CHS2_CAEEL
ID CHS2_CAEEL Reviewed; 1668 AA.
AC G5EBQ8; A0A0K3ATY7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Chitin synthase chs-2 {ECO:0000305};
DE EC=2.4.1.16 {ECO:0000305|PubMed:16098962};
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase chs-2 {ECO:0000305};
GN Name=chs-2 {ECO:0000303|PubMed:16098962, ECO:0000312|WormBase:F48A11.1a};
GN ORFNames=F48A11.1 {ECO:0000312|WormBase:F48A11.1a};
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:AAX62733.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAX62733.1};
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 DISRUPTION PHENOTYPE.
RX PubMed=15777697; DOI=10.1016/j.gene.2004.11.045;
RA Fanelli E., Di Vito M., Jones J.T., De Giorgi C.;
RT "Analysis of chitin synthase function in a plant parasitic nematode,
RT Meloidogyne artiellia, using RNAi.";
RL Gene 349:87-95(2005).
CC -!- FUNCTION: May be involved in chitin synthesis in the pharynx during
CC larval development. {ECO:0000269|PubMed:16098962}.
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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16098962};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F48A11.1a};
CC IsoId=G5EBQ8-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F48A11.1b};
CC IsoId=G5EBQ8-2; Sequence=VSP_059315;
CC -!- DEVELOPMENTAL STAGE: Specifically expressed just prior to each larval
CC molt (PubMed:11589574). Expression is restricted to the pharynx and
CC specifically to the glandular cells g1 and g2 in the terminal bulb, the
CC 3 m4 myo-epithelial cells in the metacorpus and the 3 m3 myo-epithelial
CC cells in the procorpus (PubMed:16098962, PubMed:11589574). Not
CC expressed in adults (PubMed:11589574). {ECO:0000269|PubMed:11589574,
CC ECO:0000269|PubMed:16098962}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a severe delay in
CC larval development with most animals arrested at the L1 larval stage
CC (PubMed:16098962, PubMed:15777697). Arrested larvae have a disorganized
CC and larger pharynx grinder probably causing feeding defects and thus a
CC delayed growth (PubMed:16098962). {ECO:0000269|PubMed:15777697,
CC ECO:0000269|PubMed:16098962}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; AY874872; AAX62733.1; -; mRNA.
DR EMBL; BX284602; CCD71483.1; -; Genomic_DNA.
DR EMBL; BX284602; CTQ86483.1; -; Genomic_DNA.
DR PIR; T32452; T32452.
DR RefSeq; NP_001300544.1; NM_001313615.1. [G5EBQ8-2]
DR RefSeq; NP_493682.2; NM_061281.5. [G5EBQ8-1]
DR AlphaFoldDB; G5EBQ8; -.
DR STRING; 6239.F48A11.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EPD; G5EBQ8; -.
DR PaxDb; G5EBQ8; -.
DR EnsemblMetazoa; F48A11.1a.1; F48A11.1a.1; WBGene00000497. [G5EBQ8-1]
DR EnsemblMetazoa; F48A11.1b.1; F48A11.1b.1; WBGene00000497. [G5EBQ8-2]
DR GeneID; 173405; -.
DR CTD; 173405; -.
DR WormBase; F48A11.1a; CE39155; WBGene00000497; chs-2. [G5EBQ8-1]
DR WormBase; F48A11.1b; CE50690; WBGene00000497; chs-2. [G5EBQ8-2]
DR eggNOG; KOG2571; Eukaryota.
DR GeneTree; ENSGT00530000064569; -.
DR HOGENOM; CLU_004002_0_0_1; -.
DR InParanoid; G5EBQ8; -.
DR OrthoDB; 124503at2759; -.
DR PhylomeDB; G5EBQ8; -.
