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Reviewed, UniProtKB/Swiss-Prot O54782 (MA2B2_MOUSE)

Last modified November 3, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Epididymis-specific alpha-mannosidase
    EC=3.2.1.24
Alternative name(s):
    Mannosidase alpha class 2B member 2
Gene names
Name: Man2b2
Synonyms: Kiaa0935
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1018 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Plays an important role in the early step of spermatogenesis.

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted.

Tissue specificity

Mainly expressed in the narrow region between the caput and corpus epididymis.

Developmental stage

Specifically expressed in type A spermatogonia at stages IX-XI of spermatogenesis. Detected there until the cell developed into type B spermatogonia.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processmannose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-mannosidase activity

Inferred from electronic annotation. Source: EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 1018997Epididymis-specific alpha-mannosidase
PRO_0000012078

Sites

Active site1511Nucleophile By similarity
Metal binding361Zinc By similarity
Metal binding381Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding4201Zinc By similarity

Amino acid modifications

Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation6201N-linked (GlcNAc...) Potential
Glycosylation6521N-linked (GlcNAc...) Potential
Glycosylation8181N-linked (GlcNAc...) Potential
Glycosylation8221N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2011S → T in BAA24266. Ref.1
Sequence conflict3371M → I in BAB23655. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O54782-1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 41AD7AAEA7CC88A9

FASTA1,018115,610
        10         20         30         40         50         60 
MGPLRWLPLL GQLLLLWPRA AQPAGPIRAF VVPHSHMDVG WVFTVQESMR AYAANVYTTV 

        70         80         90        100        110        120 
VAELVRGGQR RFIAVEQEFF RLWWDGVASE QQKQQVRQLL HEGRLEFVLG GQVMHDEAVT 

       130        140        150        160        170        180 
HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLISRIDYDL 

       190        200        210        220        230        240 
KDAMQEAQML QFVWHGSPSL SGQQEIFTHV MDHYSYCTPS HIPFSNRSGF YWNGVAVFPE 

       250        260        270        280        290        300 
PPPDGVYPNM SEPVTGANIH LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFD 

       310        320        330        340        350        360 
NMDPLLDYIN QRTAQFGISV QYATLNDYFQ ALHATNMTWG IRDHQDFLPY SSEPLQAWTG 

       370        380        390        400        410        420 
FYTSRSTLKG LARQASALLY AGESMFTRYM WPDPSGTLDP TWALQQLQQL RWAVSEVQHH 

       430        440        450        460        470        480 
DAITGTESPK VKNMYTEHLR MGMLGVRKLM VSIALGGPPG SGTGAPKDIM GPQVTPVLSV 

       490        500        510        520        530        540 
DTRPVGYSAS VYNPLAWKIT TIITLTVAFP NVSVTDELGH PVSTQIQNST KDPSAYDLLI 

       550        560        570        580        590        600 
LTTIPGLNYR HYQVMHARGD QAGTRELVAP RANTLKFSLK LRNQPSQEGK RLVPVMNDCY 

       610        620        630        640        650        660 
ILLFDQDTNM LHSIQDRQSN RTVRMTQEFL EYQANWDVKQ GPISDNYLFA PNNTAEPSWE 

       670        680        690        700        710        720 
AVGMEMVAGT LVTDIRQYFY RYITDQEYIY SIHTRLAHPS LAGELLCQRI EQQYRVGPLD 

       730        740        750        760        770        780 
LNREAILRTS SDLNSQQVLY SDNNGYQMQR RPYKAFKSNP IPRNYYPMVQ SAFIEDDKSR 

       790        800        810        820        830        840 
LVLLAERPHG VSSQGNGQVE VMLHRRLWNN LAWDLKYNLT LNDTSIVHPV LWLMLGPKST 

       850        860        870        880        890        900 
MTALHPRSGV ALQHGPVVLL KELADEETPV HGPHNPWPVT LPPNLHLQIL SVPGWTYSRS 

       910        920        930        940        950        960 
HAQHLRNLQR GHPEKPQANL QRVLLRLRHL YEAGEDPVLS RPATVDLKVV LRGLGSVVAV 

       970        980        990       1000       1010 
EERSLTGTWD VQMLQRWHWS TKTDHLKGHP TSPPRPPGGS IITVYPKEIR TFFIKFQQ 

« Hide

References

« Hide 'large scale' references
[1]"Stage-specific expression of a mouse homologue of the porcine 135kDa alpha-D-mannosidase (MAN2B2) in type A spermatogonia."
Hiramoto S., Tamba M., Kiuchi S., Jin Y.-Z., Bannai S., Sugita Y., Dacheux F., Dacheux J.-L., Yoshida M., Okamura N.
Biochem. Biophys. Res. Commun. 241:439-445(1997) [PubMed: 9425289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ddY.
Tissue: Testis.
[2]"Locarization of a mouse homologue of the porcine 135kDa a-D-mannosidase, mMAN2B2, in acrosome and its involvement in the sperm-egg interaction."
Hiramoto S., Noguchi J., Endoh Y., Tamba M., Okamura N.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Liver and Thymus.
[4]"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].
Strain: CD-1.
Tissue: Neural stem cell.
[5]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1018.
Tissue: Embryonic tail.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB006458 mRNA. Translation: BAA24266.1.
AB083124 Genomic DNA. Translation: BAC53862.1.
AK004900 mRNA. Translation: BAB23655.1.
AK040388 mRNA. Translation: BAC30580.1.
BC066211 mRNA. Translation: AAH66211.1.
AK173067 mRNA. Translation: BAD32345.1.
IPIIPI00117842.
PIRJC5799.
RefSeqNP_032576.2.
UniGeneMm.761

3D structure databases

HSSPHSSP built from PDB template 1O7D based on UniProtKB Q29451.
ModBaseSearch...

Protein-protein interaction databases

STRINGO54782.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PRIDEO54782.

Genome annotation databases

EnsemblENSMUST00000031002; ENSMUSP00000031002; ENSMUSG00000029119; Mus musculus. [Genome view]
GeneID17160.
KEGGmmu:17160.

Organism-specific databases

CTD17160.
MGIMGI:1195262. Man2b2.
RougeSearch...

Phylogenomic databases

HOGENOMO54782.
HOVERGENO54782.
OMAEIRTFFV.

Enzyme and pathway databases

BRENDA3.2.1.24. 244.

Gene expression databases

ArrayExpressO54782.
BgeeO54782.
CleanExMM_MAN2B2.
GenevestigatorO54782.
GermOnlineENSMUSG00000029119. Mus musculus.

Family and domain databases

InterProIPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_central.
IPR000602. Glyco_hydro_38_core.
[Graphical view]
Gene3DG3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit.
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio291434.
SOURCESearch...

Entry information

Entry nameMA2B2_MOUSE
AccessionPrimary (citable) accession number: O54782
Secondary accession number(s): Q69ZV1, Q8BH85, Q9DBK2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 7, 2005
Last modified: November 3, 2009
This is version 77 of the entry and version 2 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents