EXT1_CAEEL
ID EXT1_CAEEL Reviewed; 382 AA.
AC O01704; A4F1W7; Q9U3J6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Exostosin-1 homolog {ECO:0000305};
DE AltName: Full=Multiple exostoses homolog 1;
DE AltName: Full=Related to mammalian RIB protein 1;
DE Flags: Precursor;
GN Name=rib-1; ORFNames=F12F6.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RIB-2.
RX PubMed=17237233; DOI=10.1074/jbc.m611107200;
RA Kitagawa H., Izumikawa T., Mizuguchi S., Dejima K., Nomura K.H., Egusa N.,
RA Taniguchi F., Tamura J., Gengyo-Ando K., Mitani S., Nomura K., Sugahara K.;
RT "Expression of rib-1, a Caenorhabditis elegans homolog of the human tumor
RT suppressor EXT genes, is indispensable for heparan sulfate synthesis and
RT embryonic morphogenesis.";
RL J. Biol. Chem. 282:8533-8544(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-382.
RX PubMed=9110175; DOI=10.1101/gr.7.4.359;
RA Clines G.A., Ashley J.A., Shah S., Lovett M.;
RT "The structure of the human multiple exostoses 2 gene and characterization
RT of homologs in mouse and Caenorhabditis elegans.";
RL Genome Res. 7:359-367(1997).
RN [4]
RP FUNCTION.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24052309; DOI=10.1126/science.1242528;
RA Pedersen M.E., Snieckute G., Kagias K., Nehammer C., Multhaupt H.A.,
RA Couchman J.R., Pocock R.;
RT "An epidermal microRNA regulates neuronal migration through control of the
RT cellular glycosylation state.";
RL Science 341:1404-1408(2013).
CC -!- FUNCTION: Required for the biosynthesis of heparan sulfate by
CC positively regulating N-acetylglucosamine transferase II (GlcNAcT-II)
CC and glucuronyl transferase II (GlcAT-II) activities of
CC glycosyltransferase rib-2 (PubMed:17237233). Probably not directly
CC involved in chondroitin sulfate biosynthesis but negatively regulates
CC chondroitin sulfate levels (PubMed:16828468, PubMed:17237233).
CC Maternally required for normal ventral epidermal enclosure and for
CC embryo elongation during the early stages of embryonic development
CC (PubMed:17237233). In addition, involved in the elongation of the
CC pharyngeal isthmus and in the organization of the actin cytoskeleton in
CC the pharyngeal muscles during the later stages embryonic development
CC (PubMed:16828468). In adults, regulates egg-laying and the normal
CC morphogenesis of the vulva (PubMed:17237233). Also involved in the
CC directed migration of hermaphrodite-specific neurons (PubMed:17237233,
CC PubMed:24052309). {ECO:0000269|PubMed:16828468,
CC ECO:0000269|PubMed:17237233, ECO:0000269|PubMed:24052309}.
CC -!- SUBUNIT: Interacts with rib-2. {ECO:0000269|PubMed:17237233}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Golgi
CC apparatus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the failure of
CC hermaphrodite-specific neurons to migrate to their correct position
CC associated with a defect in axonal guidance.
CC {ECO:0000269|PubMed:24052309}.
CC -!- MISCELLANEOUS: Does not display any N-acetylglucosamine transferase II
CC (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities when
CC expressed alone in vitro. {ECO:0000269|PubMed:17237233}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; AB241458; BAF48989.1; -; mRNA.
DR EMBL; Z73425; CAB61014.1; -; Genomic_DNA.
DR EMBL; U94834; AAC47509.1; -; mRNA.
DR RefSeq; NP_502180.1; NM_069779.4.
DR AlphaFoldDB; O01704; -.
DR SMR; O01704; -.
DR BioGRID; 43177; 1.
DR STRING; 6239.F12F6.3.2; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR EPD; O01704; -.
DR PaxDb; O01704; -.
DR PRIDE; O01704; -.
DR EnsemblMetazoa; F12F6.3a.1; F12F6.3a.1; WBGene00004360.
DR GeneID; 178080; -.
DR KEGG; cel:CELE_F12F6.3; -.
DR UCSC; F12F6.3.2; c. elegans.
DR CTD; 178080; -.
DR WormBase; F12F6.3a; CE24898; WBGene00004360; rib-1.
DR eggNOG; KOG1021; Eukaryota.
DR GeneTree; ENSGT00940000163960; -.
DR HOGENOM; CLU_013906_5_1_1; -.
DR InParanoid; O01704; -.
DR OMA; IFNFYHG; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; O01704; -.
DR PRO; PR:O01704; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004360; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O01704; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:WormBase.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:WormBase.
DR GO; GO:0060465; P:pharynx development; IMP:WormBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..382
FT /note="Exostosin-1 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000149662"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 382 AA; 44926 MW; 6840F03355CC7F49 CRC64;
MQNVMKFHLV IFMLFGSVRL QNPTIERKQC TMSNCFDFSK CSTSKKVYIH PMEKRFEESP
QSVIYSKILK HFLESNHYTN DPNEACIFLL GIDTTDRDVR SQNYVKNVND YIESLDPSVW
NNGRNHLIFN FYHGTFPDYD DHNLNFDTGE AMIARASSSE NNFIKVFDVS LPLFHENHPY
EIKESKSERN DDRIENQRKY LVSFKGKRYV YGIGSGTRNL VHHLHNGDDI VMVTTCKHNN
DWQVYQDDRC QRDNDEYDRW EYDELLANST FCLVPRGRRL GSFRFLETLR SGCVPVVISD
SWILPFSETI DWNSAAIVVA ERDALSIPEL LMSTSRRRVK ELRESARNVY DAYLRSIQVI
SDHVLRIIFK RIDNKIELED HQ
