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Q8K2I4 (MANBA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-mannosidase

EC=3.2.1.25
Alternative name(s):
Lysosomal beta A mannosidase
Mannanase
Short name=Mannase
Gene names
Name:Manba
Synonyms:Bmn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides By similarity. UniProtKB O00462

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. UniProtKB O00462

Pathway

Glycan metabolism; N-glycan degradation.

Subcellular location

Lysosome By similarity UniProtKB O00462.

Tissue specificity

Highest level in liver, high levels in lung, testis, skin and spleen, moderate level in thymus. Activity found in plasma, kidney, liver, spleen, pancreas, brain, testis, epididymis, heart, lung and skeletal muscle. Ref.1 Ref.4

Disruption phenotype

Mice show vacuolation in the central nervous system and accumulation of disaccharides in brain and epididymis. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 879860Beta-mannosidase
PRO_0000250613

Sites

Active site4571Proton donor By similarity UniProtKB Q75W54

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation7361N-linked (GlcNAc...) Potential
Glycosylation8031N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1301I → V in AAK18177. Ref.1
Sequence conflict1301I → V in BAE24954. Ref.2
Sequence conflict1301I → V in BAE38715. Ref.2
Sequence conflict143 – 1453QFR → RFW in BAE38715. Ref.2
Sequence conflict1531C → R in BAE38715. Ref.2
Sequence conflict160 – 1623SYR → RYP in BAE38715. Ref.2
Sequence conflict2361K → E in AAK18177. Ref.1
Sequence conflict2361K → E in BAE24954. Ref.2
Sequence conflict2361K → E in BAE38715. Ref.2
Sequence conflict2361K → E in BAE41690. Ref.2
Sequence conflict2481G → S in AAK18177. Ref.1
Sequence conflict2481G → S in BAE24954. Ref.2
Sequence conflict2641N → H in BAE38715. Ref.2
Sequence conflict3761F → L in BAE24954. Ref.2
Sequence conflict4911K → N in BAE38715. Ref.2
Sequence conflict5111M → I in BAE38715. Ref.2
Sequence conflict7141H → Y in BAE38715. Ref.2
Sequence conflict7441G → R in BAE38715. Ref.2
Sequence conflict8341S → G in BAE38715. Ref.2
Sequence conflict8481R → Q in BAE38715. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8K2I4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 1DE203C44557719B

FASTA879100,831
        10         20         30         40         50         60 
MHLHLLLILA LFRAGCVVAG PSYSLSGSWR VSNGNGSLEL PATVPGYVHS ALHQHGLIQD 

        70         80         90        100        110        120 
PYYRFNDLNY RWISLDNWTY STEFKIPFNL SEWQKVKLIF DGVDTVAEIL FNNVTIGKTD 

       130        140        150        160        170        180 
NMFTGYSFDI TNVVKDVNSL KLQFRSAVQY AECQSKAHTS YRVPPECPPV EQKGECHVNF 

       190        200        210        220        230        240 
IRKAQCSFSW DWGPSFPSQG IWKDVRIEAY NIAHLDYLTF LPVYDNASQA WNIEIKASFD 

       250        260        270        280        290        300 
VASSKSVGGQ VTVAIPQLKT QQTNDIELQQ EQRIVKLLVK IRKDVAVETW WPRGHGNQTG 

       310        320        330        340        350        360 
YNMTILFALD GGLKIEKAAK VYFRTVQLIE EGIKGSPGLS FYFKINGLPI FLKGSNWIPA 

       370        380        390        400        410        420 
DSFQDKVTSD RLQLLFQSVV DANMNTLRVW GGGIYEQDEF YALCDELGIM VWQDFMFASA 

       430        440        450        460        470        480 
LYPTEPGFLA SVRKEVTYQV RRLKSHPSII IWSGNNENEV ALSVNWFHVN PRDMKTYIDD 

       490        500        510        520        530        540 
YVTLYVKNIR KIVLSEDKSR PFIASSPTNG MKTMEEGWIS YDPYSIQYGD IHFYNYADDC 

       550        560        570        580        590        600 
WNWKIFPKAR LVSEYGYQSW PSFSTLEKVS SQEDWAYNSR FSLHRQHHED GNHQMLHQVK 

       610        620        630        640        650        660 
MHFKLPQGTD PLRTFKDTIY LTQVMQAQCI KTETEFYLRS RSEIVDGKGH TMGALYWQLN 

       670        680        690        700        710        720 
DIWQAPSWAS LEYGGKWKML HYFARRFFAP LLPVGFEDEG VFYVYGVSDL HKDHHTQLTV 

       730        740        750        760        770        780 
RLHHWSSPKP LCSLVNSSIV VKAGEAVVLF QMPVSELLKR CRGCTRETCV VSFYFSTDKE 

       790        800        810        820        830        840 
LFSPTNYHFL SSLKDAKGLL EANITVNISQ KGNVFVFDLE TSAVAPFVWL DVGSIPGRFS 

       850        860        870 
DNGFLMIRKK LSVLFYPWKP TSKSELQQAF SVTSLTDTY 

« Hide

References

« Hide 'large scale' references
[1]"Mouse beta-mannosidase, cDNA cloning, expression, and chromosomal localization."
Beccari T., Bibi L., Stinchi S., Stirling J.L., Orlacchio A.
Biosci. Rep. 21:315-323(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Spleen.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell, Embryonic heart, Embryonic stem cell and Mammary gland.
[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].
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Beta-mannosidosis mice: a model for the human lysosomal storage disease."
Zhu M., Lovell K.L., Patterson J.S., Saunders T.L., Hughes E.D., Friderici K.H.
Hum. Mol. Genet. 15:493-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF306557 mRNA. Translation: AAK18177.1.
AK010623 mRNA. Translation: BAB27069.1.
AK142165 mRNA. Translation: BAE24954.1.
AK166340 mRNA. Translation: BAE38715.1.
AK170290 mRNA. Translation: BAE41690.1.
BC031409 mRNA. Translation: AAH31409.1.
RefSeqNP_081564.3. NM_027288.3.
UniGeneMm.280536.

3D structure databases

ProteinModelPortalQ8K2I4.
SMRQ8K2I4. Positions 25-879.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029814.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

PTM databases

PhosphoSiteQ8K2I4.

Proteomic databases

PaxDbQ8K2I4.
PRIDEQ8K2I4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029814; ENSMUSP00000029814; ENSMUSG00000028164.
GeneID110173.
KEGGmmu:110173.
UCSCuc008rlu.2. mouse.

Organism-specific databases

CTD4126.
MGIMGI:88175. Manba.

Phylogenomic databases

eggNOGCOG3250.
GeneTreeENSGT00390000001670.
HOGENOMHOG000186862.
HOVERGENHBG052404.
InParanoidQ8K2I4.
KOK01192.
OrthoDBEOG7S7SD2.
PhylomeDBQ8K2I4.
TreeFamTF105723.

Enzyme and pathway databases

UniPathwayUPA00280.

Gene expression databases

ArrayExpressQ8K2I4.
BgeeQ8K2I4.
CleanExMM_MANBA.
GenevestigatorQ8K2I4.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

NextBio363463.
PROQ8K2I4.
SOURCESearch...

Entry information

Entry nameMANBA_MOUSE
AccessionPrimary (citable) accession number: Q8K2I4
Secondary accession number(s): Q3TDB3 expand/collapse secondary AC list , Q3TLS7, Q3UQT5, Q99MS1, Q9CRH3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries