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Q9CPX3

- LYZL1_MOUSE

UniProt

Q9CPX3 - LYZL1_MOUSE

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Protein
Lysozyme-like protein 1
Gene
Lyzl1, Lyc2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541 By similarity
Active sitei71 – 711 By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme-like protein 1 (EC:3.2.1.17)
Gene namesi
Name:Lyzl1
Synonyms:Lyc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1914578. Lyzl1.

Subcellular locationi

Secreted Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 148129Lysozyme-like protein 1
PRO_0000240636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 145 By similarity
Disulfide bondi49 ↔ 133 By similarity
Glycosylationi58 – 581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi83 ↔ 98 By similarity
Disulfide bondi94 ↔ 112 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

BgeeiQ9CPX3.
CleanExiMM_LYZL1.
GenevestigatoriQ9CPX3.

Interactioni

Subunit structurei

Monomer Inferred.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025076.

Structurei

3D structure databases

ProteinModelPortaliQ9CPX3.
SMRiQ9CPX3. Positions 20-147.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG72851.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiQ9CPX3.
KOiK01185.
OMAiTWCRRAK.
OrthoDBiEOG7BW0M5.
PhylomeDBiQ9CPX3.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CPX3-1 [UniParc]FASTAAdd to Basket

« Hide

MKSVGVFALI ISFSIVAESK IYTRCKLAKI FAKAGLDNYG GFALGNWLCM    50
AYYESHYNTT AENVLEDGST DYGIFQINSF TWCRNARKHQ KNHCHVACSA 100
LITDDLTDAI LCAKKIVKET QGMNYWQGWK KNCENKDMSE WKRGCEVS 148
Length:148
Mass (Da):16,802
Last modified:June 1, 2001 - v1
Checksum:iED87F25FF85E571A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY572447 mRNA. Translation: AAS77886.1.
AK006241 mRNA. Translation: BAB24475.1.
AK006630 mRNA. Translation: BAB24680.1.
BC048450 mRNA. Translation: AAH48450.1.
CCDSiCCDS29035.1.
RefSeqiNP_080368.1. NM_026092.3.
UniGeneiMm.158148.

Genome annotation databases

EnsembliENSMUST00000025076; ENSMUSP00000025076; ENSMUSG00000024233.
GeneIDi67328.
KEGGimmu:67328.
UCSCiuc008dyd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY572447 mRNA. Translation: AAS77886.1 .
AK006241 mRNA. Translation: BAB24475.1 .
AK006630 mRNA. Translation: BAB24680.1 .
BC048450 mRNA. Translation: AAH48450.1 .
CCDSi CCDS29035.1.
RefSeqi NP_080368.1. NM_026092.3.
UniGenei Mm.158148.

3D structure databases

ProteinModelPortali Q9CPX3.
SMRi Q9CPX3. Positions 20-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000025076.

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025076 ; ENSMUSP00000025076 ; ENSMUSG00000024233 .
GeneIDi 67328.
KEGGi mmu:67328.
UCSCi uc008dyd.1. mouse.

Organism-specific databases

CTDi 84569.
MGIi MGI:1914578. Lyzl1.

Phylogenomic databases

eggNOGi NOG72851.
GeneTreei ENSGT00550000074398.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi Q9CPX3.
KOi K01185.
OMAi TWCRRAK.
OrthoDBi EOG7BW0M5.
PhylomeDBi Q9CPX3.
TreeFami TF324882.

Miscellaneous databases

NextBioi 324250.
PROi Q9CPX3.
SOURCEi Search...

Gene expression databases

Bgeei Q9CPX3.
CleanExi MM_LYZL1.
Genevestigatori Q9CPX3.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Zhang K., 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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiLYZL1_MOUSE
AccessioniPrimary (citable) accession number: Q9CPX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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