LOCUS NP_000519 1011 aa linear PRI 22-OCT-2008
DEFINITION mannosidase, alpha, class 2B, member 1 precursor [Homo sapiens].
ACCESSION NP_000519
VERSION NP_000519.2 GI:51873064
DBSOURCE REFSEQ: accession NM_000528.3
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 1011)
AUTHORS Sbaragli,M., Bibi,L., Pittis,M.G., Balducci,C., Heikinheimo,P.,
Ricci,R., Antuzzi,D., Parini,R., Spaccini,L., Bembi,B. and
Beccari,T.
TITLE Identification and characterization of five novel MAN2B1 mutations
in Italian patients with alpha-mannosidosis
JOURNAL Hum. Mutat. 25 (3), 320 (2005)
PUBMED 15712269
REMARK GeneRIF: 5 new mutations were found in the MAN2B1 gene: c.157G>T,
c.562C>T, c.599A>T, c.293dupA, c.2402G>A (p.E53X, p.R188X, p.H200L,
p.Y99VfsX61, p.G801D). p.H200L could involve the catalytic
mechanism. p.G801D would affect correct folding.
REFERENCE 2 (residues 1 to 1011)
AUTHORS Zhang,H., Li,X.J., Martin,D.B. and Aebersold,R.
TITLE Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry
JOURNAL Nat. Biotechnol. 21 (6), 660-666 (2003)
PUBMED 12754519
REFERENCE 3 (residues 1 to 1011)
AUTHORS Olmez,A., Nilssen,O., Coskun,T. and Klenow,H.
TITLE Alpha-mannosidosis and mutational analysis in a Turkish patient
JOURNAL Turk. J. Pediatr. 45 (1), 46-50 (2003)
PUBMED 12718372
REFERENCE 4 (residues 1 to 1011)
AUTHORS Berg,T., Riise,H.M., Hansen,G.M., Malm,D., Tranebjaerg,L.,
Tollersrud,O.K. and Nilssen,O.
TITLE Spectrum of mutations in alpha-mannosidosis
JOURNAL Am. J. Hum. Genet. 64 (1), 77-88 (1999)
PUBMED 9915946
REFERENCE 5 (residues 1 to 1011)
AUTHORS Gotoda,Y., Wakamatsu,N., Kawai,H., Nishida,Y. and Matsumoto,T.
TITLE Missense and nonsense mutations in the lysosomal alpha-mannosidase
gene (MANB) in severe and mild forms of alpha-mannosidosis
JOURNAL Am. J. Hum. Genet. 63 (4), 1015-1024 (1998)
PUBMED 9758606
REFERENCE 6 (residues 1 to 1011)
AUTHORS Emiliani,C., Martino,S., Stirling,J.L., Maras,B. and Orlacchio,A.
TITLE Partial sequence of the purified protein confirms the identity of
cDNA coding for human lysosomal alpha-mannosidase B
JOURNAL Biochem. J. 305 (PT 2), 363-366 (1995)
PUBMED 7832746
REFERENCE 7 (residues 1 to 1011)
AUTHORS Nebes,V.L. and Schmidt,M.C.
TITLE Human lysosomal alpha-mannosidase: isolation and nucleotide
sequence of the full-length cDNA
JOURNAL Biochem. Biophys. Res. Commun. 200 (1), 239-245 (1994)
PUBMED 8166692
REMARK Erratum:[Biochem Biophys Res Commun 1997 Mar 17;232(2):583]
REFERENCE 8 (residues 1 to 1011)
AUTHORS Kaneda,Y., Hayes,H., Uchida,T., Yoshida,M.C. and Okada,Y.
TITLE Regional assignment of five genes on human chromosome 19
JOURNAL Chromosoma 95 (1), 8-12 (1987)
PUBMED 3034518
REFERENCE 9 (residues 1 to 1011)
AUTHORS Champion,M.J. and Shows,T.B.
TITLE Electrophoretic abnormalities of lysosomal enzymes in mucolipidosis
fibroblast lines
JOURNAL Am. J. Hum. Genet. 29 (2), 149-163 (1977)
PUBMED 848490
REFERENCE 10 (residues 1 to 1011)
AUTHORS Phillips,N.C., Robinson,D. and Winchester,B.G.
TITLE Characterization of human liver alpha-D-mannosidase purified by
affinity chromatography
JOURNAL Biochem. J. 153 (3), 579-587 (1976)
PUBMED 821469
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DB237901.1, BC000736.2 and
BM982008.1.