DR PRO; PR:G5EBQ8; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000497; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EBQ8; baseline and differential.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; ISS:WormBase.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006031; P:chitin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; Coiled coil; Developmental protein;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1668
FT /note="Chitin synthase chs-2"
FT /id="PRO_0000443249"
FT TOPO_DOM 1..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..176
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..301
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..487
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..576
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..1045
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1067..1074
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1122..1136
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1159..1179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1180..1375
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1376..1396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1397..1440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1441..1461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1462..1668
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1280..1335
FT /evidence="ECO:0000255"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 2..86
FT /note="MNTLDHRPLGRMETMEGKPDEDEVPTSSNSDAKGKGYYYSSGTVPTDDSTLE
FT EKCQQKTFDPSCPTPKTPVIVPNREFDPNFSTV -> DRTMDRRDRDDNHSNYYIAEGT
FT V (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059315"
SQ SEQUENCE 1668 AA; 190185 MW; 0E06C8E0716AE536 CRC64;
MMNTLDHRPL GRMETMEGKP DEDEVPTSSN SDAKGKGYYY SSGTVPTDDS TLEEKCQQKT
FDPSCPTPKT PVIVPNREFD PNFSTVTENK GWDIFRLLPP KPDRLGHGFW HDASLQVLKL
ATFLVLFLLT LGSAVVAKST FILMTSAIGW GGQTITICNQ VISEATQNTV KLKNAHVVKW
VWATLLALSA PEALCFVRSM HRTMFRNVKR PTFIQFVFVL IIETFHSIGV GILVFRIFPD
LDAVTAAQLT NAMCFVPAIL SVISRKPNKS ALLLVIIDFA AIAAQSSGFW ALPMFLPNLQ
KHLVAIPVSL TLISLAWWQN FVHRDSVFPP VRTLAKFAQR LSERRSKTYA FVSLWKICIY
VVCCFLFISS RMKIEDMLQK DPFGEKLLSV AGHDMNQTQI EKFQLRINQM IEQANREAGF
YAAAEKKKQP PKKQPKADEA EQVDAGEYMM KRFKRFIGDA GENEEEEPEE EEFSSYNIYS
NYVERNQLTM AYDALWLVIF QFGAVFVCYH SSKFACKVMM QRMGFALPMA LSVPVTVLLL
STNCRMRQKD SCYGTNVLTV ELFWQCNGAS MSLADFILTP QTWIWLCWLA SQFWITIHLW
NPKHERLAKS EKLFILPYYI GAFVDQSLAF NRRRDDKAKI KAEDLEFDAE DSSLTYETIP
GLQNKTPPSV CSASSSKLEN GLIRDSASSA DAITKIYACA TMWHETGVEM TCMLKSLFRM
DEDQCARRNA QKYLKVIDPD YYEFEAHIFF DDAYDVNEYG EPEINKFVKQ IVNVIDQAAS
AVHQTQMRLK PPKKAKTPYG GKLTYIMPGK NKLFIHLKDN QKIRHRKRWS QVMYLYYLLG
YRLMMKVDDP SRKEIISENT FILTLDGDVD FTPSSVYLLV DLMKKNRRLG AACGRIHPRG
DGAMVWYQKF EYAIGHWLQK ATEHMIGCVM CSPGCFSLFR AYALMDDNVA RRYALKSEEP
KHFIQYDQGE DRWLCTLLLQ RGYRVEYCAA SDAQTFAPEG FNEFFNQRRR WIPSTIFNIM
DLLKDYRNVV RVNESISIWY IIYQLVMLIS SILGPGTIFV MIIGAISISF SIDTLISLVI
VSIPVVVFIV VCLTAKPEHQ LICAQTIGAI FAMLMTAVVV GTSLQLQKDG LLSPHSMFTV
AVATSFLTAA ILHPLEFTCI IPGTIYFLAI PCMYMLLPIY SVCNMHTVSW GTREDPRPTE
KNTLAKKTPG NLESGDGAGN SENWCTRFLC CGRGTVHPMT MVINEKLNEV IKKVDRLDRK
HHPSLARRAS ILSSTGGTIQ IDKCSEADED EQAEIEDALE MSNQSHAAKK NQKWKQAQSE
AWLADKALKR AEREYLEPEE ESFWNDVIER YLSPLIMDGK DMDRLRAGLI AIRNSHTVYF
LMINIVFIIS VLVLQIHKDC LNIEWPLGPK FNHTVRPCYA NHDDNQKEEV WVMTRLQLEP
IGLVFLIFFV SILVIQFLAM LCHRFGTLAH IIASTELFCF RKTMDRLSED ELVAQNAVEI
ARELQAIRGI DENAHNIDNP TEDRGISRRR VVQNLESSRK SMMKRKTETL DAAFKKRFFA
LSSEQTPDPA GFSARDNSKR LTLRKGTIRA LEHRRDSLFG TLDNRKDDEV DATSMRGPAQ
RRLERLFTAQ QDQNSPTSDG NRRKSNSRPW DQPTSSATSS GDVELRRF
