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Protein

Epididymis-specific alpha-mannosidase

Gene

Man2b2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays an important role in the early step of spermatogenesis.

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361ZincBy similarity
Metal bindingi38 – 381ZincBy similarity
Active sitei151 – 1511NucleophileBy similarity
Metal bindingi151 – 1511ZincBy similarity
Metal bindingi420 – 4201ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Epididymis-specific alpha-mannosidase (EC:3.2.1.24)
Alternative name(s):
Mannosidase alpha class 2B member 2
Gene namesi
Name:Man2b2
Synonyms:Kiaa0935
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1195262. Man2b2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 1018997Epididymis-specific alpha-mannosidasePRO_0000012078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi818 – 8181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi822 – 8221N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO54782.
PaxDbiO54782.
PRIDEiO54782.

PTM databases

PhosphoSiteiO54782.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiO54782.
CleanExiMM_MAN2B2.
ExpressionAtlasiO54782. baseline and differential.
GenevisibleiO54782. MM.

Interactioni

Protein-protein interaction databases

IntActiO54782. 1 interaction.
MINTiMINT-4100949.
STRINGi10090.ENSMUSP00000031002.

Structurei

3D structure databases

ProteinModelPortaliO54782.
SMRiO54782. Positions 27-807.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG306356.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000113450.
HOVERGENiHBG052392.
InParanoidiO54782.
KOiK12312.
OMAiYSTEPFQ.
OrthoDBiEOG7RFTGG.
PhylomeDBiO54782.
TreeFamiTF332447.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O54782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPLRWLPLL GQLLLLWPRA AQPAGPIRAF VVPHSHMDVG WVFTVQESMR
60 70 80 90 100
AYAANVYTTV VAELVRGGQR RFIAVEQEFF RLWWDGVASE QQKQQVRQLL
110 120 130 140 150
HEGRLEFVLG GQVMHDEAVT HLDDQILQLT EGHGFLYETF GIRPQFSWHV
160 170 180 190 200
DPFGASATTP TLFALAGFNA HLISRIDYDL KDAMQEAQML QFVWHGSPSL
210 220 230 240 250
SGQQEIFTHV MDHYSYCTPS HIPFSNRSGF YWNGVAVFPE PPPDGVYPNM
260 270 280 290 300
SEPVTGANIH LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFD
310 320 330 340 350
NMDPLLDYIN QRTAQFGISV QYATLNDYFQ ALHATNMTWG IRDHQDFLPY
360 370 380 390 400
SSEPLQAWTG FYTSRSTLKG LARQASALLY AGESMFTRYM WPDPSGTLDP
410 420 430 440 450
TWALQQLQQL RWAVSEVQHH DAITGTESPK VKNMYTEHLR MGMLGVRKLM
460 470 480 490 500
VSIALGGPPG SGTGAPKDIM GPQVTPVLSV DTRPVGYSAS VYNPLAWKIT
510 520 530 540 550
TIITLTVAFP NVSVTDELGH PVSTQIQNST KDPSAYDLLI LTTIPGLNYR
560 570 580 590 600
HYQVMHARGD QAGTRELVAP RANTLKFSLK LRNQPSQEGK RLVPVMNDCY
610 620 630 640 650
ILLFDQDTNM LHSIQDRQSN RTVRMTQEFL EYQANWDVKQ GPISDNYLFA
660 670 680 690 700
PNNTAEPSWE AVGMEMVAGT LVTDIRQYFY RYITDQEYIY SIHTRLAHPS
710 720 730 740 750
LAGELLCQRI EQQYRVGPLD LNREAILRTS SDLNSQQVLY SDNNGYQMQR
760 770 780 790 800
RPYKAFKSNP IPRNYYPMVQ SAFIEDDKSR LVLLAERPHG VSSQGNGQVE
810 820 830 840 850
VMLHRRLWNN LAWDLKYNLT LNDTSIVHPV LWLMLGPKST MTALHPRSGV
860 870 880 890 900
ALQHGPVVLL KELADEETPV HGPHNPWPVT LPPNLHLQIL SVPGWTYSRS
910 920 930 940 950
HAQHLRNLQR GHPEKPQANL QRVLLRLRHL YEAGEDPVLS RPATVDLKVV
960 970 980 990 1000
LRGLGSVVAV EERSLTGTWD VQMLQRWHWS TKTDHLKGHP TSPPRPPGGS
1010
IITVYPKEIR TFFIKFQQ
Length:1,018
Mass (Da):115,610
Last modified:June 7, 2005 - v2
Checksum:i41AD7AAEA7CC88A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011S → T in BAA24266 (PubMed:9425289).Curated
Sequence conflicti337 – 3371M → I in BAB23655 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19243.1.
PIRiJC5799.
RefSeqiNP_032576.2. NM_008550.2.
UniGeneiMm.761.

Genome annotation databases

EnsembliENSMUST00000031002; ENSMUSP00000031002; ENSMUSG00000029119.
GeneIDi17160.
KEGGimmu:17160.
UCSCiuc008xfb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19243.1.
PIRiJC5799.
RefSeqiNP_032576.2. NM_008550.2.
UniGeneiMm.761.

3D structure databases

ProteinModelPortaliO54782.
SMRiO54782. Positions 27-807.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54782. 1 interaction.
MINTiMINT-4100949.
STRINGi10090.ENSMUSP00000031002.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

PTM databases

PhosphoSiteiO54782.

Proteomic databases

MaxQBiO54782.
PaxDbiO54782.
PRIDEiO54782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031002; ENSMUSP00000031002; ENSMUSG00000029119.
GeneIDi17160.
KEGGimmu:17160.
UCSCiuc008xfb.2. mouse.

Organism-specific databases

CTDi23324.
MGIiMGI:1195262. Man2b2.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG306356.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000113450.
HOVERGENiHBG052392.
InParanoidiO54782.
KOiK12312.
OMAiYSTEPFQ.
OrthoDBiEOG7RFTGG.
PhylomeDBiO54782.
TreeFamiTF332447.

Miscellaneous databases

ChiTaRSiMan2b2. mouse.
NextBioi291434.
PROiO54782.
SOURCEiSearch...

Gene expression databases

BgeeiO54782.
CleanExiMM_MAN2B2.
ExpressionAtlasiO54782. baseline and differential.
GenevisibleiO54782. MM.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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: 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1018.
    Tissue: Embryonic tail.

Entry informationi

Entry nameiMA2B2_MOUSE
AccessioniPrimary (citable) accession number: O54782
Secondary accession number(s): Q69ZV1, Q8BH85, Q9DBK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 7, 2005
Last modified: June 24, 2015
This is version 125 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.