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P34098 (MANA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal alpha-mannosidase

Short name=Laman
EC=3.2.1.24
Alternative name(s):
Alpha-D-mannoside mannohydrolase
Alpha-mannosidase A
Gene names
Name:manA
ORF Names:DDB_G0292206
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length1010 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Tetramer of equimolar amounts of 60 and 58 kDa subunits.

Subcellular location

Alpha-mannosidase 60 kDa subunit: Lysosome. Note: A few precursors are secreted. The mature 58 and 60 kDa subunits are lysosomal.

Alpha-mannosidase 58 kDa subunit: Lysosome.

Induction

Via a protein termed prestarvation factor which is produced and secreted by both growing and developing cells.

Post-translational modification

First cleaved into the mature 58 kDa subunit and an intermediate 82 kDa subunit. The latter is then cleaved to its mature 60 kDa subunit form. These events occur in multiple intracellular compartments. The 60 kDa subunit may form one or more intramolecular disulfide bonds.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Sequence caution

The sequence AAA33224.1 differs from that shown. Reason: Frameshift at positions 123, 128 and 1001.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4018Pro I Potential
PRO_0000012081
Chain41 – 507467Alpha-mannosidase 60 kDa subunit
PRO_0000012082
Propeptide508 – 59588Pro II Potential
PRO_0000012083
Chain596 – 1010415Alpha-mannosidase 58 kDa subunit
PRO_0000012084

Sites

Active site1731Nucleophile By similarity
Metal binding511Zinc By similarity
Metal binding531Zinc By similarity
Metal binding1731Zinc By similarity
Metal binding4201Zinc By similarity
Site507 – 5082Cleavage; to produce 60 kDa subunit Potential
Site589 – 5902Cleavage; to produce 58 and 82 kDa subunits; alternate Probable
Site593 – 5942Cleavage; to produce 58 and 82 kDa subunits; alternate Probable

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation7601N-linked (GlcNAc...) Potential
Glycosylation7841N-linked (GlcNAc...) Potential
Glycosylation8281N-linked (GlcNAc...) Potential
Glycosylation9541N-linked (GlcNAc...) Potential
Glycosylation9631N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict514 – 5152IP → TL in AAA33224. Ref.1
Sequence conflict9781D → Y in AAA33224. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P34098 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 80C65C941232573F

FASTA1,010113,429
        10         20         30         40         50         60 
MVIKKLFILI FCLFLIINEI NGKKTKINDI KKSKPKLSST LLNVHIVAHT HDDVGWLKTV 

        70         80         90        100        110        120 
DEYYYGSNMS IAFAGVQYTL DTAITCLLAN PERKFIYVEI AFFQRWWDEQ STTMQNIVKG 

       130        140        150        160        170        180 
LVESGQLEFI NGGYCMNDEA TTYYDDTIDQ MTLGHQFLWE NFGVMPKIGW HIDPFGHSAT 

       190        200        210        220        230        240 
QARIFGQLGF DAFIIGRMDY QDIEARLENK QMEFMWRSTQ STPENQVFTS VLRAMYCTPD 

       250        260        270        280        290        300 
GFNFEQGDDP IQDDPNLFDN NVDSRAEQFT QVALEYATHY RTNNVLIPFG CDFAYLNAQM 

       310        320        330        340        350        360 
YYKNIDKLIA HINSNPDKYG LNLLYSTPSI YIDAVNDANL VWEVKTDDLF PYADNEFSYW 

       370        380        390        400        410        420 
TGYFVSRPAL KGYVRQNNAL LHVVEQMLVT SSNLMPSSRS EQLVDDIVIM REVMGIAQHH 

       430        440        450        460        470        480 
DAVSGTEQQH VADDYAERLS IGNCASLETI NTVVGTLLTA NGNSKSAAAT PTISFCPLLN 

       490        500        510        520        530        540 
QSICPATDPL SSGTSVPVLI YNSLSWTRNE PVRIPIPIAN VTVTSSSNGS ITSQVNQING 

       550        560        570        580        590        600 
TFILEFLATI PPLGYSTYII TSTASDFVEP NSIPAIIIQD EIIVSGGGKI NEKVSYNDPI 

       610        620        630        640        650        660 
ILENDYINVQ FSSQDGSILS ITNKTSGVTS SITQEYIWYN PSVGNDDSAQ CSGAYIFRPV 

       670        680        690        700        710        720 
EDFAYPYNNA TPSVSIIRGE ISSSIRRFWS NEMVQTFRLY SNADHLEVEE IIGPIDISDG 

       730        740        750        760        770        780 
IGKEIVSRYT TTLVTDQTWY SDSQGMEMQK RITNYRPSWN LTVVQPTSGN YVPVNAIAYI 

       790        800        810        820        830        840 
QDPNQSLQFT IVTDRSRGCA SLRDGQLDMM MHRRTLKDDG RGVGQPMNES TQIVTTSKLI 

       850        860        870        880        890        900 
FHDISSYAQS HYRPAALSLS HPLLPMFTTT QQSSNDWNSQ YQGVYSPLTS ASPLPNGLKI 

       910        920        930        940        950        960 
QTLQWLDNQD NTILLRIENI YQIDGQDSQD PQTITLDLST IFSTITITSA TEMNLTGVQK 

       970        980        990       1000       1010 
LSNLSRLKWK TVDGKNYDHK SSSSTKEDSS NGFVFTFSPM QIRTFIITTN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the structural gene coding for the developmentally regulated lysosomal enzyme, alpha-mannosidase, in Dictyostelium discoideum."
Schatzle J., Bush J., Cardelli J.
J. Biol. Chem. 267:4000-4007(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 41-63 AND 596-612.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M82822 Genomic DNA. Translation: AAA33224.1. Frameshift.
AAFI02000188 Genomic DNA. Translation: EAL61313.1.
PIRA42265.

3D structure databases

ProteinModelPortalP34098.
SMRP34098. Positions 32-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0201569.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PRIDEP34098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0201569; DDB0201569; DDB_G0292206.
KEGGddi:DDB_G0292206.

Organism-specific databases

dictyBaseDDB_G0292206. manA.

Phylogenomic databases

eggNOGNOG306356.
KOK12311.
OMAITSATEM.
PhylomeDBP34098.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. 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.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

PROP34098.

Entry information

Entry nameMANA_DICDI
AccessionPrimary (citable) accession number: P34098
Secondary accession number(s): Q54DI0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 4, 2007
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase