CHS1_CAEEL
ID CHS1_CAEEL Reviewed; 1322 AA.
AC G5ECD6;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Chitin synthase chs-1 {ECO:0000305};
DE EC=2.4.1.16 {ECO:0000305|PubMed:16098962, ECO:0000305|PubMed:20971008};
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase chs-1 {ECO:0000305};
GN Name=chs-1 {ECO:0000303|PubMed:16098962, ECO:0000312|WormBase:T25G3.2};
GN ORFNames=T25G3.2 {ECO:0000312|WormBase:T25G3.2};
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|EMBL:AAX62732.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAX62732.1};
RX PubMed=16098962; DOI=10.1016/j.ydbio.2005.06.037;
RA Zhang Y., Foster J.M., Nelson L.S., Ma D., Carlow C.K.;
RT "The chitin synthase genes chs-1 and chs-2 are essential for C. elegans
RT development and responsible for chitin deposition in the eggshell and
RT pharynx, respectively.";
RL Dev. Biol. 285:330-339(2005).
RN [2] {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 [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=11589574; DOI=10.1007/s004380100513;
RA Veronico P., Gray L.J., Jones J.T., Bazzicalupo P., Arbucci S.,
RA Cortese M.R., Di Vito M., De Giorgi C.;
RT "Nematode chitin synthases: gene structure, expression and function in
RT Caenorhabditis elegans and the plant parasitic nematode Meloidogyne
RT artiellia.";
RL Mol. Genet. Genomics 266:28-34(2001).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17869112; DOI=10.1016/j.cub.2007.08.011;
RA Maruyama R., Velarde N.V., Klancer R., Gordon S., Kadandale P., Parry J.M.,
RA Hang J.S., Rubin J., Stewart-Michaelis A., Schweinsberg P., Grant B.D.,
RA Piano F., Sugimoto A., Singson A.;
RT "EGG-3 regulates cell-surface and cortex rearrangements during egg
RT activation in Caenorhabditis elegans.";
RL Curr. Biol. 17:1555-1560(2007).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20971008; DOI=10.1016/j.cub.2010.09.059;
RA Johnston W.L., Krizus A., Dennis J.W.;
RT "Eggshell chitin and chitin-interacting proteins prevent polyspermy in C.
RT elegans.";
RL Curr. Biol. 20:1932-1937(2010).
CC -!- FUNCTION: Essential for the embryonic synthesis of chitin, a component
CC of the eggshell. {ECO:0000269|PubMed:16098962,
CC ECO:0000269|PubMed:20971008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000305|PubMed:16098962, ECO:0000305|PubMed:20971008};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17869112,
CC ECO:0000269|PubMed:20971008}; Multi-pass membrane protein
CC {ECO:0000255}. Note=egg-1, egg-2 and egg-3 maintain the homogenous
CC distribution of chs-1 at the unfertilized oocyte cell membrane, thus
CC ensuring the formation of a continuous and cohesive eggshell chitin
CC layer (PubMed:20971008, PubMed:17869112). In the fertilized embryo, co-
CC localizes with egg-3 to cytoplasmic foci in an egg-3-dependent manner
CC (PubMed:17869112). {ECO:0000269|PubMed:17869112,
CC ECO:0000269|PubMed:20971008}.
CC -!- DEVELOPMENTAL STAGE: Expressed at L3-L4 larval stages and in adults.
CC {ECO:0000269|PubMed:11589574}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes the production of
CC abnormal eggs characterized by a spherical morphology, the absence of
CC the eggshell chitin layer, increased permeability to small molecules
CC and a failure to divide (PubMed:16098962). Loss of polar body formation
CC and loss of egg-3 and mbk-2 cortical localization in oocytes
CC (PubMed:17869112). RNAi-mediated knockdown causes polyspermy in 40
CC percent of animals and a failure to internalize egg-1 after oocyte
CC fertilization (PubMed:20971008). Simultaneous RNAi-mediated knockdown
CC with mat-1 prevents the formation of the eggshell chitin layer
CC (PubMed:20971008). {ECO:0000269|PubMed:16098962,
CC ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:20971008}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; AY874871; AAX62732.1; -; mRNA.
DR EMBL; BX284601; CAA96688.2; -; Genomic_DNA.
DR PIR; T25284; T25284.
DR RefSeq; NP_492113.2; NM_059712.4.
DR AlphaFoldDB; G5ECD6; -.
DR STRING; 6239.T25G3.2.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EPD; G5ECD6; -.
DR PaxDb; G5ECD6; -.