On Sep 3, 2004 this sequence version replaced gi:10834968.
Summary: This gene encodes an enzyme that hydrolyzes terminal,
non-reducing alpha-D-mannose residues in alpha-D-mannosides. Its
activity is necessary for the catabolism of N-linked carbohydrates
released during glycoprotein turnover and it is member of family 38
of glycosyl hydrolases. The full length protein is processed in two
steps. First, a 49 aa leader sequence is cleaved off and the
remainder of the protein is processed into 3 peptides of 70 kDa, 42
kDa (D) and 13/15 kDa (E). Next, the 70 kDa peptide is further
processed into three peptides (A, B and C). The A, B and C peptides
are disulfide-linked. Defects in this gene have been associated
with lysosomal alpha-mannosidosis. [provided by RefSeq].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..1011
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="19"
/map="19cen-q13.1"
Protein 1..1011
/product="mannosidase, alpha, class 2B, member 1
precursor"
/EC_number="3.2.1.24"
/note="mannosidase, alpha B, lysosomal; lysosomal acid
alpha-mannosidase"
sig_peptide 1..49
/calculated_mol_wt=5049
mat_peptide 50..345
/product="mannosidase, alpha, class 2B, member 1, A
peptide"
/calculated_mol_wt=34257
mat_peptide 346..429
/product="mannosidase, alpha, class 2B, member 1, B
peptide"
/calculated_mol_wt=9578
mat_peptide 430..601
/product="mannosidase, alpha, class 2B, member 1, C
peptide"
/calculated_mol_wt=18886
mat_peptide 602..882
/product="mannosidase, alpha, class 2B, member 1, D
peptide"
/calculated_mol_wt=31575
mat_peptide 883..1011
/product="mannosidase, alpha, class 2B, member 1, E
peptide"
/calculated_mol_wt=14491
CDS 1..1011
/gene="MAN2B1"
/gene_synonym="MANB"
/gene_synonym="LAMAN"
/coded_by="NM_000528.3:77..3112"
/db_xref="CCDS:CCDS32919.1"
/db_xref="GeneID:4125"
/db_xref="HGNC:6826"
/db_xref="HPRD:02007"
/db_xref="MIM:609458"
ORIGIN
1 mgayarasgv cargcldsag pwtmsralrp plpplcffll llaaagarag gyetcptvqp
61 nmlnvhllph thddvgwlkt vdqyfygikn diqhagvqyi ldsvisalla dptrrfiyve
121 iaffsrwwhq qtnatqevvr dlvrqgrlef anggwvmnde aathygaivd qmtlglrfle
181 dtfgndgrpr vawhidpfgh sreqaslfaq mgfdgfffgr ldyqdkwvrm qklemeqvwr
241 astslkppta dlftgvlpng ynpprnlcwd vlcvdqplve dprspeynak elvdyflnva
301 taqgryyrtn htvmtmgsdf qyenanmwfk nldklirlvn aqqakgssvh vlystpacyl
361 welnkanltw svkhddffpy adgphqfwtg yfssrpalkr yerlsynflq vcnqlealvg
421 laanvgpygs gdsaplneam avlqhhdavs gtsrqhvand yarqlaagwg pcevllsnal
481 arlrgfkdhf tfcqqlnisi cplsqtaarf qvivynplgr kvnwmvrlpv segvfvvkdp
541 ngrtvpsdvv ifpssdsqah ppellfsasl palgfstysv aqvprwkpqa rapqpiprrs
601 wspaltiene hiratfdpdt gllmeimnmn qqlllpvrqt ffwynasigd nesdqasgay
661 ifrpnqqkpl pvsrwaqihl vktplvqevh qnfsawcsqv vrlypgqrhl elewsvgpip
721 vgdtwgkevi srfdtpletk grfytdsngr eilerrrdyr ptwklnqtep vagnyypvnt
781 riyitdgnmq ltvltdrsqg gsslrdgsle lmvhrrllkd dgrgvseplm engsgawvrg
841 rhlvlldtaq aaaaghrlla eqevlapqvv lapgggaayn lgapprtqfs glrrdlppsv
901 hlltlaswgp emvllrlehq favgedsgrn lsapvtlnlr dlfstftitr lqettlvanq
961 lreaasrlkw ttntgptphq tpyqldpani tlepmeirtf lasvqwkevd g
//