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Q9DA11 (LYZL6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Lysozyme-like protein 6

EC=3.2.1.17
Gene names
Name:Lyzl6
Synonyms:Lyc1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Subunit structure

Monomer Probable.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlysozyme activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 148129Lysozyme-like protein 6
PRO_0000240641

Sites

Active site541 By similarity
Active site711 By similarity

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 145 By similarity
Disulfide bond49 ↔ 133 By similarity
Disulfide bond83 ↔ 98 By similarity
Disulfide bond94 ↔ 112 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DA11-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 81C6F74A2387D97A

FASTA14816,818
        10         20         30         40         50         60 
MLKALFICVA SCLLVVNDGN IIHRCSLAKI LYEEDLDGFE GYSLPDWLCL AFVESNFNIS 

        70         80         90        100        110        120 
KVNENVDGSF DYGIFQINSR YWCNDYQSHS ENFCHVDCQE LLSPNLISTI HCAKKIVSGP 

       130        140 
GGMKNWVEWK LHCLGRPLSY WMTGCHLG 

« Hide

References

« Hide 'large scale' references
[1]Zhang K., Dang Y., Yu L.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY566284 mRNA. Translation: AAS68631.1.
AK006279 mRNA. Translation: BAB24499.1.
BC048617 mRNA. Translation: AAH48617.1.
IPIIPI00117864.
RefSeqNP_081359.1.
UniGeneMm.275677.

3D structure databases

ProteinModelPortalQ9DA11.
SMRQ9DA11. Positions 19-147.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DA11.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEQ9DA11.

Genome annotation databases

EnsemblENSMUST00000021328; ENSMUSP00000021328; ENSMUSG00000020945; Mus musculus. [Genome view]
ENSMUST00000107014; ENSMUSP00000102628; ENSMUSG00000020945; Mus musculus. [Genome view]
GeneID69444.
KEGGmmu:69444.
UCSCuc007lvl.1. mouse.

Organism-specific databases

CTD69444.
MGIMGI:1916694. Lyzl6.

Phylogenomic databases

HOGENOMHBG505822.
HOVERGENHBG052297.
InParanoidQ9DA11.
OMAWCNDYKS.
OrthoDBEOG9MD0K1.
PhylomeDBQ9DA11.

Enzyme and pathway databases

BRENDA3.2.1.17. 244.

Gene expression databases

ArrayExpressQ9DA11.
BgeeQ9DA11.
CleanExMM_LYZL6.
GenevestigatorQ9DA11.
GermOnlineENSMUSG00000020945. Mus musculus.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio329470.
SOURCESearch...

Entry information

Entry nameLYZL6_MOUSE
AccessionPrimary (citable) accession number: Q9DA11
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: August 10, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families