Reviewed, UniProtKB/Swiss-Prot Q99126 (CHS3_USTMA)

Names and origin

Protein names

Recommended name:
    Chitin synthase 3
    EC=2.4.1.16
Alternative name(s):
    Chitin-UDP acetyl-glucosaminyl transferase 3
    Chitin synthase I

Gene names

Name:	CHS3
Synonyms:	CHS1
ORF Names:	UM10120, UM00474

Organism

Ustilago maydis (Smut fungus) [Complete proteome]

Taxonomic identifier

5270 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	1029 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays a major role in cell wall biogenesis.
Catalytic activity	UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1).
Subcellular location	Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note: A constitutive cytoplasmic pool is present that localizes to intracellular microvesicles termed chitosomes. Chitosomes constitute a separate secretory route distinct from the typical secretory pathway and serve as a vehicle for delivering the enzyme to the sites on the cell surface where polysaccharide sythesis takes place. Localizes to septa of yeast-like cells and to the basal septum separating the living tip cell from the vacuolated part in hyphae. Ref.3 Ref.4
Sequence similarities	Belongs to the chitin synthase family. Class I subfamily.
Sequence caution	The sequence CAA61027.1 differs from that shown. Reason: Frameshift at several positions. The sequence CAA61027.1 differs from that shown. Reason: Miscellaneous discrepancy. Internal deletion and contaminating sequence at the C-terminus from position 892 onwards. The sequence EAK81385.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Cytoplasmic vesicle Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW chitin biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitin synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1029	1029	Chitin synthase 3		PRO_0000193719
Regions
	Transmembrane	723 – 743	21	Potential
	Transmembrane	760 – 780	21	Potential
	Transmembrane	796 – 816	21	Potential
	Transmembrane	830 – 850	21	Potential
	Transmembrane	860 – 880	21	Potential
	Transmembrane	963 – 983	21	Potential
	Transmembrane	998 – 1018	21	Potential
	Compositional bias	175 – 181	7	Poly-Asp
	Compositional bias	231 – 238	8	Poly-Asp
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Glycosylation	514	1	N-linked (GlcNAc...) Potential
	Glycosylation	527	1	N-linked (GlcNAc...) Potential
	Glycosylation	689	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	8	1	A → G in CAA61027. Ref.2
	Sequence conflict	12 – 13	2	AA → G in CAA61027. Ref.2
	Sequence conflict	29	1	D → A in CAA61027. Ref.2
	Sequence conflict	62	1	A → E in CAA61027. Ref.2
	Sequence conflict	121	1	S → T in CAA61027. Ref.2
	Sequence conflict	271 – 274	4	MAGP → YGWT in CAA61027. Ref.2
	Sequence conflict	293	1	A → R in CAA61027. Ref.2
	Sequence conflict	312	1	G → R in CAA61027. Ref.2
	Sequence conflict	349 – 354	6	DDFASE → TDLER in CAA61027. Ref.2
	Sequence conflict	520	1	D → E in CAA61027. Ref.2
	Sequence conflict	526 – 527	2	EN → GD in CAA61027. Ref.2
	Sequence conflict	539	1	L → V in CAA61027. Ref.2
	Sequence conflict	545 – 546	2	GA → AQ in CAA61027. Ref.2
	Sequence conflict	630	1	A → R in CAA61027. Ref.2
	Sequence conflict	692 – 747	56	FFAAV…FRILT → SP in CAA61027. Ref.2
	Sequence conflict	882	1	L → W in CAA61027. Ref.2
	Sequence conflict	885	1	F → M in CAA61027. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99126-1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 73AFE99E52CF2F80	FASTA	1,029	113,242
	10 20 30 40 50 60 MAYYSRPASA GAARAQDDQD PYPYYPDPDL IVGSGANTSF VNPYEASGAA SSASHTSPFS 70 80 90 100 110 120 DAHAASASPA SILPLSHQQV SAHAPQQQHM SISVDPRDGQ QSRMPGLSES FYSQAAYALA 130 140 150 160 170 180 SPPPAAGALS PSAHLATLPE HSQAPLSGSV DGEYTYYSQS AAGHYSSLAH RHGQDDEDDD 190 200 210 220 230 240 DAETKYSPSS AHDEKYAYDR PDSAAAGTSP FGRAAGIAYL QSPYAQVARN DDDDEDEDAE 250 260 270 280 290 300 DPYRVLTRDS AFGGDNGQGY DPNSAYGGAG MAGPTGQFGD NHFDTQHFGP APARGAQLRR 310 320 330 340 350 360 HKTKKNVRLT KGNLILDCPV PTKLQTFLTR RAEDEFTTMR YSAVTCDPDD FASESFTLRP 370 380 390 400 410 420 ALYGRHTELF IAITMYNEDE VLFCRTFHGV MKNIAHLCSR NKSRTWGKDG WKKVVVAIIS 430 440 450 460 470 480 DGRKKIHPRV LDCLAALGVY QDGVAKNMVD GKEVRAHLYE YTTQLSIDSN LQFKGAERGL 490 500 510 520 530 540 VPMQIIFCLK EKNAKKINSH RWFFNAFCPI LQPNVTILLD VGTRPENKSI YYLWKSFDLN 550 560 570 580 590 600 SNVAGACGEI CAETKGKWGV GPLLLNPLVA AQNFEYKISN ILDKTTESVM GYISVLPGAF 610 620 630 640 650 660 SAYRYIALQN DEFGHGPLAS YFKGENLLGA DADVFTSNMY LAEDRILCFE LAAKRGHGWV 670 680 690 700 710 720 LKYVKSARGV TDVPEGLPEF ISQRRRWLNG SFFAAVYALY HTAQFVRSGH NVWRKSLLVF 730 740 750 760 770 780 ESFYSFVNMC FAWFGLANYY IFFRILTTSL EDPTFKLRGI GVFNVFMQYI YLGTVVSSFI 790 800 810 820 830 840 FAMGNRPQGS KWKYWAAVVV FALLTVYMMV AAVLCLSKVV ARVEHDAIYA QMVVSLLATY 850 860 870 880 890 900 GVYLISSLLA CDPLHLITSF LQYLLLAPTY INILNIYAFC NLHDFSWGTK GDTSISADLG 910 920 930 940 950 960 AVVSTSKGTV EITLPTAQAD IDTAYDDALN NLRTRPMIIR GDASNAEKEA RQMDYYKNIR 970 980 990 1000 1010 1020 TNVVLAWALS NGVLAAFILN GDAAGTFSDT GGVTRTKVYM VLVLIFVAGM ACIRFIGSTL YLTIRLING

