P29029 (CHIT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endochitinase
EC=3.2.1.14

Alternative name(s):
Soluble cell wall protein 2

Gene names

Name:	CTS1
Synonyms:	SCW2
Ordered Locus Names:	YLR286C
ORF Names:	L8003.13

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chitinase is required for cell separation during growth of Saccharomyces cerevisiae.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Subcellular location	Secreted. Secreted › cell wall. Note: Most of the enzyme is secreted, but a significant amount of chitinase is also found associated with the cell wall through binding of C-terminal domain to chitin. Ref.5
Post-translational modification	Extensively glycosylated with a series of short O-linked mannose oligosaccharides ranging in size from Man2 to Man5.
Miscellaneous	Present with 6350 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Chitin degradation Polysaccharide degradation
Cellular component	Cell wall Secreted
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW chitin catabolic process Inferred by curator. Source: SGD cytokinesis, completion of separation Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD endoplasmic reticulum Inferred from direct assay. Source: SGD extracellular region Inferred from direct assay Ref.1. Source: SGD fungal-type cell wall Inferred from direct assay Ref.1. Source: SGD nuclear envelope Inferred from direct assay. Source: SGD
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitin binding Inferred from electronic annotation. Source: UniProtKB-KW endochitinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.1 Ref.5

Chain

21 – 562

542

Endochitinase

PRO_0000011936

Regions

Region

21 – 327

307

Catalytic

Region

481 – 562

82

Chitin-binding, high affinity

Compositional bias

328 – 480

153

Ser/Thr-rich

Sites

Active site

157

1

Proton donor By similarity

Amino acid modifications

Glycosylation

553

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

16

1

L → P in strain: DBY939.

Natural variant

23

1

R → S in strain: DBY939 and SEY6210.

Natural variant

321

1

T → S in strain: DBY939.

Natural variant

336 – 340

5

Missing in strain: DBY939.

Natural variant

399

1

S → A in strain: DBY939.

Natural variant

433 – 434

2

PI → SL in strain: DBY939.

Natural variant

461

1

T → K in strain: DBY939.

Natural variant

477 – 481

5

Missing in strain: DBY939.

Experimental info

Sequence conflict

168

1

A → R in AAA34539. Ref.1

Sequence conflict

168

1

A → R in AAA34538. Ref.1

Secondary structure

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562

Helix Strand Turn

Details...

Beta strand

28 – 35

8

Helix

44 – 48

5

Beta strand

50 – 52

3

Beta strand

54 – 64

11

Turn

65 – 67

3

Helix

72 – 74

3

Helix

87 – 98

12

Beta strand

102 – 108

7

Helix

119 – 133

15

Turn

143 – 146

4

Beta strand

150 – 155

6

Helix

164 – 175

12

Beta strand

178 – 180

3

Beta strand

183 – 186

4

Beta strand

189 – 193

5

Turn

195 – 197

3

Helix

198 – 203

6

Beta strand

207 – 212

6

Beta strand

214 – 216

3

Helix

226 – 235

10

Beta strand

243 – 251

9

Beta strand

254 – 257

4

Helix

263 – 273

11

Beta strand

279 – 285

7

Helix

287 – 292

6

Helix

300 – 311

12

Sequences

	Sequence		Length	Mass (Da)
	P29029 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 0ABCEFBF448E1E19	FASTA	562	59,015
	10 20 30 40 50 60 MSLLYIILLF TQFLLLPTDA FDRSANTNIA VYWGQNSAGT QESLATYCES SDADIFLLSF 70 80 90 100 110 120 LNQFPTLGLN FANACSDTFS DGLLHCTQIA EDIETCQSLG KKVLLSLGGA SGSYLFSDDS 130 140 150 160 170 180 QAETFAQTLW DTFGEGTGAS ERPFDSAVVD GFDFDIENNN EVGYSALATK LRTLFAEGTK 190 200 210 220 230 240 QYYLSAAPQC PYPDASVGDL LENADIDFAF IQFYNNYCSV SGQFNWDTWL TYAQTVSPNK 250 260 270 280 290 300 NIKLFLGLPG SASAAGSGYI SDTSLLESTI ADIASSSSFG GIALWDASQA FSNELNGEPY 310 320 330 340 350 360 VEILKNLLTS ASQTATTTVA TSKTSAASTS SASTSSASTS QKKTTQSTTS TQSKSKVTLS 370 380 390 400 410 420 PTASSAIKTS ITQTTKTLTS STKTKSSLGT TTTESTLNSV AITSMKTTLS SQITSAALVT 430 440 450 460 470 480 PQTTTTSIVS SAPIQTAITS TLSPATKSSS VVSLQTATTS TLSPTTTSTS SGSTSSGSTS 490 500 510 520 530 540 SDSTARTLAK ELNAQYAAGK LNGKSTCTEG EIACSADGKF AVCDHSAWVY MECASGTTCY 550 560 AYDSGDSVYT QCNFSYLESN YF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chitinase is required for cell separation during growth of Saccharomyces cerevisiae." Kuranda M.J., Robbins P.W. J. Biol. Chem. 266:19758-19767(1991) [PubMed: 1918080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-38. Strain: DBY918 and DBY939.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating." Cappellaro C., Mrsa V., Tanner W. J. Bacteriol. 180:5030-5037(1998) [PubMed: 9748433] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-32, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74070 Genomic DNA. Translation: AAA34539.1.
M74069 Genomic DNA. Translation: AAA34538.1.
U17243 Genomic DNA. Translation: AAB67331.1.
AY693040 Genomic DNA. Translation: AAT93059.1.
BK006945 Genomic DNA. Translation: DAA09597.1.

PIR

A41035.
B41035.
S50371.

RefSeq

NP_013388.1. NM_001182173.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UY2	X-ray	1.60	A	22-315	[»]
2UY3	X-ray	1.90	A	22-315	[»]
2UY4	X-ray	1.75	A	22-315	[»]
2UY5	X-ray	1.60	A	22-315	[»]

ProteinModelPortal

P29029.

SMR

P29029. Positions 25-312.

ModBase

Search...

Protein-protein interaction databases

STRING

P29029.

Protein family/group databases

CAZy

CBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Proteomic databases

PeptideAtlas

P29029.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR286C; YLR286C; YLR286C.

GeneID

850992.

KEGG

sce:YLR286C.

NMPDR

fig|4932.3.peg.4404.

Organism-specific databases

CYGD

YLR286c.

SGD

S000004276. CTS1.

Phylogenomic databases

eggNOG

fuNOG05730.

GeneTree

EFGT00050000000133.

HOGENOM

HBG588556.

OMA

YWGQNSA.

OrthoDB

EOG40KC7X.

Gene expression databases

ArrayExpress

P29029.

Genevestigator

P29029.

GermOnline

YLR286C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005089. CBM_fam19.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01183.

Pfam

PF03427. CBM_19. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967519.

Entry information

Entry name

CHIT_YEAST

Accession

Primary (citable) accession number: P29029
Secondary accession number(s): D6VYT1, P29028

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program