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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC

Gene

MAN1C1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce first Man8GlcNAc2 then Man6GlcNAc and a small amount of Man5GlcNAc.

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine.

Pathwayi

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. post-translational protein modification Source: Reactome
  3. protein N-linked glycosylation Source: UniProtKB
  4. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.2.1.113. 2681.
ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC (EC:3.2.1.113)
Alternative name(s):
HMIC
Mannosidase alpha class 1C member 1
Processing alpha-1,2-mannosidase IC
Short name:
Alpha-1,2-mannosidase IC
Gene namesi
Name:MAN1C1
Synonyms:MAN1A3, MAN1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19080. MAN1C1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei23 – 4321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini44 – 630587LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. Golgi membrane Source: Reactome
  3. integral component of Golgi membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38788.

Polymorphism and mutation databases

BioMutaiMAN1C1.
DMDMi17369308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630Mannosyl-oligosaccharide 1,2-alpha-mannosidase ICPRO_0000210315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641Phosphoserine1 Publication
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi618 – 6181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NR34.
PaxDbiQ9NR34.
PRIDEiQ9NR34.

PTM databases

PhosphoSiteiQ9NR34.

Expressioni

Tissue specificityi

Expressed in most tissues with the exception of lung, muscle and pancreas. Highly expressed in placenta.

Gene expression databases

BgeeiQ9NR34.
CleanExiHS_MAN1C1.
ExpressionAtlasiQ9NR34. baseline and differential.
GenevestigatoriQ9NR34.

Organism-specific databases

HPAiHPA048352.

Interactioni

Protein-protein interaction databases

BioGridi121395. 1 interaction.
IntActiQ9NR34. 1 interaction.
MINTiMINT-1187619.
STRINGi9606.ENSP00000363452.

Structurei

3D structure databases

ProteinModelPortaliQ9NR34.
SMRiQ9NR34. Positions 163-617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
GeneTreeiENSGT00390000016529.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiQ9NR34.
KOiK01230.
OMAiRSWGWAM.
OrthoDBiEOG7X0VH1.
PhylomeDBiQ9NR34.
TreeFamiTF313420.

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.

Sequencei

Sequence statusi: Complete.

Q9NR34-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMRKVPGFV PASPWGLRLP QKFLFLLFLS GLVTLCFGAL FLLPHSSRLK
60 70 80 90 100
RLFLAPRTQQ PGLEVVAEIA GHAPAREQEP PPNPAPAAPA PGEDDPSSWA
110 120 130 140 150
SPRRRKGGLR RTRPTGPREE ATAARGNSIP ASRPGDEGVP FRFDFNAFRS
160 170 180 190 200
RLRHPVLGTR ADESQEPQSQ VRAQREKIKE MMQFAWQSYK RYAMGKNELR
210 220 230 240 250
PLTKDGYEGN MFGGLSGATV IDSLDTLYLM ELKEEFQEAK AWVGESFHLN
260 270 280 290 300
VSGEASLFEV NIRYIGGLLS AFYLTGEEVF RIKAIRLGEK LLPAFNTPTG
310 320 330 340 350
IPKGVVSFKS GNWGWATAGS SSILAEFGSL HLEFLHLTEL SGNQVFAEKV
360 370 380 390 400
RNIRKVLRKI EKPFGLYPNF LSPVSGNWVQ HHVSVGGLGD SFYEYLIKSW
410 420 430 440 450
LMSGKTDMEA KNMYYEALEA IETYLLNVSP GGLTYIAEWR GGILDHKMGH
460 470 480 490 500
LACFSGGMIA LGAEDAKEEK RAHYRELAAQ ITKTCHESYA RSDTKLGPEA
510 520 530 540 550
FWFNSGREAV ATQLSESYYI LRPEVVESYM YLWRQTHNPI YREWGWEVVL
560 570 580 590 600
ALEKYCRTEA GFSGIQDVYS STPNHDNKQQ SFFLAETLKY LYLLFSEDDL
610 620 630
LSLEDWVFNT EAHPLPVNHS DSSGRAWGRH
Length:630
Mass (Da):70,911
Last modified:October 1, 2000 - v1
Checksum:i80FFC71EFB36552A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261655 mRNA. Translation: AAF97058.1.
AL031280, AL020996 Genomic DNA. Translation: CAI19714.1.
BC137017 mRNA. Translation: AAI37018.1.
CCDSiCCDS265.1.
RefSeqiNP_001275939.1. NM_001289010.1.
NP_065112.1. NM_020379.3.
UniGeneiHs.197043.

Genome annotation databases

EnsembliENST00000374332; ENSP00000363452; ENSG00000117643.
GeneIDi57134.
KEGGihsa:57134.
UCSCiuc001bkm.2. human.

Polymorphism and mutation databases

BioMutaiMAN1C1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261655 mRNA. Translation: AAF97058.1.
AL031280, AL020996 Genomic DNA. Translation: CAI19714.1.
BC137017 mRNA. Translation: AAI37018.1.
CCDSiCCDS265.1.
RefSeqiNP_001275939.1. NM_001289010.1.
NP_065112.1. NM_020379.3.
UniGeneiHs.197043.

3D structure databases

ProteinModelPortaliQ9NR34.
SMRiQ9NR34. Positions 163-617.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121395. 1 interaction.
IntActiQ9NR34. 1 interaction.
MINTiMINT-1187619.
STRINGi9606.ENSP00000363452.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteiQ9NR34.

Polymorphism and mutation databases

BioMutaiMAN1C1.
DMDMi17369308.

Proteomic databases

MaxQBiQ9NR34.
PaxDbiQ9NR34.
PRIDEiQ9NR34.

Protocols and materials databases

DNASUi57134.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374332; ENSP00000363452; ENSG00000117643.
GeneIDi57134.
KEGGihsa:57134.
UCSCiuc001bkm.2. human.

Organism-specific databases

CTDi57134.
GeneCardsiGC01P025943.
HGNCiHGNC:19080. MAN1C1.
HPAiHPA048352.
neXtProtiNX_Q9NR34.
PharmGKBiPA38788.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300315.
GeneTreeiENSGT00390000016529.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiQ9NR34.
KOiK01230.
OMAiRSWGWAM.
OrthoDBiEOG7X0VH1.
PhylomeDBiQ9NR34.
TreeFamiTF313420.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.113. 2681.
ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

Miscellaneous databases

ChiTaRSiMAN1C1. human.
GenomeRNAii57134.
NextBioi63051.
PROiQ9NR34.

Gene expression databases

BgeeiQ9NR34.
CleanExiHS_MAN1C1.
ExpressionAtlasiQ9NR34. baseline and differential.
GenevestigatoriQ9NR34.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a cDNA encoding a novel human Golgi alpha 1,2-mannosidase involved in N-glycan biosynthesis."
    Tremblay L.O., Herscovics A.
    J. Biol. Chem. 275:31655-31660(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Eye.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMA1C1_HUMAN
AccessioniPrimary (citable) accession number: Q9NR34
Secondary accession number(s): A6NNE2, B2RNP2, Q9Y545
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.