Epididymis-specific alpha-mannosidase precursor - Pongo abelii (Sumatran orangutan)

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Q5RDJ3 (MA2B2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Epididymis-specific alpha-mannosidase
EC=3.2.1.24

Alternative name(s):
Mannosidase alpha class 2B member 2

Gene names

Name:

MAN2B2

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	1009 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mannose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-mannosidase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

23

Potential

Chain

986

Epididymis-specific alpha-mannosidase

PRO_0000012080

Sites

Active site

1

Nucleophile By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q5RDJ3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 0F25A14EEA5D30C5
Show »

1,009

113,832

        10         20         30         40         50         60 
MGRLYWLPLL APLLLLRPPG VQSAGPIRAF VVPHSHMDVG WVYTVQESMQ AYAANVYTSV 

        70         80         90        100        110        120 
VEELARGQQR RFIAVEQEFF RLWWGGVASD QQKHQVHQLL EEGRLEFVIG GQVMHDEAVT 

       130        140        150        160        170        180 
HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLSSRIDYDL 

       190        200        210        220        230        240 
KAAMQEARGL QFVWRGSPSL SEQEEIFTHI MDQYSYCTPS HIPFSNRSGF YWNGVAIFPK 

       250        260        270        280        290        300 
PPPDGVYPNM SEPVTPANIN LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFA 

       310        320        330        340        350        360 
NMNPLLDHIN SHAAKLGVSV QYATLGDYFR ALHTLNITWR VRDHHDFLPY STEPFQAWTG 

       370        380        390        400        410        420 
FYTSRSALKG LARRASALLY AGESMFTHYM WPAPCGHLDP TWALQQLQQL RWAVSEVQHH 

       430        440        450        460        470        480 
DAITGTESPK VRDMYVMHLA SGMLGVRKLM ASIILDKLQP QAPMAASSGA GPAGHFASVY 

       490        500        510        520        530        540 
NPLAWTVTTI VTLTVGFPGV HVTDEAGHPV PSQIQNSTET PSVYDLLILT TIPGLSYRHY 

       550        560        570        580        590        600 
SIRPTAGAQE GTQEPAATVA TTLQFGRRLR RRTSHVGRHL VPVANDCYTV LLDQDTNLMH 

       610        620        630        640        650        660 
SIWERQSNQT VRVTQEFLEY HVNGDVKQGP ISDNYLFTPG KAAVPAWEAV EMEIVAGQLV 

       670        680        690        700        710        720 
TEIRQYFYRN MTARNYTYAI RSRLTHVPQG HDGELLCHRI EQEYQAGPLE LNREAVLRTS 

       730        740        750        760        770        780 
TNLNSQQVIY SDNNGYQMQR RPYVSYVNNS IARNYYPMVQ SAFMEDGKSR LVLLSERAHG 

       790        800        810        820        830        840 
ISSQGNGQVE VMLHRRLWNN FDWDLGYNLT LNDTSIVHPV LWLLLGSWSL TTALRQRSAM 

       850        860        870        880        890        900 
ALQHRPVVLF GDLAGTAPKL PGPQQQEAVT LPPNLHLQIL SIPGWRYSSN HTEHAQNLRK 

       910        920        930        940        950        960 
GNRGEVQADL HRVLLRLHHL YEVGEDPVLS QPVTVNLEAV LQALGSVVAV EERSLTGTWD 

       970        980        990       1000 
VSMLHRWSWR TGSGRRRGDT TSPSRPPGGP IITVHPKEIR TFFIHFQQQ

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR857915 mRNA. Translation: CAH90164.1.
RefSeq	NP_001125051.1. NM_001131579.1.
UniGene	Pab.7285.
3D structure databases
ProteinModelPortal	Q5RDJ3.
ModBase	Search...
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100171932.
KEGG	pon:100171932.
Organism-specific databases
CTD	23324.
Phylogenomic databases
HOVERGEN	HBG052392.
KO	K12312.
Family and domain databases
Gene3D	2.60.40.1180. 1 hit. 3.20.110.10. 1 hit.
InterPro	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_dom. IPR000602. Glyco_hydro_38_N. [Graphical view]
Pfam	PF09261. Alpha-mann_mid. 1 hit. PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view]
SMART	SM00872. Alpha-mann_mid. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MA2B2_PONAB

Accession

Primary (citable) accession number: Q5RDJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents