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O09159

- MA2B1_MOUSE

UniProt

O09159 - MA2B1_MOUSE

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Protein

Lysosomal alpha-mannosidase

Gene

Man2b1

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

Functioni

Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.

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 bindingi72 – 721ZincBy similarity
Metal bindingi74 – 741ZincBy similarity
Active sitei196 – 1961NucleophileBy similarity
Metal bindingi196 – 1961ZincBy similarity
Metal bindingi446 – 4461ZincBy similarity

GO - Molecular functioni

  1. alpha-mannosidase activity Source: MGI
  2. mannose binding Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. learning or memory Source: MGI
  2. mannose metabolic process Source: MGI
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:
Lysosomal alpha-mannosidase (EC:3.2.1.24)
Short name:
Laman
Alternative name(s):
Lysosomal acid alpha-mannosidase
Mannosidase alpha class 2B member 1
Mannosidase alpha-B
Gene namesi
Name:Man2b1
Synonyms:Laman, Man2b, Manb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:107286. Man2b1.

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4949Sequence AnalysisAdd
BLAST
Chaini50 – 1013964Lysosomal alpha-mannosidasePRO_0000012076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 358By similarity
Disulfide bondi268 ↔ 273By similarity
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi412 ↔ 472By similarity
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi493 ↔ 501By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi633 – 6331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi646 – 6461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi693 – 6931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi767 – 7671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO09159.
PaxDbiO09159.
PRIDEiO09159.

Expressioni

Gene expression databases

BgeeiO09159.
CleanExiMM_MAN2B1.
GenevestigatoriO09159.

Interactioni

Protein-protein interaction databases

IntActiO09159. 2 interactions.
MINTiMINT-1675875.

Structurei

3D structure databases

ProteinModelPortaliO09159.
SMRiO09159. Positions 51-341, 349-421, 431-583, 606-875, 886-1007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000007676.
HOVERGENiHBG052391.
InParanoidiO09159.
KOiK12311.
OMAiNMQLTVL.
OrthoDBiEOG786H2P.
TreeFamiTF313840.

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.

O09159-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTGPLTSGV RAGGGNTGWL WMSSCNLGSP VLPISFLFWL LLAAPGARAA
60 70 80 90 100
GYKTCPPTKP GMLNVHLLPH THDDVGWLKT VDQYYYGILS DVQHASVQYI
110 120 130 140 150
LDSVVSSLLE KPTRRFIYVE MAFFSRWWKQ QTSATQDAVR NLVRQGRLEF
160 170 180 190 200
VNGGWVMNDE AATHYGAIVD QMTLGLRFLQ DTFGSDGLPR VAWHIDPFGH
210 220 230 240 250
SREQASLFAQ MGFDGFFLGR IDYQDKLNRK KKLRMEELWR ASDSLEPPAA
260 270 280 290 300
DLFTGVLPNN YNPPKYLCWD VLCTDPPVVD NPRSPEFNAK TLVNYFLKLA
310 320 330 340 350
SSQKGFYRTN HTVMTMGSDF HYENANMWFK NMDKLIRLVN AQQVNGSLVH
360 370 380 390 400
VLYSTPTCYL WELNKANLTW TVKEDDFFPY ADGPHMFWTG YFSSRPALKR
410 420 430 440 450
YERLSYNFLQ VCNQLEALVG PEANVGPYGS GDSAPLQEAM AVLQHHDAVS
460 470 480 490 500
GTARQNVVND YARQLAAGWG PCEVLVSNAL ARLSHYKQNF SFCRELNISI
510 520 530 540 550
CPVSQTSERF QVTLYNPLGR KVDQMVRLPV YEGNFIVKDP HDKNISSNVV
560 570 580 590 600
MVPSYYSETY QWELLFPASV PALGFSTYSV AKMSDLNHQA HNLLSRPRKH
610 620 630 640 650
KSHHVLVIEN KYMRATFDSG TGLLMKIENL EQNLSLPVSQ GFFWYNASVG
660 670 680 690 700
DEESSQASGA YIFRPNVGKP IPVSRWAQIS LVKTALVQEV HQNFSAWCSQ
710 720 730 740 750
VIRLYKGQRH LELEWTVGPI PVRDDWGKEV ISRFDTPMKT KGQFFTDSNG
760 770 780 790 800
REILKRRDDY RPTWTLNQTE PVAGNYYPVN TRIYITDGQM QLTVLTDRSQ
810 820 830 840 850
GGSSLQDGSL ELMVHRRLLV DDDRGVSEPL LETDTGDKVR GRHLVLLSSV
860 870 880 890 900
SDAAARHRLL AEQEVLAPQV VLSLGGSSPY HSRATPKTQF SGLRQELPPQ
910 920 930 940 950
VHLLTLARWG PKMLLLRLEH QFALKEDSDR NLSSPVTLNV QNLFQTFTIN
960 970 980 990 1000
YLQETTLAAN QPLSRASRLK WMTNTGPTSY PEPSKLDPTS VTLKPMEIRT
1010
FLASVQWQEH RPA
Length:1,013
Mass (Da):114,648
Last modified:July 27, 2011 - v4
Checksum:iA83B5397D9D38D31
GO

Sequence cautioni

The sequence AAC09470.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC53369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 495PGARA → LASG in AAC53369. (PubMed:9355733)Curated
Sequence conflicti45 – 495PGARA → LASG in AAC78560. (PubMed:9799835)Curated
Sequence conflicti344 – 3441V → A in AAC53369. (PubMed:9355733)Curated
Sequence conflicti344 – 3441V → A in AAC78560. (PubMed:9799835)Curated
Sequence conflicti344 – 3441V → A in AAH05430. (PubMed:15489334)Curated
Sequence conflicti344 – 3441V → A in AAC09470. (PubMed:9305783)Curated
Sequence conflicti980 – 9801Y → F in AAC53369. (PubMed:9355733)Curated
Sequence conflicti980 – 9801Y → F in AAC78560. (PubMed:9799835)Curated
Sequence conflicti980 – 9801Y → F in AAH05430. (PubMed:15489334)Curated
Sequence conflicti980 – 9801Y → F in AAC09470. (PubMed:9305783)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29947 mRNA. Translation: AAC53369.1. Different initiation.
AF044192
, AF044174, AF044175, AF044176, AF044177, AF044178, AF044179, AF044180, AF044181, AF044182, AF044183, AF044184, AF044185, AF044186, AF044187, AF044188, AF044189, AF044190, AF044191 Genomic DNA. Translation: AAC78560.1.
AK147928 mRNA. Translation: BAE28235.1.
AK004817 mRNA. Translation: BAB23588.1.
BC005430 mRNA. Translation: AAH05430.1.
U87240 mRNA. Translation: AAC09470.1. Different initiation.
CCDSiCCDS22494.1.
PIRiT42385.
RefSeqiNP_034894.2. NM_010764.2.
UniGeneiMm.4219.

Genome annotation databases

EnsembliENSMUST00000034121; ENSMUSP00000034121; ENSMUSG00000005142.
GeneIDi17159.
KEGGimmu:17159.
UCSCiuc009mpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29947 mRNA. Translation: AAC53369.1 . Different initiation.
AF044192
, AF044174 , AF044175 , AF044176 , AF044177 , AF044178 , AF044179 , AF044180 , AF044181 , AF044182 , AF044183 , AF044184 , AF044185 , AF044186 , AF044187 , AF044188 , AF044189 , AF044190 , AF044191 Genomic DNA. Translation: AAC78560.1 .
AK147928 mRNA. Translation: BAE28235.1 .
AK004817 mRNA. Translation: BAB23588.1 .
BC005430 mRNA. Translation: AAH05430.1 .
U87240 mRNA. Translation: AAC09470.1 . Different initiation.
CCDSi CCDS22494.1.
PIRi T42385.
RefSeqi NP_034894.2. NM_010764.2.
UniGenei Mm.4219.

3D structure databases

ProteinModelPortali O09159.
SMRi O09159. Positions 51-341, 349-421, 431-583, 606-875, 886-1007.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O09159. 2 interactions.
MINTi MINT-1675875.

Protein family/group databases

CAZyi GH38. Glycoside Hydrolase Family 38.

Proteomic databases

MaxQBi O09159.
PaxDbi O09159.
PRIDEi O09159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034121 ; ENSMUSP00000034121 ; ENSMUSG00000005142 .
GeneIDi 17159.
KEGGi mmu:17159.
UCSCi uc009mpk.1. mouse.

Organism-specific databases

CTDi 4125.
MGIi MGI:107286. Man2b1.

Phylogenomic databases

eggNOGi COG0383.
GeneTreei ENSGT00510000046304.
HOGENOMi HOG000007676.
HOVERGENi HBG052391.
InParanoidi O09159.
KOi K12311.
OMAi NMQLTVL.
OrthoDBi EOG786H2P.
TreeFami TF313840.

Miscellaneous databases

ChiTaRSi Man2b1. mouse.
NextBioi 291430.
PROi O09159.
SOURCEi Search...

Gene expression databases

Bgeei O09159.
CleanExi MM_MAN2B1.
Genevestigatori O09159.

Family and domain databases

Gene3Di 1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProi IPR011013. 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 ]
Pfami PF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view ]
SMARTi SM00872. Alpha-mann_mid. 1 hit.
[Graphical view ]
SUPFAMi SSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA."
    Beccari T., Appolloni M.G., Costanzi E., Stinchi S., Stirling J.L., Della Fazia M.A., Servillo G., Viola M.P., Orlacchio A.
    Biochem. J. 327:45-49(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  2. "Promoter characterization and structure of the gene encoding mouse lysosomal alpha-d-mannosidase."
    Stinchi S., Orlacchio A., Costanzi E., Stirling J.L., Menghini A.R., Orlacchio A., Beccari T.
    Mamm. Genome 9:869-873(1998) [PubMed] [Europe PMC] [Abstract]
    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: Lung.
  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: C57BL/6J.
    Tissue: Mammary gland.
  5. "Cloning, expression, purification, and characterization of the murine lysosomal acid alpha-mannosidase."
    Merkle R.K., Zhang Y., Ruest P.J., Lal A., Liao Y.-F., Moremen K.W.
    Biochim. Biophys. Acta 1336:132-146(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-1013.
    Tissue: Liver.

Entry informationi

Entry nameiMA2B1_MOUSE
AccessioniPrimary (citable) accession number: O09159
Secondary accession number(s): O55037
, Q3UGH3, Q64443, Q9DBQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 123 of the entry and version 4 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