O09159
Gene name |
Man2b1 (Laman, Man2b, Manb) |
Protein name |
Lysosomal alpha-mannosidase |
Names |
Laman, Lysosomal acid alpha-mannosidase, Mannosidase alpha class 2B member 1, Mannosidase alpha-B |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:17159 |
EC number |
3.2.1.24: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O09159
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O09159-F1 | Predicted | AlphaFoldDB |
55 variants for O09159
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs229798129 | 11 | R>C | No | EVA | |
| rs212026544 | 12 | A>S | No | EVA | |
| rs3388998427 | 15 | G>A | No | EVA | |
| rs3388979462 | 80 | T>I | No | EVA | |
| rs3398920797 | 90 | S>G | No | EVA | |
| rs3399443561 | 112 | P>R | No | EVA | |
| rs3389002283 | 115 | R>L | No | EVA | |
| rs239809986 | 133 | S>N | No | EVA | |
| rs3388998229 | 140 | R>Q | No | EVA | |
| rs3388998291 | 145 | Q>L | No | EVA | |
| rs3388990568 | 150 | F>L | No | EVA | |
| rs3388967466 | 167 | A>T | No | EVA | |
| rs3388998268 | 174 | L>F | No | EVA | |
| rs3388997951 | 201 | S>Y | No | EVA | |
| rs3388949202 | 212 | G>S | No | EVA | |
| rs3389002241 | 242 | S>C | No | EVA | |
| rs3388998020 | 242 | S>R | No | EVA | |
| rs3388991470 | 250 | A>T | No | EVA | |
| rs215544436 | 266 | Y>D | No | EVA | |
| rs230110066 | 291 | T>K | No | EVA | |
| rs3388973954 | 303 | Q>L | No | EVA | |
| rs3389002207 | 320 | F>Y | No | EVA | |
| rs3388985205 | 343 | Q>H | No | EVA | |
| rs13466172 | 344 | V>A | No | EVA | |
| rs3388993837 | 371 | T>I | No | EVA | |
| rs3388993885 | 372 | V>M | No | EVA | |
| rs51646694 | 434 | A>T | No | EVA | |
| rs3388985255 | 452 | T>I | No | EVA | |
| rs3388993893 | 470 | G>E | No | EVA | |
| rs3399443532 | 485 | H>Y | No | EVA | |
| rs238119812 | 541 | H>Q | No | EVA | |
| rs237885175 | 567 | P>L | No | EVA | |
| rs252251572 | 581 | A>T | No | EVA | |
| rs218288944 | 604 | H>R | No | EVA | |
| rs3388998029 | 644 | W>G | No | EVA | |
| rs212252889 | 653 | E>K | No | EVA | |
| rs212252889 | 653 | E>Q | No | EVA | |
| rs3388998009 | 666 | N>K | No | EVA | |
| rs3388993907 | 674 | S>R | No | EVA | |
| rs3388998266 | 697 | W>C | No | EVA | |
| rs3388973944 | 719 | P>S | No | EVA | |
| rs225699258 | 725 | D>E | No | EVA | |
| rs3388994868 | 734 | F>I | No | EVA | |
| rs13466173 | 750 | G>D | No | EVA | |
| rs3389003123 | 762 | P>L | No | EVA | |
| rs3388990552 | 806 | Q>* | No | EVA | |
| rs3388994892 | 810 | L>F | No | EVA | |
| rs3388991433 | 820 | V>I | No | EVA | |
| rs3388998326 | 826 | V>M | No | EVA | |
| rs3388998516 | 881 | H>R | No | EVA | |
| rs3388979465 | 919 | E>K | No | EVA | |
| rs3388997967 | 938 | L>F | No | EVA | |
| rs3388991472 | 953 | Q>H | No | EVA | |
| rs3389003169 | 959 | A>S | No | EVA | |
| rs13466169 | 980 | Y>F | No | EVA |
No associated diseases with O09159
4 regional properties for O09159
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glycoside hydrolase family 38, N-terminal domain | 64 - 381 | IPR000602 |
| domain | Glycosyl hydrolase family 38, C-terminal | 608 - 823 | IPR011682 |
| domain | Glycoside hydrolase family 38, central domain | 386 - 483 | IPR015341 |
