PYR1_CAEEL
ID PYR1_CAEEL Reviewed; 2198 AA.
AC Q18990;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=CAD protein {ECO:0000250|UniProtKB:P27708};
DE Includes:
DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase {ECO:0000250|UniProtKB:P27708};
DE EC=6.3.5.5 {ECO:0000250|UniProtKB:P27708};
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000250|UniProtKB:P27708};
DE EC=2.1.3.2 {ECO:0000250|UniProtKB:P27708};
DE Includes:
DE RecName: Full=Dihydroorotase {ECO:0000250|UniProtKB:P27708};
DE EC=3.5.2.3 {ECO:0000250|UniProtKB:P27708};
GN Name=pyr-1 {ECO:0000303|PubMed:16828468, ECO:0000312|WormBase:D2085.1};
GN ORFNames=D2085.1 {ECO:0000312|WormBase:D2085.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-1602.
RX PubMed=16828468; DOI=10.1016/j.ydbio.2006.06.008;
RA Franks D.M., Izumikawa T., Kitagawa H., Sugahara K., Okkema P.G.;
RT "C. elegans pharyngeal morphogenesis requires both de novo synthesis of
RT pyrimidines and synthesis of heparan sulfate proteoglycans.";
RL Dev. Biol. 296:409-420(2006).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-1602.
RX PubMed=20148972; DOI=10.1111/j.1742-4658.2010.07573.x;
RA Levitte S., Salesky R., King B., Coe Smith S., Depper M., Cole M.,
RA Hermann G.J.;
RT "A Caenorhabditis elegans model of orotic aciduria reveals enlarged
RT lysosome-related organelles in embryos lacking umps-1 function.";
RL FEBS J. 277:1420-1439(2010).
RN [4]
RP MUTAGENESIS OF HIS-1602.
RX PubMed=30102152; DOI=10.7554/elife.36588;
RA Liu Y., Zou W., Yang P., Wang L., Ma Y., Zhang H., Wang X.;
RT "Autophagy-dependent ribosomal RNA degradation is essential for maintaining
RT nucleotide homeostasis during C. elegans development.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: This protein is a 'fusion' protein encoding four enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, ATCase and
CC DHOase) (By similarity). Involved in the elongation of the pharyngeal
CC isthmus during development, probably by providing precursors of UDP-
CC sugars required for heparan sulfate proteoglycan biosynthesis
CC (PubMed:16828468). Regulates the organization of the actin and
CC intermediate filaments cytoskeleton in the pharyngeal muscles
CC (PubMed:16828468). {ECO:0000250|UniProtKB:P27708,
CC ECO:0000269|PubMed:16828468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000250|UniProtKB:P27708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC Evidence={ECO:0000250|UniProtKB:P27708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000250|UniProtKB:P27708};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P27708};
CC Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity).
CC {ECO:0000250|UniProtKB:P27708};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 4 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000250|UniProtKB:P27708}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000250|UniProtKB:P27708}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000250|UniProtKB:P27708}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P27708}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine.
CC {ECO:0000269|PubMed:16828468}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly in gut precursor cells
CC from the 4E embryonic stage until the bean stage. Expression resumes at
CC the L1 larval stage and continues into adulthood.
CC {ECO:0000269|PubMed:16828468}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at the
CC embryonic stage or at the L1 larval stage (PubMed:16828468). The few
CC surviving animals grow more slowly (PubMed:16828468). L1 larvae have
CC incomplete pharyngeal isthmus elongation, 36 percent of which have the
CC pharynx detached from the buccal cavity (PubMed:16828468). In an umps-1
CC zu456 mutant background embryo, prevents the formation of abnormally
CC enlarged gut granules (PubMed:20148972). {ECO:0000269|PubMed:16828468,
CC ECO:0000269|PubMed:20148972}.
CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC (carbamoyl phosphate synthase) form together the glutamine-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5). {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily. {ECO:0000305}.
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DR EMBL; BX284602; CAA91059.2; -; Genomic_DNA.
DR RefSeq; NP_495838.2; NM_063437.4.
DR AlphaFoldDB; Q18990; -.
DR SMR; Q18990; -.