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521.
[2]	"Two chitin synthase genes from Ustilago maydis." Xoconostle-Cazares B., Leon-Ramirez C., Ruiz-Herrera J. Microbiology 142:377-387(1996) [PubMed: 8932711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-891. Strain: RK32 / A2B3.
[3]	"Immunolocalization of chitin synthases in the phytopathogenic dimorphic fungus Ustilago maydis." Ruiz-Herrera J., Xoconostle-Cazares B., Reynaga-Pena C.G., Leon-Ramirez C., Carabez-Trejo A. FEMS Yeast Res. 6:999-1009(2006) [PubMed: 17042749] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Polar localizing class V myosin chitin synthases are essential during early plant infection in the plant pathogenic fungus Ustilago maydis." Weber I., Assmann D., Thines E., Steinberg G. Plant Cell 18:225-242(2006) [PubMed: 16314447] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACP01000009 Genomic DNA. Translation: EAK81385.1. Sequence problems. X87748 Genomic DNA. Translation: CAA61027.1. Sequence problems.
PIR	S55520.
RefSeq	XP_756621.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q99126.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Genome annotation databases
GeneID	3628493.
KEGG	uma:UM00474.1.
Enzyme and pathway databases
BRENDA	2.4.1.16. 2320.
Family and domain databases
InterPro	IPR004834. Chitin_synth. IPR013616. Chitin_synth_N. [Graphical view]
Pfam	PF01644. Chitin_synth_1. 1 hit. PF08407. Chitin_synth_1N. 1 hit. [Graphical view]
ProDom	PD002998. Chitin_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

CHS3_USTMA

Accession

Primary (citable) accession number: Q99126
Secondary accession number(s): Q4PHD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 9, 2007
Last modified:	October 13, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)