| domain | Glycosyl hydrolases family 38, C-terminal beta sandwich domain | 901 - 1002 | IPR041147 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.2.1.24 | Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| lysosomal lumen | The volume enclosed within the lysosomal membrane. |
| lysosome | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-mannosidase activity | Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. |
| mannose binding | Binding to mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| learning or memory | The acquisition and processing of information and/or the storage and retrieval of this information over time. |
| mannose metabolic process | The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. The D-(+)-form is widely distributed in mannans and hemicelluloses and is of major importance in the core oligosaccharide of N-linked oligosaccharides of glycoproteins. |
| oligosaccharide catabolic process | The chemical reactions and pathways resulting in the breakdown of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. |
| protein modification process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGTGPLTSGV | RAGGGNTGWL | WMSSCNLGSP | VLPISFLFWL | LLAAPGARAA | GYKTCPPTKP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GMLNVHLLPH | THDDVGWLKT | VDQYYYGILS | DVQHASVQYI | LDSVVSSLLE | KPTRRFIYVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MAFFSRWWKQ | QTSATQDAVR | NLVRQGRLEF | VNGGWVMNDE | AATHYGAIVD | QMTLGLRFLQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DTFGSDGLPR | VAWHIDPFGH | SREQASLFAQ | MGFDGFFLGR | IDYQDKLNRK | KKLRMEELWR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ASDSLEPPAA | DLFTGVLPNN | YNPPKYLCWD | VLCTDPPVVD | NPRSPEFNAK | TLVNYFLKLA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SSQKGFYRTN | HTVMTMGSDF | HYENANMWFK | NMDKLIRLVN | AQQVNGSLVH | VLYSTPTCYL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WELNKANLTW | TVKEDDFFPY | ADGPHMFWTG | YFSSRPALKR | YERLSYNFLQ | VCNQLEALVG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PEANVGPYGS | GDSAPLQEAM | AVLQHHDAVS | GTARQNVVND | YARQLAAGWG | PCEVLVSNAL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ARLSHYKQNF | SFCRELNISI | CPVSQTSERF | QVTLYNPLGR | KVDQMVRLPV | YEGNFIVKDP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HDKNISSNVV | MVPSYYSETY | QWELLFPASV | PALGFSTYSV | AKMSDLNHQA | HNLLSRPRKH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| KSHHVLVIEN | KYMRATFDSG | TGLLMKIENL | EQNLSLPVSQ | GFFWYNASVG | DEESSQASGA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YIFRPNVGKP | IPVSRWAQIS | LVKTALVQEV | HQNFSAWCSQ | VIRLYKGQRH | LELEWTVGPI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PVRDDWGKEV | ISRFDTPMKT | KGQFFTDSNG | REILKRRDDY | RPTWTLNQTE | PVAGNYYPVN |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TRIYITDGQM | QLTVLTDRSQ | GGSSLQDGSL | ELMVHRRLLV | DDDRGVSEPL | LETDTGDKVR |
| 850 | 860 | 870 | 880 | 890 | 900 |
| GRHLVLLSSV | SDAAARHRLL | AEQEVLAPQV | VLSLGGSSPY | HSRATPKTQF | SGLRQELPPQ |
| 910 | 920 | 930 | 940 | 950 | 960 |
| VHLLTLARWG | PKMLLLRLEH | QFALKEDSDR | NLSSPVTLNV | QNLFQTFTIN | YLQETTLAAN |
| 970 | 980 | 990 | 1000 | 1010 | |
| QPLSRASRLK | WMTNTGPTSY | PEPSKLDPTS | VTLKPMEIRT | FLASVQWQEH | RPA |