Q9NR34 (MA1C1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MAN1C1
Synonyms:	MAN1A3, MAN1C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Cofactor	Calcium.
Enzyme regulation	Inhibited by both 1-deoxymannojirimycin and kifunensine.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Expressed in most tissues with the exception of lung, muscle and pancreas. Highly expressed in placenta.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular component	integral to Golgi membrane Traceable author statement Ref.1. Source: UniProtKB
Molecular function	calcium ion binding Traceable author statement Ref.1. Source: UniProtKB mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 630	630	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC		PRO_0000210315
Regions
	Topological domain	1 – 22	22	Cytoplasmic Potential
	Transmembrane	23 – 43	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	44 – 630	587	Lumenal Potential
Amino acid modifications
	Modified residue	132	1	Phosphoserine Ref.4
	Glycosylation	250	1	N-linked (GlcNAc...) Potential
	Glycosylation	618	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9NR34 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 80FFC71EFB36552A	FASTA	630	70,911
	10 20 30 40 50 60 MLMRKVPGFV PASPWGLRLP QKFLFLLFLS GLVTLCFGAL FLLPHSSRLK RLFLAPRTQQ 70 80 90 100 110 120 PGLEVVAEIA GHAPAREQEP PPNPAPAAPA PGEDDPSSWA SPRRRKGGLR RTRPTGPREE 130 140 150 160 170 180 ATAARGNSIP ASRPGDEGVP FRFDFNAFRS RLRHPVLGTR ADESQEPQSQ VRAQREKIKE 190 200 210 220 230 240 MMQFAWQSYK RYAMGKNELR PLTKDGYEGN MFGGLSGATV IDSLDTLYLM ELKEEFQEAK 250 260 270 280 290 300 AWVGESFHLN VSGEASLFEV NIRYIGGLLS AFYLTGEEVF RIKAIRLGEK LLPAFNTPTG 310 320 330 340 350 360 IPKGVVSFKS GNWGWATAGS SSILAEFGSL HLEFLHLTEL SGNQVFAEKV RNIRKVLRKI 370 380 390 400 410 420 EKPFGLYPNF LSPVSGNWVQ HHVSVGGLGD SFYEYLIKSW LMSGKTDMEA KNMYYEALEA 430 440 450 460 470 480 IETYLLNVSP GGLTYIAEWR GGILDHKMGH LACFSGGMIA LGAEDAKEEK RAHYRELAAQ 490 500 510 520 530 540 ITKTCHESYA RSDTKLGPEA FWFNSGREAV ATQLSESYYI LRPEVVESYM YLWRQTHNPI 550 560 570 580 590 600 YREWGWEVVL ALEKYCRTEA GFSGIQDVYS STPNHDNKQQ SFFLAETLKY LYLLFSEDDL 610 620 630 LSLEDWVFNT EAHPLPVNHS DSSGRAWGRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10915796] [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: 16710414] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF261655 mRNA. Translation: AAF97058.1. AL031280, AL020996 Genomic DNA. Translation: CAI19714.1. BC137017 mRNA. Translation: AAI37018.1.
IPI	IPI00745251.
RefSeq	NP_065112.1. NM_020379.2.
UniGene	Hs.197043.
3D structure databases
ProteinModelPortal	Q9NR34.
SMR	Q9NR34. Positions 163-617.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1187619.
STRING	Q9NR34.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
PTM databases
PhosphoSite	Q9NR34.
Polymorphism databases
DMDM	17369308.
Proteomic databases
PRIDE	Q9NR34.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374332; ENSP00000363452; ENSG00000117643.
GeneID	57134.
KEGG	hsa:57134.
UCSC	uc001bkm.2. human.
Organism-specific databases
CTD	57134.
GeneCards	GC01P025943.
H-InvDB	HIX0199919.
HGNC	HGNC:19080. MAN1C1.
neXtProt	NX_Q9NR34.
PharmGKB	PA38788.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05788.
GeneTree	ENSGT00390000016529.
HOGENOM	HBG559734.
HOVERGEN	HBG052389.
InParanoid	Q9NR34.
OMA	SGSWGWA.
OrthoDB	EOG45QHDB.
PhylomeDB	Q9NR34.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9NR34.
Bgee	Q9NR34.
CleanEx	HS_MAN1C1.
Genevestigator	Q9NR34.
GermOnline	ENSG00000117643. Homo sapiens.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
KO	K01230.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...
Other
NextBio	63051.

Entry information

Entry name

MA1C1_HUMAN

Accession

Primary (citable) accession number: Q9NR34
Secondary accession number(s): A6NNE2, B2RNP2, Q9Y545

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.