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UniProtKB/Swiss-Prot entry O54782


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MA2B2_MOUSE
Primary accession number O54782
Secondary accession numbers Q69ZV1 Q8BH85 Q9DBK2
Integrated into Swiss-Prot on November 16, 2001
Sequence was last modified on June 7, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 73)
Name and origin of the protein
Protein name Epididymis-specific alpha-mannosidase [Precursor]
Synonyms EC 3.2.1.24
Mannosidase alpha class 2B member 2
Gene name
Name: Man2b2
Synonyms: Kiaa0935
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ddY;
TISSUE=Testis;
DOI=10.1006/bbrc.1997.7768; PubMed=9425289 [NCBI, ExPASy, EBI, Israel, Japan]
Hiramoto S., Tamba M., Kiuchi S., Jin Y.-Z., Bannai S., Sugita Y., Dacheux F., Dacheux J.-L., Yoshida M., Okamura N.;
"Stage-specific expression of a mouse homologue of the porcine 135kDa alpha-D-mannosidase (MAN2B2) in type A spermatogonia.";
Biochem. Biophys. Res. Commun. 241:439-445(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hiramoto S., Noguchi J., Endoh Y., Tamba M., Okamura N.;
"Locarization of a mouse homologue of the porcine 135kDa a-D-mannosidase, mMAN2B2, in acrosome and its involvement in the sperm-egg interaction.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CD-1;
TISSUE=Neural stem cell;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1018.
TISSUE=Embryonic tail;
DOI=10.1093/dnares/11.3.205; PubMed=15368895 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
DNA Res. 11:205-218(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB006458; BAA24266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB083124; BAC53862.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004900; BAB23655.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK040388; BAC30580.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066211; AAH66211.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK173067; BAD32345.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00117842; -.
PIR JC5799; JC5799.
RefSeq NP_032576.2; -.
UniGene Mm.761
3D structure databases
HSSP Q29451; 1O7D. [HSSP ENTRY / PDB]
ModBase O54782.
Protein family/group databases
CAZy GH38; Glycoside Hydrolase Family 38.
Enzyme and pathway databases
BRENDA 3.2.1.24; 244.
Organism-specific databases
MGI MGI:1195262; Man2b2.
Gene expression databases
ArrayExpress O54782; -.
Bgee O54782; -.
CleanEx MM_MAN2B2; -.
GermOnline ENSMUSG00000029119; Mus musculus.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004559; Molecular function: alpha-mannosidase activity (inferred from electronic annotation from EC).
GO:0030246; Molecular function: carbohydrate binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006013; Biological process: mannose metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR011682; Glyco_hydro_38_C.
IPR015341; Glyco_hydro_38_central.
IPR000602; Glyco_hydro_38_core.
Graphical view of domain structure.
Gene3D G3DSA:3.20.110.10; Glyco_hydro_38_core; 1.
Pfam PF09261; Alpha-mann_mid; 1.
PF01074; Glyco_hydro_38; 1.
PF07748; Glyco_hydro_38C; 1.
Pfam graphical view of domain structure.
Genome annotation databases
Ensembl ENSMUSG00000029119; Mus musculus. [Contig view]
GeneID 17160; -.
KEGG mmu:17160; -.
Phylogenomic databases
HOGENOM O54782; -.
HOVERGEN O54782; -.
OMA O54782; EIRTFFV.
Other
NextBio 291434; -.
SOURCE Man2b2; Mus musculus.
ROUGE KIAA0935.
ProtoNet O54782.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Secreted; Signal; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1     21  21     Potential. 
CHAIN   22   1018  997     Epididymis-specific alpha-mannosidase. PRO_0000012078
ACT_SITE   151    151        Nucleophile (By similarity). 
METAL   36     36        Zinc (By similarity). 
METAL   38     38        Zinc (By similarity). 
METAL   151    151        Zinc (By similarity). 
METAL   420    420        Zinc (By similarity). 
CARBOHYD   226    226        N-linked (GlcNAc...) (Potential). 
CARBOHYD   249    249        N-linked (GlcNAc...) (Potential). 
CARBOHYD   294    294        N-linked (GlcNAc...) (Potential). 
CARBOHYD   336    336        N-linked (GlcNAc...) (Potential). 
CARBOHYD   511    511        N-linked (GlcNAc...) (Potential). 
CARBOHYD   528    528        N-linked (GlcNAc...) (Potential). 
CARBOHYD   620    620        N-linked (GlcNAc...) (Potential). 
CARBOHYD   652    652        N-linked (GlcNAc...) (Potential). 
CARBOHYD   818    818        N-linked (GlcNAc...) (Potential). 
CARBOHYD   822    822        N-linked (GlcNAc...) (Potential). 
CONFLICT   201    201        S -> T (in Ref. 1; BAA24266). 
CONFLICT   337    337        M -> I (in Ref. 3; BAB23655). 
Sequence information
Length: 1018 AA [This is the length of the unprocessed precursor] Molecular weight: 115610 Da [This is the MW of the unprocessed precursor] CRC64: 41AD7AAEA7CC88A9 [This is a checksum on the sequence]
        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 

O54782 in FASTA format

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