ID M1C1_HUMAN STANDARD; PRT; 630 AA. AC Q9NR34; Q9Y545; DT 15-JUN-2002 (Rel. 41, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC (EC 3.2.1.113) DE (Processing alpha-1,2-mannosidase IC) (Alpha-1,2-mannosidase IC) DE (Mannosidase alpha class 1C member 1) (HMIC). GN MAN1C1 OR MAN1A3 OR MAN1C. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain, and Eye; RX MEDLINE=20493536; PubMed=10915796; RA Tremblay L.O., Herscovics A.; RT "Characterization of a cDNA encoding a novel human Golgi alpha 1,2- RT mannosidase involved in N-glycan biosynthesis."; RL J. Biol. Chem. 275:31655-31660(2000). RN [2] RP SEQUENCE OF 17-212 FROM N.A. RA Grafham D.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the maturation of Asn-linked CC oligosaccharides. Trim alpha-1,2-linked mannose residues from CC Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc CC and a small amount of Man(5)GlcNAc. CC -!- CATALYTIC ACTIVITY: Hydrolysis of the terminal 1,2-linked alpha-D- CC mannose residues in the oligo-mannose oligosaccharide CC Man(9)(GlcNAc)(2). CC -!- COFACTOR: Calcium. CC -!- ENZYME REGULATION: Inhibited by both 1-deoxymannojirimycin and CC kifunensine. CC -!- PATHWAY: N-GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: Type II membrane protein. Golgi. CC -!- TISSUE SPECIFICITY: Expressed in most tissues with the exception CC of lung, muscle and pancreas. Highly expressed in placenta. CC -!- SIMILARITY: BELONGS TO FAMILY 47 OF GLYCOSYL HYDROLASES. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF261655; AAF97058.1; -. DR EMBL; AL031280; CAB50704.1; -. DR Genew; HGNC:19080; MAN1C1. DR HSSP; P32906; 1DL2. DR InterPro; IPR001382; GH_47. DR Pfam; PF01532; Glyco_hydro_47; 2. DR PRINTS; PR00747; GLYHDRLASE47. DR ProDom; PD003239; Glyco_hydro_47; 1. KW Hydrolase; Glycosidase; Glycoprotein; Transmembrane; Calcium-binding; KW Signal-anchor; Golgi stack. FT DOMAIN 1 22 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 23 43 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 44 630 LUMENAL (POTENTIAL). FT CARBOHYD 250 250 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 618 618 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 630 AA; 70910 MW; 80FFC71EFB36552A CRC64; MLMRKVPGFV PASPWGLRLP QKFLFLLFLS GLVTLCFGAL FLLPHSSRLK RLFLAPRTQQ PGLEVVAEIA GHAPAREQEP PPNPAPAAPA PGEDDPSSWA SPRRRKGGLR RTRPTGPREE ATAARGNSIP ASRPGDEGVP FRFDFNAFRS RLRHPVLGTR ADESQEPQSQ VRAQREKIKE MMQFAWQSYK RYAMGKNELR PLTKDGYEGN MFGGLSGATV IDSLDTLYLM ELKEEFQEAK AWVGESFHLN VSGEASLFEV NIRYIGGLLS AFYLTGEEVF RIKAIRLGEK LLPAFNTPTG IPKGVVSFKS GNWGWATAGS SSILAEFGSL HLEFLHLTEL SGNQVFAEKV RNIRKVLRKI EKPFGLYPNF LSPVSGNWVQ HHVSVGGLGD SFYEYLIKSW LMSGKTDMEA KNMYYEALEA IETYLLNVSP GGLTYIAEWR GGILDHKMGH LACFSGGMIA LGAEDAKEEK RAHYRELAAQ ITKTCHESYA RSDTKLGPEA FWFNSGREAV ATQLSESYYI LRPEVVESYM YLWRQTHNPI YREWGWEVVL ALEKYCRTEA GFSGIQDVYS STPNHDNKQQ SFFLAETLKY LYLLFSEDDL LSLEDWVFNT EAHPLPVNHS DSSGRAWGRH //