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4.D.1.1.12
Chitin synthase 3, Chs3, of 1165 aas and 6 TMSs. Chitin biosynthesis in yeast is accomplished by three chitin synthases (Chs) termed Chs1, Chs2 and Chs3, the last which accounts for most of the chitin deposited within the cell wall. While the overall structures of Chs1 and Chs2 are similar to those of other chitin synthases from fungi and arthropods, Chs3 lacks some of the C-terminal transmembrane helices raising questions regarding its structure and topology. Gohlke et al. 2017 determined aspects of the catalytic domain, the chitin-translocating channel and the interfacial helices in between. They identified an amphipathic, crescent-shaped alpha-helix attached to the inner side of the membrane that may control the channel entrance and a finger helix pushing the polymer into the channel. Chitin synthases form oligomeric complexes, which may be necessary for the formation of chitin nanofibrils. They detected oligomeric complexes at the bud neck, the lateral plasma membrane, and in membranes of Golgi vesicles (Gohlke et al. 2017). The combined action of two independent but redundant endocytic recycling mechanisms, together with distinct labels for vacuolar degradation, determines the final fate of the intracellular traffic of the Chs3 protein, allowing yeast cells to regulate morphogenesis, depending on environmental constraints (Arcones et al. 2016).

Accession Number:P29465
Protein Name:Chitin synthase 3
Length:1165
Molecular Weight:131601.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate chitin

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FASTA formatted sequence
1:	MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN NPDNPHFYYA 
61:	QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF SGRETDSYLL QDMNTTDKKA 
121:	SVKISDEGVA EDEFDKDGDV DNFEESSTQP INKSIKPLRK ETNDTLSFWQ MYCYFITFWA 
181:	PAPILAFCGM PKKERQMAWR EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV 
241:	STEFVVINGK AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP 
301:	KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR DAFYGLKSKA 
361:	DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP VVFDDLKTSN LQGYDLSLVL 
421:	SNGHERKIAR CLSEIIKVGE VDSKTVGCIA SDVVLYVSLV FILSVVIIKF IIACYFRWTV 
481:	ARKQGAYIVD NKTMDKHTND IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD 
541:	LLKKHSSKMF QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS 
601:	TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP LIHTICFVTC 
661:	YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN DKTTPEIALG MMDDFVTPPD 
721:	EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD DSTIPPENQQ RVPIITIVKC GTPAEQGAAK 
781:	PGNRGKRDSQ IILMSFLEKI TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV 
841:	FPDALTHMVA EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV 
901:	TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL LGEDRFLSSL 
961:	MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST VHNLFELVLI RDLCGTFCFS 
1021:	MQFVIGIELI GTMVLPLAIC FTIYVIIFAI VSKPTPVITL VLLAIILGLP GLIVVITATR 
1081:	WSYLWWMCVY ICALPIWNFV LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI 
1141:	KMRTWREFER EDILNRKEES DSFVA