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Database: UniProt
Entry: CHS1_CAEEL
LinkDB: CHS1_CAEEL
Original site: 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   08-MAY-2019, entry version 67.
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,
GN   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
RP   DISRUPTION 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.
RT   elegans development and responsible for chitin deposition in the
RT   eggshell and 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
RT   investigating 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.,
RA   Parry J.M., Hang J.S., Rubin J., Stewart-Michaelis A.,
RA   Schweinsberg P., Grant B.D., 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
RT   C. elegans.";
RL   Curr. Biol. 20:1932-1937(2010).
CC   -!- FUNCTION: Essential for the embryonic synthesis of chitin, a
CC       component 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-
CC         alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1)
CC         + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593,
CC         Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16;
CC         Evidence={ECO:0000305|PubMed:16098962,
CC         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,
CC       thus ensuring the formation of a continuous and cohesive eggshell
CC       chitin layer (PubMed:20971008, PubMed:17869112). In the fertilized
CC       embryo, co-localizes with egg-3 to cytoplasmic foci in an egg-3-
CC       dependent manner (PubMed:17869112). {ECO:0000269|PubMed:17869112,
CC       ECO:0000269|PubMed:20971008}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at L3-L4 larval stages and in
CC       adults. {ECO:0000269|PubMed:11589574}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes the
CC       production of abnormal eggs characterized by a spherical
CC       morphology, the absence of the eggshell chitin layer, increased
CC       permeability to small molecules and a failure to divide
CC       (PubMed:16098962). Loss of polar body formation and loss of egg-3
CC       and mbk-2 cortical localization in oocytes (PubMed:17869112).
CC       RNAi-mediated knockdown causes polyspermy in 40 percent of animals
CC       and a failure to internalize egg-1 after oocyte fertilization
CC       (PubMed:20971008). Simultaneous RNAi-mediated knockdown with mat-1
CC       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
CC       subfamily. {ECO:0000305}.
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   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   eggNOG; COG1215; LUCA.
DR   InParanoid; G5ECD6; -.
DR   KO; K00698; -.
DR   OMA; HRIMDSH; -.
DR   OrthoDB; 124503at2759; -.
DR   PhylomeDB; G5ECD6; -.
DR   PRO; PR:G5ECD6; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00000496; Expressed in 4 organ(s), highest expression level in germ line (C elegans).
DR   GO; GO:0005938; C:cell cortex; IDA:WormBase.
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; Complete proteome; Glycoprotein;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1322       Chitin synthase chs-1.
FT                                /FTId=PRO_0000443248.
FT   TOPO_DOM      1     39       Extracellular. {ECO:0000305}.
FT   TRANSMEM     40     60       Helical. {ECO:0000255}.
FT   TOPO_DOM     61    128       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    129    149       Helical. {ECO:0000255}.
FT   TOPO_DOM    150    156       Extracellular. {ECO:0000305}.
FT   TRANSMEM    157    177       Helical. {ECO:0000255}.
FT   TOPO_DOM    178    193       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    194    214       Helical. {ECO:0000255}.
FT   TOPO_DOM    215    221       Extracellular. {ECO:0000305}.
FT   TRANSMEM    222    242       Helical. {ECO:0000255}.
FT   TOPO_DOM    243    269       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    270    290       Helical. {ECO:0000255}.
FT   TOPO_DOM    291    316       Extracellular. {ECO:0000305}.
FT   TRANSMEM    317    337       Helical. {ECO:0000255}.
FT   TOPO_DOM    338    342       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    343    363       Helical. {ECO:0000255}.
FT   TOPO_DOM    364    396       Extracellular. {ECO:0000305}.
FT   TRANSMEM    397    417       Helical. {ECO:0000255}.
FT   TOPO_DOM    418    836       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    837    857       Helical. {ECO:0000255}.
FT   TOPO_DOM    858    865       Extracellular. {ECO:0000305}.
FT   TRANSMEM    866    886       Helical. {ECO:0000255}.
FT   TOPO_DOM    887    892       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    893    913       Helical. {ECO:0000255}.
FT   TOPO_DOM    914    922       Extracellular. {ECO:0000305}.
FT   TRANSMEM    923    943       Helical. {ECO:0000255}.
FT   TOPO_DOM    944    951       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    952    972       Helical. {ECO:0000255}.
FT   TOPO_DOM    973   1148       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1149   1169       Helical. {ECO:0000255}.
FT   TOPO_DOM   1170   1209       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1210   1230       Helical. {ECO:0000255}.
FT   TOPO_DOM   1231   1322       Extracellular. {ECO:0000305}.
FT   COILED      455    486       {ECO:0000255}.
FT   COILED     1019   1053       {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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