Reviewed, UniProtKB/Swiss-Prot P29030 (CHIT_BRUMA)

Names and origin

Protein names	Recommended name:     Endochitinase     EC=3.2.1.14 Alternative name(s):     MF1 antigen
Organism	Brugia malayi (Filarial nematode worm)
Taxonomic identifier	6279 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Brugia

Protein attributes

Sequence length	504 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	Microfilarial chitinase, which may function to degrade chitin-containing structures in the micro-filaria or in its mosquito vector during parasite development and transmission.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Developmental stage	The appearance of the MF1 antigen correspond with the onset of the parasite's ability to infect the mosquito.
Post-translational modification	O-glycosylated.
Miscellaneous	Known to bind calcium.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. Contains 1 chitin-binding type-2 domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Domain	Repeat Signal
Ligand	Calcium Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase 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
	Signal peptide	1 – 22	22
	Chain	23 – 504	482	Endochitinase		PRO_0000011947
Regions
	Repeat	407 – 420	14	1
	Repeat	421 – 434	14	2
	Repeat	435 – 448	14	3; approximate
	Domain	448 – 504	57	Chitin-binding type-2
	Region	23 – 400	378	Catalytic
	Region	407 – 448	42	3 X 14 AA approximate tandem repeats of E-T-E-A-Y-[ED]-T-D-E-T-E-E-T-S
	Compositional bias	401 – 448	48	Ser/Thr-rich (linker)
Sites
	Active site	148	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	480 ↔ 493		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29030-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: A78BE7BFB8E3709B	FASTA	504	55,971
	10 20 30 40 50 60 MNRTTLILFF IILSNTITVI HGYVRGCYYT NWAQYRDGEG KFLPGNIPNG LCTHILYAFA 70 80 90 100 110 120 KVDELGDSKP FEWNDEDTEW SKGMYSAVTK LRETNPGLKV LLSYGGYNFG SAIFTGIAKS 130 140 150 160 170 180 AQKTERFIKS AIAFLRKNNF DGFDLDWEYP VGVAEEHAKL VEAMKTAFVE EAKTSGKQRL 190 200 210 220 230 240 LLTAAVSAGK GTIDGSYNVE SLGKNFDLLF LMSYDLHGSW EKNVDLHGKL HPTKGEVSGI 250 260 270 280 290 300 GIFNTEFAAD YWASKGMPKE KIIIGIPMYA QGWTLDNPSE TAIGAAASRP SSASKTNPAG 310 320 330 340 350 360 GTASYWEICK YLKEGGKETV HQEGVGAYMV KGDQWYGYDN EETIRIKMKW LKEKGYGGAF 370 380 390 400 410 420 IWALDFDDFT GKSCGKGPYP LLNAISSELE GESENPEITT EEPSITETEA YETDETEETS 430 440 450 460 470 480 ETEAYDTDET EETSETEATT YDTDETEGQE CPERDGLFPH PTDCHLFIQC ANNIAYVMQC 490 500 PATTFFNDAI KVCDHMTNAP DTCI

References

[1]

"Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis." Fuhrman J.A., Lane W.S., Smith R.F., Piessens W.F., Perler F.B. Proc. Natl. Acad. Sci. U.S.A. 89:1548-1552(1992) [PubMed: 1542646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M73689 mRNA. Translation: AAA27854.1.
PIR	A38221.
3D structure databases
HSSP	HSSP built from PDB template 1LG2 based on UniProtKB Q13231.
ModBase	Search...
Protein family/group databases
CAZy	CBM14. Carbohydrate-Binding Module Family 14. GH18. Glycoside Hydrolase Family 18.
Enzyme and pathway databases
BRENDA	3.2.1.14. 27.
Family and domain databases
InterPro	IPR002557. Chitin-bd_peritrophin-A. IPR011583. Chitinase_II. IPR001223. Glyco_hydro18cat. IPR001579. Glyco_hydro_18_chit_AS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF01607. CBM_14. 1 hit. PF00704. Glyco_hydro_18. 1 hit. [Graphical view]
ProDom	PD000471. Chitinase_II. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00494. ChtBD2. 1 hit. SM00636. Glyco_18. 1 hit. [Graphical view]
PROSITE	PS50940. CHIT_BIND_II. 1 hit. PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIT_BRUMA

Accession

Primary (citable) accession number: P29030

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)