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Protein

Alpha-mannosidase 2

Gene

Man2a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.1 Publication

Catalytic activityi

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.1 Publication

Cofactori

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

Enzyme regulationi

Inhibited by swainsonine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi174 – 1741ZincBy similarity
Metal bindingi176 – 1761ZincBy similarity
Active sitei288 – 2881NucleophileBy similarity
Metal bindingi288 – 2881ZincBy similarity
Metal bindingi568 – 5681ZincBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. mannose metabolic process Source: InterPro
  2. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199013. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase 2 (EC:3.2.1.114)
Alternative name(s):
Golgi alpha-mannosidase II
Short name:
AMan II
Short name:
Man II
Mannosidase alpha class 2A member 1
Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
Gene namesi
Name:Man2a1
Synonyms:Mana2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi3038. Man2a1.

Subcellular locationi

Golgi apparatus membrane 3 Publications; Single-pass type II membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence Analysis
Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 11481122LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11481148Alpha-mannosidase 2PRO_0000206904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineBy similarity
Modified residuei82 – 821PhosphoserineBy similarity
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP28494.
PRIDEiP28494.

PTM databases

PhosphoSiteiP28494.

Expressioni

Tissue specificityi

Liver.2 Publications

Gene expression databases

GenevestigatoriP28494.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Protein-protein interaction databases

IntActiP28494. 1 interaction.
MINTiMINT-4574652.
STRINGi10116.ENSRNOP00000020767.

Structurei

3D structure databases

ProteinModelPortaliP28494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000293253.
HOVERGENiHBG052390.
InParanoidiP28494.
OMAiFFEHVTH.

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.

P28494-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPRGPRQE GSFPQGQLSI
60 70 80 90 100
LQEKIDHLER LLAENNEIIS NIRDSVINLS ESVEDGPRGP AGNASQGSAH
110 120 130 140 150
LHSAQLALQA DPKDCLFASQ SGNQHRDVQM LDVYDLIPFD NPDGGVWKQG
160 170 180 190 200
FDIKYEADEW DREPLQVFVV PHSHNDPGWL KTFNDYFRDK TQYIFNNMVL
210 220 230 240 250
KLKEDSSRKF IWSEISYLAK WWDIIDNPKK EAVKSLLQNG QLEIVTGGWV
260 270 280 290 300
MADEATTHYF ALIDQLIEGH QWLEKNLGVK PRSGWAIDPF GHSPTMTYLL
310 320 330 340 350
KRAGFSHMLI QRVHYSVKKH FSLQKTLEFF WRQNWDLGST TDILCHMMPF
360 370 380 390 400
YSYDIPHTCG PDPKICCQFD FKRLPGGRYG CPWGVPPEAI SPGNVQSRAQ
410 420 430 440 450
MLLDQYRKKS KLFRTKVLLA PLGDDFRFSE YTEWDLQYRN YEQLFSYMNS
460 470 480 490 500
QPHLKVKIQF GTLSDYFDAL EKSVAAEKKG GQSVFPALSG DFFTYADRDD
510 520 530 540 550
HYWSGYFTSR PFYKRMDRIM ESRLRTAEIL YHLALKQAQK YKINKFLSSP
560 570 580 590 600
HYTTLTEARR NLGLFQHHDA ITGTAKDWVV VDYGTRLFQS LNSLEKIIGD
610 620 630 640 650
SAFLLILKDK KLYQSDPSKA FLEMDTKQSS QDSLPKKNII QLSAQEPRYL
660 670 680 690 700
VVYNPFEQER HSVVSVRVNS ATVKVLSDLG KAVEVQVSAV WKDMRTTSQA
710 720 730 740 750
AYEVAFLAHL PPLGLKVYKI LESQSSSSHL ADYFLYNNDG QAESGIFHMK
760 770 780 790 800
NMVDSGDAIT IENSFLTLGF DRSGLMEKVR RKEDNKQQEL KVQFLWYGTT
810 820 830 840 850
NKRDKSGAYL FLPDGQGQPY VSLRTPFVRV TRGRIYSDVT CFLEHVTHKV
860 870 880 890 900
RLYHIQGIEG QSMEVSNIVD IRSVHNREIV MRISSKINNQ NRYYTDLNGY
910 920 930 940 950
QIQPRRTMAK LPLQANVYPM STMAYIQDAA HRLTLLSAQS LGASSMASGQ
960 970 980 990 1000
IEVFMDRRLM QDDNRGLGQG VHDNKITANL FRILLEKRNG MNMEEDKKSP
1010 1020 1030 1040 1050
VSYPSLLSHM TSAFLNHPFL PMVLSGQLPS PAIELLSEFR LLQSSLPCDI
1060 1070 1080 1090 1100
HLVNLRTIQS KVGKGYSDEA ALILHRKVFD CQLSSRAMGL PCSTTQGKMS
1110 1120 1130 1140
IPKLFNNFAV ESFIPSSLSL MHSPPDAQNT SEVSLSPMEI STSRIRLR
Length:1,148
Mass (Da):131,242
Last modified:October 29, 2014 - v2
Checksum:i8FEEAA55D4AD068B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461G → GFSPHIIRVERKG in AAA66457. (PubMed:2748583)
Sequence conflicti157 – 1571A → G AA sequence (PubMed:2246269)Curated
Sequence conflicti160 – 1601W → I AA sequence (PubMed:2246269)Curated
Sequence conflicti244 – 2441I → G AA sequence (PubMed:2246269)Curated
Sequence conflicti247 – 2471G → K AA sequence (PubMed:2246269)Curated
Sequence conflicti493 – 4931F → I AA sequence (PubMed:1885615)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06062074 Genomic DNA. No translation available.
AABR06062075 Genomic DNA. No translation available.
CH473997 Genomic DNA. Translation: EDL91825.1.
M24353 mRNA. Translation: AAA66457.1.
PIRiA33901.
RefSeqiNP_037111.2. NM_012979.2.
UniGeneiRn.163804.

