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
  • Lysosome
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