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Q9C512

- MNS1_ARATH

UniProt

Q9C512 - MNS1_ARATH

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Protein
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
Gene
MNS1, MANIB, At1g51590, F19C24.18, F5D21.1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Class I alpha-mannosidase essential for early N-glycan processing. Progressively trim alpha-1,2-linked mannose residues. Produces Man5GlcNAc2 from Man8GlcNAc2, but only Man6GlcNAc2 from Man9GlcNAc2. Have difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.2 Publications

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.1 Publication

Cofactori

Calcium or manganese. Magnesium can be used to a lesser extent.

Enzyme regulationi

Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine.2 Publications

pH dependencei

Optimum pH is 6.0. Stable from pH 4.5 to 6.5.1 Publication

Temperature dependencei

Optimum temperature is 25 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Proton donor By similarity
Active sitei312 – 3121 By similarity
Active sitei445 – 4451 By similarity

GO - Molecular functioni

  1. alpha-mannosidase activity Source: TAIR
  2. calcium ion binding Source: InterPro
  3. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. N-glycan processing Source: TAIR
  2. root development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Magnesium, Manganese

Enzyme and pathway databases

BioCyciARA:AT1G51590-MONOMER.
ARA:GQT-893-MONOMER.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 (EC:3.2.1.113)
Short name:
AtMANIb
Alternative name(s):
Alpha-mannosidase IB
Gene namesi
Name:MNS1
Synonyms:MANIB
Ordered Locus Names:At1g51590
ORF Names:F19C24.18, F5D21.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G51590.

Subcellular locationi

Golgi apparatus membrane; Single-pass type II membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei28 – 4720Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini48 – 560513Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: TAIR
  2. Golgi membrane Source: UniProtKB-SubCell
  3. endosome Source: TAIR
  4. integral component of membrane Source: UniProtKB-KW
  5. trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype; due the redundancy with MNS2. Lack of complex N-glycans, shorter roots and increased lateral root formation in mns1 and mns2 double mutants.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
PRO_0000397933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi326 – 3261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi377 ↔ 409 By similarity
Glycosylationi459 – 4591N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9C512.
PRIDEiQ9C512.

Expressioni

Tissue specificityi

Expressed in flowers, siliques, stems, leaves, roots, pollen grains, shoot apical meristems, hypocotyls and upper region of the root.2 Publications

Gene expression databases

GenevestigatoriQ9C512.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G51590.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9C512.
SMRiQ9C512. Positions 97-536.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili47 – 8034 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181987.
InParanoidiQ9C512.
KOiK01230.
OMAiLHAWSSY.
PhylomeDBiQ9C512.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9C512-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MARSRSISGY GIWKYLNPAY YLRRPRRLAL LFIVFVSVSM LVWDRINLAR    50
EHEVEVFKLN EEVSRLEQML EELNGGVGNK PLKTLKDAPE DPVDKQRRQK 100
VKEAMIHAWS SYEKYAWGKD ELQPRTKDGT DSFGGLGATM VDSLDTLYIM 150
GLDEQFQKAR EWVASSLDFD KDYDASMFET TIRVVGGLLS AYDLSGDKMF 200
LEKAKDIADR LLPAWNTPTG IPYNIINLRN GNAHNPSWAA GGDSILADSG 250
TEQLEFIALS QRTGDPKYQQ KVEKVITELN KNFPADGLLP IYINPDNANP 300
SYSTTTFGAM GDSFYEYLLK VWVQGNKTSA VKPYRDMWEK SMKGLLSLVK 350
KSTPSSFTYI CEKNGNNLID KMDELACFAP GMLALGASGY GPDEEKKFLS 400
LAGELAWTCY NFYQSTPTKL AGENYFFTAG QDMSVGTSWN ILRPETVESL 450
FYLWRLTGNK TYQEWGWNIF QAFEKNSRVE SGYVGLKDVN TGAKDNKMQS 500
FFLAETLKYL YLLFSPSSVI SLDEWVFNTE AHPLKIVARN DPRKPTIALR 550
QRKFGHQINV 560
Length:560
Mass (Da):63,532
Last modified:June 1, 2001 - v1
Checksum:iBCC20CB9E63020B9
GO
Isoform 2 (identifier: Q9C512-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:456
Mass (Da):51,349
Checksum:i16E3C4590FAFCDFC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104Missing in isoform 2.
VSP_039724Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC024261 Genomic DNA. Translation: AAG52623.1.
AC025294 Genomic DNA. Translation: AAG50876.1.
CP002684 Genomic DNA. Translation: AEE32686.1.
CP002684 Genomic DNA. Translation: AEE32687.1.
AY081353 mRNA. Translation: AAL91242.1.
AY128845 mRNA. Translation: AAM91245.1.
PIRiE96554.
RefSeqiNP_001031171.1. NM_001036094.1. [Q9C512-2]
NP_175570.1. NM_104037.4. [Q9C512-1]
UniGeneiAt.26180.
At.37784.
At.66909.

Genome annotation databases

EnsemblPlantsiAT1G51590.1; AT1G51590.1; AT1G51590. [Q9C512-1]
GeneIDi841584.
KEGGiath:AT1G51590.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC024261 Genomic DNA. Translation: AAG52623.1 .
AC025294 Genomic DNA. Translation: AAG50876.1 .
CP002684 Genomic DNA. Translation: AEE32686.1 .
CP002684 Genomic DNA. Translation: AEE32687.1 .
AY081353 mRNA. Translation: AAL91242.1 .
AY128845 mRNA. Translation: AAM91245.1 .
PIRi E96554.
RefSeqi NP_001031171.1. NM_001036094.1. [Q9C512-2 ]
NP_175570.1. NM_104037.4. [Q9C512-1 ]
UniGenei At.26180.
At.37784.
At.66909.

3D structure databases

ProteinModelPortali Q9C512.
SMRi Q9C512. Positions 97-536.
ModBasei Search...

Protein-protein interaction databases

STRINGi 3702.AT1G51590.1-P.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbi Q9C512.
PRIDEi Q9C512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G51590.1 ; AT1G51590.1 ; AT1G51590 . [Q9C512-1 ]
GeneIDi 841584.
KEGGi ath:AT1G51590.

Organism-specific databases

TAIRi AT1G51590.

Phylogenomic databases

eggNOGi NOG300315.
HOGENOMi HOG000181987.
InParanoidi Q9C512.
KOi K01230.
OMAi LHAWSSY.
PhylomeDBi Q9C512.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci ARA:AT1G51590-MONOMER.
ARA:GQT-893-MONOMER.

Miscellaneous databases

PROi Q9C512.

Gene expression databases

Genevestigatori Q9C512.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Class I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana."
    Liebminger E., Huttner S., Vavra U., Fischl R., Schoberer J., Grass J., Blaukopf C., Seifert G.J., Altmann F., Mach L., Strasser R.
    Plant Cell 21:3850-3867(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
  5. "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
    Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
    Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMNS1_ARATH
AccessioniPrimary (citable) accession number: Q9C512
Secondary accession number(s): Q2V4H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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