELYEC VLFTASLAKY
ADPVADLLDK WNVFRARLFR ESCVYYRGNY IKDLNRLGRD LQKIVIVDNS PASYIFHPDN
AVPVKSWFDD VTDCELRELI PLFEKLSKVD SVYSVLCNSN QPLNNQTNQQ QHPQELQQAP
NQLHQQLQQQ QQQQTISATT VITQATTLSA PTMLNQQQTS PPSPQSELLQ KT
