MANBA_RAT
ID MANBA_RAT Reviewed; 881 AA.
AC Q4FZV0; Q2NKP5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Beta-mannosidase;
DE EC=3.2.1.25 {ECO:0000250|UniProtKB:Q95327};
DE AltName: Full=Lysosomal beta A mannosidase;
DE AltName: Full=Mannanase;
DE Short=Mannase;
DE Flags: Precursor;
GN Name=Manba {ECO:0000312|RGD:1305785};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC residue from the non-reducing end of all N-linked glycoprotein
CC oligosaccharides. {ECO:0000250|UniProtKB:Q8K2I4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000250|UniProtKB:Q95327};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000250|UniProtKB:Q8K2I4}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8K2I4}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q95327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q4FZV0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q4FZV0-2; Sequence=VSP_052170;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
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DR EMBL; BC099094; AAH99094.1; -; mRNA.
DR EMBL; BC111710; AAI11711.1; -; mRNA.
DR RefSeq; NP_001026825.1; NM_001031655.1. [Q4FZV0-1]
DR AlphaFoldDB; Q4FZV0; -.
DR SMR; Q4FZV0; -.
DR STRING; 10116.ENSRNOP00000018202; -.
DR BindingDB; Q4FZV0; -.
DR ChEMBL; CHEMBL3431; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GlyGen; Q4FZV0; 8 sites.
DR PaxDb; Q4FZV0; -.
DR PRIDE; Q4FZV0; -.
DR Ensembl; ENSRNOT00000087371; ENSRNOP00000072765; ENSRNOG00000052247. [Q4FZV0-1]
DR GeneID; 310864; -.
DR KEGG; rno:310864; -.
DR CTD; 4126; -.
DR RGD; 1305785; Manba.
DR eggNOG; KOG2230; Eukaryota.
DR GeneTree; ENSGT00390000001670; -.
DR HOGENOM; CLU_005015_3_1_1; -.
DR InParanoid; Q4FZV0; -.
DR OMA; KRQWKGP; -.
DR OrthoDB; 517710at2759; -.
DR PhylomeDB; Q4FZV0; -.
DR TreeFam; TF105723; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8853383; Lysosomal oligosaccharide catabolism.
DR SABIO-RK; Q4FZV0; -.
DR UniPathway; UPA00280; -.
DR PRO; PR:Q4FZV0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000052247; Expressed in kidney and 19 other tissues.
DR Genevisible; Q4FZV0; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:RGD.
DR GO; GO:0016787; F:hydrolase activity; ISO:RGD.
DR GO; GO:0005537; F:mannose binding; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041447; Mannosidase_ig.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49303; SSF49303; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Lysosome; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..881
FT /note="Beta-mannosidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250614"
FT ACT_SITE 457
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT ACT_SITE 554
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..176
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT DISULFID 540..629
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT DISULFID 732..761
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT DISULFID 764..769
FT /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT VAR_SEQ 1..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052170"
SQ SEQUENCE 881 AA; 101221 MW; 023E3BE808CE6306 CRC64;
MHLHLLFLLA LCGAGCMAAG PSYSLRGSWR VSNGNSSLEL PATVPGYVHS ALQQHGLIQD
PYYRFNDLNY RWISLDNWTY STEFKIPFNR SEWQKVKLIF DGVDTVAEIL FNNVTIGKTD
NMFTRYSFDV TNVVKDVNSL KLRFQSAVQY AECQSKAHTQ YRVPPECPPV EQKGECHVNF
IRKEQCSFSW DWGPSFPSQG IWKDVRIEAY NIAHLDHLTF LPLYDNTSQA WTIEIEASFD
VVSTKPVGGQ VTIAIPELKT QQANHIELQH GQRIVKLLVK IRKDVTVETW WPHGHGNQTG
YNTTILFALD GGLKIEKAAK VYFRTVQLIE EPITGSPGLS FYFKINGLPI FLKGSNWIPA
DSFQDKVTSE LLQLLLQSAV DANMNTLRVW GGGIYEQDEF YALCDELGIM VWQDFMFASA
LYPTEPGFLE SVRKEVTYQV RRLKSHPSVI IWSGNNENEV ALRVNWFHVN PRDLGTYIND
YVTLYVKTIR EIVLSEDRSR PFIASSPTNG VKTMTEGWIS KDPYSTQYGD MHFYDYFSDC
WDWKVFPKAR LVSEYGYQSW PSFSTLQKVS RQEDWSYSSR FSLHRQHHGN GNNEMLHQVQ
LHFQLPQRRD PVRAFKDTIY LTQVMQAQCI KTETEFYLRS RSEIVNGEGH TMGALYWQLN
DIWQAPSWAS LEYGGKWKML HYFAQRFFAP LLPVGFEDEG VFYVYGVSDL HKDYPTKLTV
RLHRWSSQKP LCTFVSLSAV IKAGEAMVLF QMPVSKLLKR CKECTRDTCV VSFYLSTDNE
LFSPTNYHFL SSLKDAKGMV KANITVSISQ KGDLFVFDLK SSTSAITPFV WLDVGSIPGR
FSDNGFLMIK KELSVLFYPW KPTSKSELQQ AFSVTSLTDL Y