Genome annotation databases

EnsembliENSRNOT00000020767; ENSRNOP00000020767; ENSRNOG00000015439.
GeneIDi25478.
UCSCiRGD:3038. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06062074 Genomic DNA. No translation available.
AABR06062075 Genomic DNA. No translation available.
CH473997 Genomic DNA. Translation: EDL91825.1.
M24353 mRNA. Translation: AAA66457.1.
PIRiA33901.
RefSeqiNP_037111.2. NM_012979.2.
UniGeneiRn.163804.

3D structure databases

ProteinModelPortaliP28494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28494. 1 interaction.
MINTiMINT-4574652.
STRINGi10116.ENSRNOP00000020767.

Chemistry

ChEMBLiCHEMBL2257.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

PTM databases

PhosphoSiteiP28494.

Proteomic databases

PaxDbiP28494.
PRIDEiP28494.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020767; ENSRNOP00000020767; ENSRNOG00000015439.
GeneIDi25478.
UCSCiRGD:3038. rat.

Organism-specific databases

RGDi3038. Man2a1.

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000293253.
HOVERGENiHBG052390.
InParanoidiP28494.
OMAiFFEHVTH.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_199013. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

NextBioi606801.
PROiP28494.

Gene expression databases

GenevestigatoriP28494.

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

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Isolation of a rat liver Golgi mannosidase II clone by mixed oligonucleotide-primed amplification of cDNA."
    Moremen K.W.
    Proc. Natl. Acad. Sci. U.S.A. 86:5276-5280(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-521, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "Mannosidase II and the 135-kDa Golgi-specific antigen recognized monoclonal antibody 53FC3 are the same dimeric protein."
    Baron M.D., Garoff H.
    J. Biol. Chem. 265:19928-19931(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 156-171 AND 243-256, SUBCELLULAR LOCATION, SUBUNIT.
  5. "Novel purification of the catalytic domain of Golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme."
    Moremen K.W., Touster O., Robbins P.W.
    J. Biol. Chem. 266:16876-16885(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 107-136 AND 478-496, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    Strain: Sprague-Dawley.
    Tissue: Liver.

Entry informationi

Entry nameiMA2A1_RAT
AccessioniPrimary (citable) accession number: P28494
Secondary accession number(s): G3V7Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 29, 2014
Last modified: February 4, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.