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Database: UniProt
Entry: A0A1I7VAU2_LOALO
LinkDB: A0A1I7VAU2_LOALO
Original site: A0A1I7VAU2_LOALO 
ID   A0A1I7VAU2_LOALO        Unreviewed;       608 AA.
AC   A0A1I7VAU2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
OS   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_11741};
RN   [1] {ECO:0000313|Proteomes:UP000095285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Loa loa.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:EN70_11741}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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:0000256|ARBA:ARBA00000319};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; A0A1I7VAU2; -.
DR   STRING; 7209.A0A1I7VAU2; -.
DR   WBParaSite; EN70_11741; EN70_11741; EN70_11741.
DR   eggNOG; KOG2571; Eukaryota.
DR   Proteomes; UP000095285; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd04190; Chitin_synth_C; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF12; CHITIN SYNTHASE CHS-1; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        373..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        464..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   608 AA;  69997 MW;  3F44E7CD2886E617 CRC64;
     MDGDNRSSEG AEVDVGDLRV TNDESDKTMT LYICATMWHE TRIEMMQMLK SIIKLDKEHS
     ITLIERRHWD DIKYRLEAHI FFDDVWEDQM ECGRAPNGFF QTFFHLLLEL TQNETTGEKS
     VATDRVLVNT AYGGRLVVRL PAGTLLFVHL KDKQLVRHKK RWSQVMYLYY LLGHRIMDSH
     MSIEDRQLEA DNTYILAIDG DSKFEPSAVM KLLRLMNMKN EIGCACGRIH PIGEGIMIWY
     QKFEYAISHW FQKATEHVFG CVLCAPGCFS LFRASALMDD NVMHKYTKTA SEPRHFVQYD
     QGEDRWLSTL LLKQGYRIEY AAVADAETYA PEGFHEFFNQ RRRWTPSSIA NTVDLLADYK
     HVCQTNNSIS KMYIIYQSMM IGFSLLSPSI VFTMLVYAQV ATFEVESDKM LLYNSLPVFI
     FIVLCFIADS NYQIIFAKFI SVMYGFVMLA VAVATTNQII LERLIFFLMI PCTYIFMSLY
     ALINLNIINW GTREAAFTTA GTHASDTGFR DLLRRLGLYK IIDFVRSPPS WNSTITTTAI
     TATAAAVEVQ EIKRKERNNS SSVHFDTTTT GHAHLHFLSA PQVLLDNQKE QDKVNDFVFF
     LIDDHLVA
//
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