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Q29451

- MA2B1_BOVIN

UniProt

Q29451 - MA2B1_BOVIN

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Protein

Lysosomal alpha-mannosidase

Gene

MAN2B1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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

Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Zinc1 Publication
Metal bindingi75 – 751Zinc1 Publication
Active sitei197 – 1971Nucleophile1 Publication
Metal bindingi197 – 1971Zinc1 Publication
Metal bindingi448 – 4481Zinc1 Publication

GO - Molecular functioni

  1. alpha-mannosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. mannose metabolic process Source: InterPro
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
Cleaved into the following 5 chains:
Gene namesi
Name:MAN2B1
Synonyms:MANB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 7

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5050Add
BLAST
Chaini51 – 999949Lysosomal alpha-mannosidasePRO_0000012060Add
BLAST
Chaini51 – 347297Lysosomal alpha-mannosidase A peptidePRO_0000012061Add
BLAST
Chaini348 – 43184Lysosomal alpha-mannosidase B peptidePRO_0000012062Add
BLAST
Chaini432 – 590159Lysosomal alpha-mannosidase C peptidePRO_0000012063Add
BLAST
Propeptidei591 – 62131Sequence AnalysisPRO_0000012064Add
BLAST
Chaini622 – 871250Lysosomal alpha-mannosidase D peptidePRO_0000012065Add
BLAST
Chaini872 – 999128Lysosomal alpha-mannosidase E peptidePRO_0000012066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 360
Glycosylationi134 – 1341N-linked (GlcNAc...)
Disulfide bondi269 ↔ 274
Glycosylationi369 – 3691N-linked (GlcNAc...)
Disulfide bondi414 ↔ 474
Disulfide bondi495 ↔ 503
Glycosylationi499 – 4991N-linked (GlcNAc...)
Glycosylationi634 – 6341N-linked (GlcNAc...)
Glycosylationi640 – 6401N-linked (GlcNAc...)
Glycosylationi681 – 6811N-linked (GlcNAc...)
Glycosylationi755 – 7551N-linked (GlcNAc...)
Glycosylationi919 – 9191N-linked (GlcNAc...)

Post-translational modificationi

Processed into 5 peptides of 35/38 kDa (A), 11/13 kDa (B) and 22 kDa (C), 38 kDa (D) and 13/15 kDa (E). The A, B and C peptides are disulfide-linked into a 67 kDa complex.
Heavily glycosylated. Some sugar chains are of the high-mannose type.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ29451.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008193.

Structurei

Secondary structure

1
999
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 7010
Beta strandi76 – 805
Helixi82 – 876
Turni91 – 933
Helixi98 – 11114
Beta strandi117 – 1193
Helixi122 – 1309
Helixi134 – 14512
Beta strandi148 – 1536
Beta strandi155 – 1573
Beta strandi161 – 1633
Helixi166 – 18419
Helixi185 – 1884
Beta strandi191 – 20010
Helixi203 – 2119
Beta strandi216 – 2205
Helixi224 – 2329
Beta strandi236 – 2416
Beta strandi244 – 2463
Turni248 – 2514
Beta strandi252 – 2576
Helixi290 – 30516
Beta strandi308 – 31710
Helixi326 – 34116
Beta strandi351 – 3555
Helixi358 – 36710
Helixi392 – 3943
Helixi398 – 42023
Helixi436 – 4449
Turni448 – 4525
Helixi457 – 48630
Helixi498 – 5003
Helixi504 – 5085
Beta strandi510 – 5189
Beta strandi520 – 5223
Beta strandi524 – 5329
Beta strandi537 – 5404
Beta strandi542 – 5443
Beta strandi550 – 5534
Turni555 – 5573
Beta strandi560 – 5689
Beta strandi572 – 5809
Beta strandi595 – 5973
Beta strandi599 – 6057
Turni607 – 6093
Beta strandi611 – 6177
Beta strandi623 – 6253
Beta strandi627 – 6359
Beta strandi653 – 6575
Beta strandi659 – 6613
Beta strandi666 – 6716
Beta strandi676 – 6838
Beta strandi686 – 6927
Beta strandi697 – 7059
Beta strandi716 – 7238
Beta strandi731 – 7366
Beta strandi739 – 7457
Beta strandi750 – 7523
Helixi761 – 7633
Beta strandi765 – 77410
Beta strandi776 – 78611
Beta strandi788 – 7903
Beta strandi797 – 8059
Beta strandi811 – 8133
Helixi822 – 8254
Beta strandi826 – 83712
Helixi838 – 85316
Beta strandi857 – 8626
Beta strandi880 – 8834
Beta strandi890 – 8989
Beta strandi901 – 9077
Turni912 – 9198
Beta strandi924 – 9274
Beta strandi929 – 94315
Beta strandi947 – 9504
Helixi951 – 9533
Beta strandi978 – 9814
Beta strandi986 – 9949

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7DX-ray2.70A51-348[»]
B349-432[»]
C433-591[»]
D592-873[»]
E874-999[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29451.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000007676.
HOVERGENiHBG052391.
InParanoidiQ29451.
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.

