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Protein

Lysosomal alpha-mannosidase

Gene

MAN2B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi73Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi75ZincCombined sources1 Publication1
Active sitei197Nucleophile1 Publication1
Metal bindingi197ZincCombined sources1 Publication1
Metal bindingi448Zinc; via tele nitrogenCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.1.24. 908.
ReactomeiR-BTA-6798695. Neutrophil degranulation.
R-BTA-8853383. Lysosomal oligosaccharide catabolism.

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
Proteomesi
  • UP000009136 Componentsi: Chromosome 7, Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

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

Chemistry databases

ChEMBLiCHEMBL1932902.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 50Add BLAST50
ChainiPRO_000001206051 – 999Lysosomal alpha-mannosidaseAdd BLAST949
ChainiPRO_000001206151 – 347Lysosomal alpha-mannosidase A peptideAdd BLAST297
ChainiPRO_0000012062348 – 431Lysosomal alpha-mannosidase B peptideAdd BLAST84
ChainiPRO_0000012063432 – 590Lysosomal alpha-mannosidase C peptideAdd BLAST159
PropeptideiPRO_0000012064591 – 621Sequence analysisAdd BLAST31
ChainiPRO_0000012065622 – 871Lysosomal alpha-mannosidase D peptideAdd BLAST250
ChainiPRO_0000012066872 – 999Lysosomal alpha-mannosidase E peptideAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56Interchain (with C-360)Combined sources1 Publication
Glycosylationi134N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi269 ↔ 2741 Publication
Disulfide bondi360Interchain (with C-56)Combined sources1 Publication
Glycosylationi369N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi414Interchain (with C-474)Combined sources1 Publication
Disulfide bondi474Interchain (with C-414)Combined sources1 Publication
Disulfide bondi495 ↔ 5031 Publication
Glycosylationi499N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi634N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi640N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi681N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi755N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi919N-linked (GlcNAc...)PROSITE-ProRule annotation1

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

PaxDbiQ29451.
PRIDEiQ29451.

PTM databases

UniCarbKBiQ29451.

Expressioni

Gene expression databases

BgeeiENSBTAG00000006241.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008193.

Structurei

Secondary structure

1999
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 70Combined sources10
Beta strandi76 – 80Combined sources5
Helixi82 – 87Combined sources6
Turni91 – 93Combined sources3
Helixi98 – 111Combined sources14
Beta strandi117 – 119Combined sources3
Helixi122 – 130Combined sources9
Helixi134 – 145Combined sources12
Beta strandi148 – 153Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi161 – 163Combined sources3
Helixi166 – 184Combined sources19
Helixi185 – 188Combined sources4
Beta strandi191 – 200Combined sources10
Helixi203 – 211Combined sources9
Beta strandi216 – 220Combined sources5
Helixi224 – 232Combined sources9
Beta strandi236 – 241Combined sources6
Beta strandi244 – 246Combined sources3
Turni248 – 251Combined sources4
Beta strandi252 – 257Combined sources6
Helixi290 – 305Combined sources16
Beta strandi308 – 317Combined sources10
Helixi326 – 341Combined sources16
Beta strandi351 – 355Combined sources5
Helixi358 – 367Combined sources10
Helixi392 – 394Combined sources3
Helixi398 – 420Combined sources23
Helixi436 – 444Combined sources9
Turni448 – 452Combined sources5
Helixi457 – 486Combined sources30
Helixi498 – 500Combined sources3
Helixi504 – 508Combined sources5
Beta strandi510 – 518Combined sources9
Beta strandi520 – 522Combined sources3
Beta strandi524 – 532Combined sources9
Beta strandi537 – 540Combined sources4
Beta strandi542 – 544Combined sources3
Beta strandi550 – 553Combined sources4
Turni555 – 557Combined sources3
Beta strandi560 – 568Combined sources9
Beta strandi572 – 580Combined sources9
Beta strandi595 – 597Combined sources3
Beta strandi599 – 605Combined sources7
Turni607 – 609Combined sources3
Beta strandi611 – 617Combined sources7
Beta strandi623 – 625Combined sources3
Beta strandi627 – 635Combined sources9
Beta strandi653 – 657Combined sources5
Beta strandi659 – 661Combined sources3
Beta strandi666 – 671Combined sources6
Beta strandi676 – 683Combined sources8
Beta strandi686 – 692Combined sources7
Beta strandi697 – 705Combined sources9
Beta strandi716 – 723Combined sources8
Beta strandi731 – 736Combined sources6
Beta strandi739 – 745Combined sources7
Beta strandi750 – 752Combined sources3
Helixi761 – 763Combined sources3
Beta strandi765 – 774Combined sources10
Beta strandi776 – 786Combined sources11
Beta strandi788 – 790Combined sources3
Beta strandi797 – 805Combined sources9
Beta strandi811 – 813Combined sources3
Helixi822 – 825Combined sources4
Beta strandi826 – 837Combined sources12
Helixi838 – 853Combined sources16
Beta strandi857 – 862Combined sources6
Beta strandi880 – 883Combined sources4
Beta strandi890 – 898Combined sources9
Beta strandi901 – 907Combined sources7
Turni912 – 919Combined sources8
Beta strandi924 – 927Combined sources4
Beta strandi929 – 943Combined sources15
Beta strandi947 – 950Combined sources4
Helixi951 – 953Combined sources3
Beta strandi978 – 981Combined sources4
Beta strandi986 – 994Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O7DX-ray2.70A51-348[»]
B349-432[»]
C433-591[»]
D592-873[»]
E874-999[»]
SMRiQ29451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29451.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1959. Eukaryota.
ENOG410XQMZ. LUCA.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000007676.
HOVERGENiHBG052391.
InParanoidiQ29451.
KOiK12311.
OMAiPPADEKI.
OrthoDBiEOG091G02IS.
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.
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.
IPR013780. Glyco_hydro_b.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti176G → R in AAB67726 (PubMed:9208932).Curated1
Sequence conflicti176G → R in AAC48763 (PubMed:9208932).Curated1
Sequence conflicti512 – 550Missing in AAC48763 (PubMed:9208932).CuratedAdd BLAST39

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti221R → H in AM; Galloway cattle. 1 Publication1
Natural varianti321F → L in AM; Angus cattle. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O7DX-ray2.70A51-348[»]
B349-432[»]
C433-591[»]
D592-873[»]
E874-999[»]
SMRiQ29451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008193.

Chemistry databases

ChEMBLiCHEMBL1932902.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

PTM databases

UniCarbKBiQ29451.

Proteomic databases

PaxDbiQ29451.
PRIDEiQ29451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4125.

Phylogenomic databases

eggNOGiKOG1959. Eukaryota.
ENOG410XQMZ. LUCA.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000007676.
HOVERGENiHBG052391.
InParanoidiQ29451.
KOiK12311.
OMAiPPADEKI.
OrthoDBiEOG091G02IS.
TreeFamiTF313840.

Enzyme and pathway databases

BRENDAi3.2.1.24. 908.
ReactomeiR-BTA-6798695. Neutrophil degranulation.
R-BTA-8853383. Lysosomal oligosaccharide catabolism.

Miscellaneous databases

EvolutionaryTraceiQ29451.
PROiQ29451.

Gene expression databases

BgeeiENSBTAG00000006241.

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.
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.
IPR013780. Glyco_hydro_b.
[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...

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: November 30, 2016
This is version 116 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

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 one 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.