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Protein

Epididymis-specific alpha-mannosidase

Gene

MAN2B2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361ZincBy similarity
Metal bindingi38 – 381ZincBy similarity
Active sitei151 – 1511NucleophileBy similarity
Metal bindingi151 – 1511ZincBy similarity
Metal bindingi420 – 4201ZincBy similarity

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:
Epididymis-specific alpha-mannosidase (EC:3.2.1.24)
Alternative name(s):
Mannosidase alpha class 2B member 2
Gene namesi
Name:MAN2B2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

  1. Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 1009986Epididymis-specific alpha-mannosidasePRO_0000012080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi516 – 5161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi675 – 6751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi808 – 8081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi812 – 8121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi890 – 8901N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5RDJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052392.
InParanoidiQ5RDJ3.
KOiK12312.

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.

Q5RDJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLYWLPLL APLLLLRPPG VQSAGPIRAF VVPHSHMDVG WVYTVQESMQ
60 70 80 90 100
AYAANVYTSV VEELARGQQR RFIAVEQEFF RLWWGGVASD QQKHQVHQLL
110 120 130 140 150
EEGRLEFVIG GQVMHDEAVT HLDDQILQLT EGHGFLYETF GIRPQFSWHV
160 170 180 190 200
DPFGASATTP TLFALAGFNA HLSSRIDYDL KAAMQEARGL QFVWRGSPSL
210 220 230 240 250
SEQEEIFTHI MDQYSYCTPS HIPFSNRSGF YWNGVAIFPK PPPDGVYPNM
260 270 280 290 300
SEPVTPANIN LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFA
310 320 330 340 350
NMNPLLDHIN SHAAKLGVSV QYATLGDYFR ALHTLNITWR VRDHHDFLPY
360 370 380 390 400
STEPFQAWTG FYTSRSALKG LARRASALLY AGESMFTHYM WPAPCGHLDP
410 420 430 440 450
TWALQQLQQL RWAVSEVQHH DAITGTESPK VRDMYVMHLA SGMLGVRKLM
460 470 480 490 500
ASIILDKLQP QAPMAASSGA GPAGHFASVY NPLAWTVTTI VTLTVGFPGV
510 520 530 540 550
HVTDEAGHPV PSQIQNSTET PSVYDLLILT TIPGLSYRHY SIRPTAGAQE
560 570 580 590 600
GTQEPAATVA TTLQFGRRLR RRTSHVGRHL VPVANDCYTV LLDQDTNLMH
610 620 630 640 650
SIWERQSNQT VRVTQEFLEY HVNGDVKQGP ISDNYLFTPG KAAVPAWEAV
660 670 680 690 700
EMEIVAGQLV TEIRQYFYRN MTARNYTYAI RSRLTHVPQG HDGELLCHRI
710 720 730 740 750
EQEYQAGPLE LNREAVLRTS TNLNSQQVIY SDNNGYQMQR RPYVSYVNNS
760 770 780 790 800
IARNYYPMVQ SAFMEDGKSR LVLLSERAHG ISSQGNGQVE VMLHRRLWNN
810 820 830 840 850
FDWDLGYNLT LNDTSIVHPV LWLLLGSWSL TTALRQRSAM ALQHRPVVLF
860 870 880 890 900
GDLAGTAPKL PGPQQQEAVT LPPNLHLQIL SIPGWRYSSN HTEHAQNLRK
910 920 930 940 950
GNRGEVQADL HRVLLRLHHL YEVGEDPVLS QPVTVNLEAV LQALGSVVAV
960 970 980 990 1000
EERSLTGTWD VSMLHRWSWR TGSGRRRGDT TSPSRPPGGP IITVHPKEIR

TFFIHFQQQ
Length:1,009
Mass (Da):113,832
Last modified:December 21, 2004 - v1
Checksum:i0F25A14EEA5D30C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857915 mRNA. Translation: CAH90164.1.
RefSeqiNP_001125051.1. NM_001131579.1.
UniGeneiPab.7285.

Genome annotation databases

GeneIDi100171932.
KEGGipon:100171932.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857915 mRNA. Translation: CAH90164.1.
RefSeqiNP_001125051.1. NM_001131579.1.
UniGeneiPab.7285.

3D structure databases

ProteinModelPortaliQ5RDJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100171932.
KEGGipon:100171932.

Organism-specific databases

CTDi23324.

Phylogenomic databases

HOVERGENiHBG052392.
InParanoidiQ5RDJ3.
KOiK12312.

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.
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiMA2B2_PONAB
AccessioniPrimary (citable) accession number: Q5RDJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 21, 2004
Last modified: January 7, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.