Q29451-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVGDARPSGV RAGGCRGAVG SRTSSRALRP PLPPLSSLFV LFLAAPCAWA
60 70 80 90 100
AGYKTCPKVK PDMLNVHLVP HTHDDVGWLK TVDQYFYGIY NNIQPAGVQY
110 120 130 140 150
ILDSVISSLL ANPTRRFIYV EIAFFSRWWR QQTNATQKIV RELVRQGRLE
160 170 180 190 200
FANGGWVMND EATTHYGAII DQMTLGLRFL EETFGSDGRP RVAWHIDPFG
210 220 230 240 250
HSREQASLFA QMGFDGFFFG RLDYQDKKVR KKTLQMEQVW RASTSLKPPT
260 270 280 290 300
ADLFTSVLPN MYNPPEGLCW DMLCADKPVV EDTRSPEYNA KELVRYFLKL
310 320 330 340 350
ATDQGKLYRT KHTVMTMGSD FQYENANTWF KNLDKLIQLV NAQQRANGIR
360 370 380 390 400
VNVLYSTPAC YLWELNKANL SWSVKKDDFF PYADGPYMFW TGYFSSRPAL
410 420 430 440 450
KRYERLSYNF LQVCNQLEAL AGPAANVGPY GSGDSAPLNE AMAVLQHHDA
460 470 480 490 500
VSGTSRQHVA NDYARQLSEG WRPCEVLMSN ALAHLSGLKE DFAFCRKLNI
510 520 530 540 550
SICPLTQTAE RFQVIVYNPL GRKVDWMVRL PVSKHVYLVK DPGGKIVPSD
560 570 580 590 600
VVTIPSSDSQ ELLFSALVPA VGFSIYSVSQ MPNQRPQKSW SRDLVIQNEY
610 620 630 640 650
LRARFDPNTG LLMELENLEQ NLLLPVRQAF YWYNASTGNN LSSQASGAYI
660 670 680 690 700
FRPNQNKPLF VSHWAQTHLV KASLVQEVHQ NFSAWCSQVV RLYPRQRHLE
710 720 730 740 750
LEWTVGPIPV GDGWGKEVIS RFDTALATRG LFYTDSNGRE ILERRRNYRP
760 770 780 790 800
TWKLNQTEPV AGNYYPVNSR IYITDGNMQL TVLTDRSQGG SSLRDGSLEL
810 820 830 840 850
MVHRRLLKDD ARGVGEPLNK EGSGLWVRGR HLVLLDKKET AAARHRLQAE
860 870 880 890 900
MEVLAPQVVL AQGGGARYRL EKAPRTQFSG LRRELPPSVR LLTLARWGPE
910 920 930 940 950
TLLLRLEHQF AVGEDSGRNL SSPVTLDLTN LFSAFTITNL RETTLAANQL
960 970 980 990
LAYASRLQWT TDTGPTPHPS PSRPVSATIT LQPMEIRTFL ASVQWEEDG
Length:999
Mass (Da):112,919
Last modified:October 16, 2013 - v4
Checksum:iC86DE7532925DB10
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761G → R in AAB67726. (PubMed:9208932)Curated
Sequence conflicti176 – 1761G → R in AAC48763. (PubMed:9208932)Curated
Sequence conflicti512 – 55039Missing in AAC48763. (PubMed:9208932)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211R → H in AM; Galloway cattle. 1 Publication
Natural varianti321 – 3211F → L in AM; Angus cattle. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31373 mRNA. Translation: AAB67726.2.
U97694
, U97686, U97687, U97688, U97689, U97690, U97691, U97692, U97693 Genomic DNA. Translation: AAC48763.1.
DAAA02019388 Genomic DNA. No translation available.
RefSeqiNP_776986.2. NM_174561.2.
UniGeneiBt.4622.

Genome annotation databases

EnsembliENSBTAT00000008193; ENSBTAP00000008193; ENSBTAG00000006241.
GeneIDi282272.
KEGGibta:282272.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31373 mRNA. Translation: AAB67726.2 .
U97694
, U97686 , U97687 , U97688 , U97689 , U97690 , U97691 , U97692 , U97693 Genomic DNA. Translation: AAC48763.1 .
DAAA02019388 Genomic DNA. No translation available.
RefSeqi NP_776986.2. NM_174561.2.
UniGenei Bt.4622.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O7D X-ray 2.70 A 51-348 [» ]
B 349-432 [» ]
C 433-591 [» ]
D 592-873 [» ]
E 874-999 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000008193.

Chemistry

ChEMBLi CHEMBL1932902.

Protein family/group databases

CAZyi GH38. Glycoside Hydrolase Family 38.

Proteomic databases

PRIDEi Q29451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000008193 ; ENSBTAP00000008193 ; ENSBTAG00000006241 .
GeneIDi 282272.
KEGGi bta:282272.

Organism-specific databases

CTDi 4125.

Phylogenomic databases

eggNOGi COG0383.
GeneTreei ENSGT00510000046304.
HOGENOMi HOG000007676.
HOVERGENi HBG052391.
InParanoidi Q29451.
KOi K12311.
OMAi NMQLTVL.
OrthoDBi EOG786H2P.
TreeFami TF313840.

Miscellaneous databases

EvolutionaryTracei Q29451.
NextBioi 20806083.

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. "Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis."
    Tollersrud O.-K., Berg T., Healy P., Evjen G., Ramachandran U., Nilssen O.
    Eur. J. Biochem. 246:410-419(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS AM HIS-221 AND LEU-321.
    Tissue: Kidney.
  2. Berg T.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 358.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  4. "The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation."
    Heikinheimo P., Helland R., Leiros H.-K.S., Leiros I., Karlsen S., Evjen G., Ravelli R., Schoehn G., Ruigrok R., Tollersrud O.-K., McSweeney S., Hough E.
    J. Mol. Biol. 327:631-644(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-999, COFACTOR, ACTIVE SITE.

Entry informationi

Entry nameiMA2B1_BOVIN
AccessioniPrimary (citable) accession number: Q29451
Secondary accession number(s): F1MMX7, O02848, O19138
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 16, 2013
Last modified: October 29, 2014
This is version 100 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3