CHS3/YBR023C Protein Information

Standard Name	Chs3p 1
Systematic Name	Ybr023cp
Alias	Cal1p 2 , Csd2p , Dit101p , Kti2p 3
ORF Classification	Verified
Description	Chitin synthase III, catalyzes the transfer of N-acetylglucosamine (GlcNAc) to chitin; required for synthesis of the majority of cell wall chitin, the chitin ring during bud emergence, and spore wall chitosan (4, 5, 6, 7)
Name Description	CHitin Synthase-related 7

Experimental Data
Molecules/cell	1510 8

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,165
Molecular Weight (Da)	131,600
Isoelectric Point (pI)	6.68

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Chs3p (InterPro)
Transmembrane Domains	There are 6 total predicted transmembrane domains (TMHMM)
Physical Interactions	There are 38 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000127918 \| P29465 MIPS: YBR023C NCBI: 172104 \| 3360 \| 498752 \| 536230 \| 584947 \| 6319497 \| NP_009579.1 GenBank/EMBL/DDBJ: DAA07145.1 \| M73697 \| X57300 \| X76078 \| Z35892
External Classifications	EC: 2.4.1.16 [Chitin synthase]

Amino Acid Sequence (or in FASTA format)
1 MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN 51 NPDNPHFYYA QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF 101 SGRETDSYLL QDMNTTDKKA SVKISDEGVA EDEFDKDGDV DNFEESSTQP 151 INKSIKPLRK ETNDTLSFWQ MYCYFITFWA PAPILAFCGM PKKERQMAWR 201 EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV STEFVVINGK 251 AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP 301 KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR 351 DAFYGLKSKA DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP 401 VVFDDLKTSN LQGYDLSLVL SNGHERKIAR CLSEIIKVGE VDSKTVGCIA 451 SDVVLYVSLV FILSVVIIKF IIACYFRWTV ARKQGAYIVD NKTMDKHTND 501 IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD LLKKHSSKMF 551 QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS 601 TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP 651 LIHTICFVTC YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN 701 DKTTPEIALG MMDDFVTPPD EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD 751 DSTIPPENQQ RVPIITIVKC GTPAEQGAAK PGNRGKRDSQ IILMSFLEKI 801 TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV FPDALTHMVA 851 EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV 901 TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL 951 LGEDRFLSSL MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST 1001 VHNLFELVLI RDLCGTFCFS MQFVIGIELI GTMVLPLAIC FTIYVIIFAI 1051 VSKPTPVITL VLLAIILGLP GLIVVITATR WSYLWWMCVY ICALPIWNFV 1101 LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI KMRTWREFER 1151 EDILNRKEES DSFVA*

Amino Acid Sequence (or in FASTA format)

       1  MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN
      51  NPDNPHFYYA QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF
     101  SGRETDSYLL QDMNTTDKKA SVKISDEGVA EDEFDKDGDV DNFEESSTQP
     151  INKSIKPLRK ETNDTLSFWQ MYCYFITFWA PAPILAFCGM PKKERQMAWR
     201  EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV STEFVVINGK
     251  AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP
     301  KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR
     351  DAFYGLKSKA DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP
     401  VVFDDLKTSN LQGYDLSLVL SNGHERKIAR CLSEIIKVGE VDSKTVGCIA
     451  SDVVLYVSLV FILSVVIIKF IIACYFRWTV ARKQGAYIVD NKTMDKHTND
     501  IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD LLKKHSSKMF
     551  QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS
     601  TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP
     651  LIHTICFVTC YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN
     701  DKTTPEIALG MMDDFVTPPD EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD
     751  DSTIPPENQQ RVPIITIVKC GTPAEQGAAK PGNRGKRDSQ IILMSFLEKI
     801  TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV FPDALTHMVA
     851  EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV
     901  TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL
     951  LGEDRFLSSL MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST
    1001  VHNLFELVLI RDLCGTFCFS MQFVIGIELI GTMVLPLAIC FTIYVIIFAI
    1051  VSKPTPVITL VLLAIILGLP GLIVVITATR WSYLWWMCVY ICALPIWNFV
    1101  LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI KMRTWREFER
    1151  EDILNRKEES DSFVA*

external links for Chs3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Chs3p

1)	Breitenbach, M. (1992) Personal Communication, Mortimer Map Edition 11
2)	Takita MA and Castilho-Valavicius B (1993) Absence of cell wall chitin in Saccharomyces cerevisiae leads to resistance to Kluyveromyces lactis killer toxin. Yeast 9(6):589-98
3)	Butler AR, et al. (1991) Intracellular expression of Kluyveromyces lactis toxin gamma subunit mimics treatment with exogenous toxin and distinguishes two classes of toxin-resistant mutant. Yeast 7(6):617-25
4)	Ziman M, et al. (1996) Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway. Mol Biol Cell 7(12):1909-19
5)	Shaw JA, et al. (1991) The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle. J Cell Biol 114(1):111-23
6)	Pammer M, et al. (1992) DIT101 (CSD2, CAL1), a cell cycle-regulated yeast gene required for synthesis of chitin in cell walls and chitosan in spore walls. Yeast 8(12):1089-99
7)	Cid VJ, et al. (1995) Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol Rev 59(3):345-86
8)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41