DR PeptideAtlas; G5ECD6; -.
DR EnsemblMetazoa; T25G3.2.1; T25G3.2.1; WBGene00000496.
DR EnsemblMetazoa; T25G3.2.2; T25G3.2.2; WBGene00000496.
DR GeneID; 172508; -.
DR KEGG; cel:CELE_T25G3.2; -.
DR CTD; 172508; -.
DR WormBase; T25G3.2; CE39183; WBGene00000496; chs-1.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004002_0_0_1; -.
DR InParanoid; G5ECD6; -.
DR OMA; NEMTGQF; -.
DR OrthoDB; 124503at2759; -.
DR PhylomeDB; G5ECD6; -.
DR PRO; PR:G5ECD6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000496; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004100; F:chitin synthase activity; ISS:WormBase.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006031; P:chitin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030703; P:eggshell formation; IMP:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1322
FT /note="Chitin synthase chs-1"
FT /id="PRO_0000443248"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..156
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..316
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..396
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 858..865
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..892
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..922
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..1148
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1149..1169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1170..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1210..1230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1231..1322
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT COILED 455..486
FT /evidence="ECO:0000255"
FT COILED 1019..1053
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1322 AA; 151056 MW; 2E1D50AFE5527459 CRC64;
MNDGENYWNA FRSHKRSATD GPTLSPWMVT VLQATKLLLF ALCNIVLTLG SVFSKLIVLI
MATNIVPRAH LIGKFARKCT KAAVRRTSTT TAGIYLSLLL IQCFPDTINL IRSGIDMWKG
QCGQLVKSVV VLESLRAIGL AVLSFHVFPQ LDLARCLVLS ACFPLVAVLQ RSLVAMVSAA
RTGRSFRNRL GRCFVAIPHV IMFLVLMSSC YVWALFDNKF TAIIALPIGV ICTSAGFWES
WIDTTHSGTS FDELYRLKYA VRKMNTTTKL IVSLMRIVCT VSVLVSAVYI NDHKKLNSSH
FVKAFFSFST RQPHTRLLLL ATGIIVLHFV MRGISRFLAA LDLHPFSFVH PLSIAPLIAY
GYVRYACQSP TCSIARRLAR FGLHWVCDQW FQSARGIASP DFYICLIWLL VGCYRGWRLV
RQRYFDTNEE IISSMPPVCN GLCIEQSLVV FQHSLNRQEK TMLTEEEDIS DENDELRIRN
DEVDRVSTVY GCATMWHETE TEMRQVLRSI LKLDVDHATR MNNKKANELR YRLEGHIFFD
DAWEDVEEDG IEKRQPNEYF NMFFDLLNEM TGERLNEEGK METRILVNTP YGGRLVVKLP
SGTLLFVHLK DKKMIRHKKR WSQVMYMYYL LGHRIMDCPL SIEDRQQMAD NTFILAIDGD
SKFEPDALLR LLHLMNAKSD IGCACGRIHP IGNGIMVWYQ KFEYAIAHWF QKAAEHVFGC
VLCAPGCFSL FRASALMDDN IMHKYTKTAS EPRHYVQYDQ GEDRWLSTLL LKQGYRIEYA
AASDAETYAP EGFEEFFNQR RRWTPSSIAN TVDLLMDYKR ASENNDAISY AYIAYQFLVI
FFSMLGPAII FTMLVFAQVA AFELRGSDVM LYNGIPIGFF IVLCFTTESN IQLIYAKYMS
IAYAFVMLAV LVATSSQIVL ETVLAPTSLF IVTMVGIFFF AACLHPKEFT NIIHGVVFFL
MIPSTYVFLT LYSLINLNVI TWGTREAVAK ATGQKTKKAP MEQFIDRVID IVKKGFRLIS
CREKKEHEER REKMEKKMQR MELALRSIES GADVKKILDA TEEKEKREEE TQTADFPIEE
NVEKTQKEIQ KANRYVWMTS HSLKVCERGK LKSAEKVFWN ELINAYLKPI KTTPAEMKAV
AEGLASLRNQ IAFTILLVNS LLALAIFLIQ KHKNVLSIKF SPIKNFRWTK MNEMTGQYEE
TDEPLKIDPL GMGIVVFLLI ILFVQTLGML LHRLNTMIGA FQEVKNLYEY GVSPVINTKN
DDERIMNNAR LMINSLGVST GHAADGYTRH RGEESDTGNV LYKLQKARLA KRMQRSALST
TE
