Epididymis-specific alpha-mannosidase precursor - Sus scrofa (Pig)

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Q28949 (MA2B2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. 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

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	995 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can digest both p-nitro-phenyl-alpha-D-mannoside and high mannose oligosaccharide (Man(8)-GlcNAc₂). May be involved in sperm maturation. Has a possible role in specific sperm-egg interaction since sperm surface mannosidase acts like a receptor for mannose-containing oligosaccharides located on the zona pellucida.
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. Note: Found at the sperm surface as a 27 kDa fragment.
Tissue specificity	Specific to the caput and corpus of the epididymis.
Post-translational modification	Processed into a 27 kDa fragment localized on the equatorial segment and the apical rim of the head of mature sperm.
Sequence similarities	Belongs to the glycosyl hydrolase 38 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5.
Sequence caution	The sequence BAA05877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing 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

21

Chain

974

Epididymis-specific alpha-mannosidase

PRO_0000012079

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

Experimental info

Sequence conflict

1

D → A AA sequence Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q28949 [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: 79D21B8CE5AE6FC2
Show »

995

114,230

        10         20         30         40         50         60 
MGPHSWLPLF MQLALLGPQW ALHFYKVKVF VVPHSHMDVG WLHTVQESMQ VYVPDVYNSV 

        70         80         90        100        110        120 
VEALTRGKRR RFIAVEQEYF RLWWDGFASA KRKQQVRQLL AEQRLEFVLG GQVMHDEAVT 

       130        140        150        160        170        180 
HFDDQILQLT EGHGFLYETF GIRPQFSWQV DPFGASATTP TLLALAGFNG HIISRIDYDL 

       190        200        210        220        230        240 
KDTMQHTQGL QFVWRGSRSL EARQEIFTHV LDQYSYCSDG FMWNGSPRFP DRPFDMDYSA 

       250        260        270        280        290        300 
VEMPVSQDSM NHYVLNLVDN VNKRAAWFRT QHVLWPWGCD RQFFNASQQF ANMDRLMDHI 

       310        320        330        340        350        360 
NKHTPELGIS MQYATLAEYF QAVFAQDVSW QVRDHRDFLP YSSAPEQTWT GFYTSQSGLK 

       370        380        390        400        410        420 
RLARRASALL YAGESLFTRY MLSAAHRFLD PAWALTQLQQ LRWAVSEVQH HDGITGTHIL 

       430        440        450        460        470        480 
AVRDMFVEHL TTGMAGVRKL MDSIAQDMPL THSGPEPGGH VAMVYNPLAW TVTTVITLTV 

       490        500        510        520        530        540 
SFPEVSVTDE SGRPVLAQVQ DSKETPSAYD LHVLTTIPGL SYQHYIIKPI RKAREDSQEA 

       550        560        570        580        590        600 
AATVPSTIQF GLKLRRQDGQ VGRNLVPVKN SCYTVFLDKD TNLMHSIWER QSNRTVRMSQ 

       610        620        630        640        650        660 
EFLAYRSVYG YEEAVTSDNY LFTPNGTAEP AWAAVRMEVV EGQLLSEIRQ YFYRQANDSD 

       670        680        690        700        710        720 
HTYAIYSRLA HGPQDSAGEL LCHRIEQEYR VGPLELNHEV VLRTSTSLNT GLVLYSDNNG 

       730        740        750        760        770        780 
YQMQRRTYRH DRNNSVSLNY YPMAQSAFIQ DGGSRLVLLS EQAHGVSSQG NGQVEVMLHR 

       790        800        810        820        830        840 
RLWNKLEWTL QYNLTHDVTS VVRPVLWLLL GPRTLTTGLR QRSGLELQHR PVVLFRELGG 

       850        860        870        880        890        900 
TVQNGPGPRK QEPVTLPPSL HLQILSIPGW KYSSNHTVHL KNLQKGHYRR AKADFRRVLL 

       910        920        930        940        950        960 
RLHHLYEAGE HQALSRPVTL NLQSVLRGLG SVVAVEERSL TGTWDVNSLH RWSWKTEDGH 

       970        980        990 
HHRGSSRRPL PPLRGPNVTI HPKEIRTFFI HFQEQ

References

[1]

"Cloning of complementary DNA encoding a 135-kilodalton protein secreted from porcine corpus epididymis and its identification as an epididymis-specific alpha-mannosidase."
Okamura N., Tamba M., Liao H.-J., Onoe S., Sugita Y., Dacheux F., Dacheux J.-L.
Mol. Reprod. Dev. 42:141-148(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Epididymis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D28521 mRNA. Translation: BAA05877.1. Different initiation.
PIR	T42762.
RefSeq	NP_999014.1. NM_213849.1.
UniGene	Ssc.14529.
3D structure databases
ProteinModelPortal	Q28949.
ModBase	Search...
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396847.
KEGG	ssc:396847.
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_PIG

Accession

Primary (citable) accession number: Q28949

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 16, 2001
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 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