DR STRING; 6239.D2085.1; -.
DR EPD; Q18990; -.
DR PaxDb; Q18990; -.
DR PeptideAtlas; Q18990; -.
DR EnsemblMetazoa; D2085.1.1; D2085.1.1; WBGene00004259.
DR GeneID; 174385; -.
DR KEGG; cel:CELE_D2085.1; -.
DR UCSC; D2085.1; c. elegans.
DR CTD; 174385; -.
DR WormBase; D2085.1; CE41886; WBGene00004259; pyr-1.
DR eggNOG; KOG0370; Eukaryota.
DR GeneTree; ENSGT00940000157241; -.
DR HOGENOM; CLU_000513_2_0_1; -.
DR InParanoid; Q18990; -.
DR OMA; IPCTSML; -.
DR OrthoDB; 273358at2759; -.
DR PhylomeDB; Q18990; -.
DR Reactome; R-CEL-70635; Urea cycle.
DR UniPathway; UPA00070; UER00115.
DR UniPathway; UPA00070; UER00116.
DR UniPathway; UPA00070; UER00117.
DR PRO; PR:Q18990; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004259; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:1905905; P:pharyngeal gland morphogenesis; IMP:UniProtKB.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:WormBase.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1370; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glutamine amidotransferase; Hydrolase; Ligase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..2198
FT /note="CAD protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438771"
FT DOMAIN 180..366
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 516..708
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1054..1245
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1318..1474
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 3..368
FT /note="GATase (Glutamine amidotransferase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 392..1467
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 392..934
FT /note="CPSase A"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 935..1467
FT /note="CPSase B"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1468..1799
FT /note="DHOase (dihydroorotase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1800..1870
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1871..2196
FT /note="ATCase (Aspartate transcarbamylase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT ACT_SITE 255
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 339
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 341
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 542..597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 665
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 681
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1080..1137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1487
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1517
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1670
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1695
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1699
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1568
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MUTAGEN 1602
FT /note="H->Q: In cu8; probable loss of dihydroorotase
FT activity. Severe late stage embryonic lethality in 50% of
FT animals. The few surviving mutants have a shorter and
FT thicker pharyngeal isthmus, an abnormal knobbed tail, mild
FT egg-laying defects, moderate fluid accumulation in the
FT coelom and a slower growth. Actin and intermediate
FT filaments are disorganized in the pharynx. Moderate
FT reduction in heparan sulfate levels and increased levels of
FT chondroitin sulfate. In an umps-1 zu456 mutant background,
FT prevents the formation of abnormally enlarged gut granules
FT in embryos. Complete embryonic lethality in a rnst-2 qx245
FT mutant background."
FT /evidence="ECO:0000269|PubMed:16828468,
FT ECO:0000269|PubMed:20148972, ECO:0000269|PubMed:30102152"
SQ SEQUENCE 2198 AA; 242582 MW; 31CFC62E64D21B1E CRC64;
MRATLHLEDG STFVGSIYGA TKSVVGEIVF QTGMVGYVES LTDPSYAKQL LTLTYPLIGN
YGVPSAEILD QFKLPAEFES DRIWPAALIV EKICVDGEHS HWQAVQSLSE WLRKADVPCL
SGIDVRQLVK KIRETGTMKA KLVIESDNAQ NFDYVDVNAE NLVDFVSRKE PVVYGSGDQT
ILAVDCGLKN NQIRCLAKRG FRVKVVPWNH PIDTESDYDG LFLSNGPGDP EICAPLVDRL
AKVIARGDKP IFGICLGHQI LSRAIGAKTY KLKYGNRGHN QPCTHYATGR CYITSQNHGY
AVDPDSLPAD WKALFTNEND KTNEGIVHSS KPFFSVQFHP EHTAGPTDCE FLFDVFADSV
RQAKSGTFMN VDQELTRLMT FTPIYHAKEQ RKVLVLGSGG LTIGQAGEFD YSGAQALKAL
REEGIRTVLI NPNIATVQTS KGFADFTYFL PITKEYVTDV IKKERPTGIL CTFGGQTALN
CAIDLYKDGI FEQYDVQVLG TQINTIMKTE DRDLFNQEIS AIGEKVAPSK AATTMEGAIE
AAEELGYPVL VRAAYALGGL GSGFADNREE LIAIAQQALA HSNQVLVDKS LKGWKEVEYE
VVRDAYDNCI TVCNMENVDP LGIHTGESVV VAPSQTLSDR EYNALRTCAI KVIRHLGIIG
ECNIQYALDP YSLTYYIIEV NARLSRSSAL ASKATGYPLA YVAAKLALGQ HLPVIRNSVT
GTTTACFEPS LDYCVVKIPR WDLGKFARVS TQIGSSMKSV GEVMGIGRCF EEALQKALRM
VSDHADGFSP YTFSRPTTAD DLSKPTDKRM FALARGMYYG DFDVEKAHEL TRIDRWFLFR
MQNIVDIYHR LEKTDVNTVS AELLLEAKQA GFSDRQIAKK IGSNEYTVRE ARFVKGITPC
VKQIDTVAGE WPAQTNYLYT TFNGIENDVS FNMKNAVMVL GSGVYRIGSS VEFDSSCVGC
IRELKALGYS TITVNCNPET VSTDYDICDR LYFEEISFET VLDVYHLEKP KGVILAFGGQ
APNNIAMSLS RAQVKIFGTS PNDIDNAEDR FKFSRKLESL KISQPQWKKS ENMEDAKNFC
AQVGYPCLIR PSYVLSGAAM NVAHNAEDLE VFLKQAAVVA KEHPVVVSKF INEAKELDVD
AVALDGKLVV MAVSEHIENA GVHSGDATLV TPAQDMNKLT LDRIKDITFR IAEAFNVNGP
FNMQLIAKNN ELKVIECNLR VSRSFPFVSK TLDYDFVALA TRAMMASDSP AIRATIKPTA
TLLKGKGRVG VKVPQFSFSR LAGADVMLGV EMASTGEVAC FGTSRCDAYL KALLSTGFVV
PKQNIFISIG GYHAKAEMLK SVEALLKLGY ELYGSKGTAD YFQSNKINVK PVDWPFEEGS
SDEKTASGTR SVVEFLENKE FHLVINLPIR GSGAYRVSAF RTHGYKTRRM AIDNGIPLIT
DIKCAKTFIQ ALEMVGKRPT MNSLVDCVTS KSLKRLPGMV DIHVHVREPG ATHKEDWATC
SKAALAGGVT TILAMPNTSP VLVDTDSFYQ TEQLASAKSV VDYALYIGAT PNNSKFAAEF
ADKAAGLKMY LNETFSTLKM DNISDWAKHL SAFPANRPIV CHAEKQTLAA ILCMAQMANR
AVHIAHVATA DEINLVKEAK QRGWNVTCEV CPHHLFLIEE DLPDGIREVR PRLVKPEDRQ
ALWDNMEYID CFATDHAPHT WAEKTGKDGK IPPGFPGVEY MLPLLLTAVH DGKLTMKELT
DRMSTNPRRI FNLPPQDDTY IEVDLNEEWT IPENGGQSKA GWTPFAGRKV FGKVHNVIIR
GEEAVIDGRI VAIPGFGKNV RLYPHSGTAH RGDSDFDQIL EPIPQQMIES SSDEQSPLHT
PPRAHTPIAF PGELLAKNCI SVKHLDKGQI NRIFELADRY KHDVEKGHPL THILNGKVLV
NLFYEVSTRT SCSFSAAMQR LGGSVISVDS QSSSVQKGET LEDTVQVLGS YGDILVLRSN
ENGAADRAAR VCDQPVINGG DGTGEHPTQA LLDVYTIRQE MGTVNGLTIA LVGDLKNGRT
VHSLAKLLCL YKDITLHYVA PSTELEMPQE VLDYVSSKSN FVQKKFTSLA EGINHVDVVY
VTRIQKERFS SPDEYNKVKG SYVINAKLLN EAARDVEEPS SLLVPARSLP IVMHPLPRVD
EIAVELDHDE RAAYFRQAKN GVFVRMSILS LLLGRGHL
