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P14410

- SUIS_HUMAN

UniProt

P14410 - SUIS_HUMAN

Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 6 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.1 Publication

    Catalytic activityi

    Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei264 – 2641Substrate
    Binding sitei388 – 3881Substrate
    Active sitei505 – 5051Nucleophile; for isomaltase activity1 PublicationPROSITE-ProRule annotation
    Binding sitei588 – 5881Substrate
    Active sitei604 – 6041For isomaltase activity1 Publication
    Binding sitei662 – 6621Substrate
    Active sitei1394 – 13941Nucleophile; for sucrase activity1 PublicationPROSITE-ProRule annotation
    Active sitei1397 – 13971For sucrase activityBy similarity
    Active sitei1500 – 15001Proton donor; for isomaltase activityBy similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: Reactome
    2. carbohydrate binding Source: InterPro
    3. oligo-1,6-glucosidase activity Source: UniProtKB-EC
    4. sucrose alpha-glucosidase activity Source: Reactome

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. polysaccharide digestion Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01688-MONOMER.
    BRENDAi3.2.1.10. 2681.
    ReactomeiREACT_9472. Digestion of dietary carbohydrate.

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sucrase-isomaltase, intestinal
    Cleaved into the following 2 chains:
    Gene namesi
    Name:SI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10856. SI.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. brush border Source: ProtInc
    3. Golgi apparatus Source: ProtInc
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]: Autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti117 – 1171Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 Publication
    VAR_025368
    Natural varianti341 – 3411L → P in CSID; causes loss of anchored SI from the membrane. 1 Publication
    VAR_025370
    Natural varianti577 – 5771V → G in CSID. 1 Publication
    Corresponds to variant rs121912615 [ dbSNP | Ensembl ].
    VAR_025371
    Natural varianti594 – 5941S → P in CSID. 1 Publication
    VAR_025372
    Natural varianti620 – 6201L → P in CSID; SI accumulates predominantly in the ER. 1 Publication
    VAR_025373
    Natural varianti694 – 6941T → P in CSID. 1 Publication
    VAR_025374
    Natural varianti1073 – 10731G → D in CSID. 1 Publication
    VAR_025375
    Natural varianti1098 – 10981Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 Publication
    VAR_007854
    Natural varianti1229 – 12291C → Y in CSID. 1 Publication
    VAR_025376
    Natural varianti1367 – 13671R → G in CSID. 1 Publication
    VAR_025377
    Natural varianti1745 – 17451F → C in CSID. 1 Publication
    Corresponds to variant rs79717168 [ dbSNP | Ensembl ].
    VAR_025379

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi222900. phenotype.
    Orphaneti306446. Congenital sucrase-isomaltase deficiency with minimal starch tolerance.
    306474. Congenital sucrase-isomaltase deficiency with starch and lactose intolerance.
    306436. Congenital sucrase-isomaltase deficiency with starch intolerance.
    306462. Congenital sucrase-isomaltase deficiency without starch intolerance.
    306486. Congenital sucrase-isomaltase deficiency without sucrose intolerance.
    PharmGKBiPA35758.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 18271826Sucrase-isomaltase, intestinalPRO_0000018551Add
    BLAST
    Chaini2 – 10071006IsomaltasePRO_0000018552Add
    BLAST
    Chaini1008 – 1827820SucrasePRO_0000018553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphoserine; by PKA1 Publication
    Disulfide bondi63 ↔ 941 PublicationPROSITE-ProRule annotation
    Disulfide bondi77 ↔ 931 PublicationPROSITE-ProRule annotation
    Disulfide bondi88 ↔ 1061 PublicationPROSITE-ProRule annotation
    Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
    Modified residuei237 – 2371SulfotyrosineSequence Analysis
    Modified residuei239 – 2391SulfotyrosineSequence Analysis
    Modified residuei391 – 3911SulfotyrosineSequence Analysis
    Modified residuei400 – 4001SulfotyrosineSequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi455 – 4551N-linked (GlcNAc...)1 Publication
    Disulfide bondi520 ↔ 5451 PublicationPROSITE-ProRule annotation
    Disulfide bondi635 ↔ 6461 PublicationPROSITE-ProRule annotation
    Modified residuei667 – 6671SulfotyrosineSequence Analysis
    Modified residuei763 – 7631SulfotyrosineSequence Analysis
    Modified residuei765 – 7651SulfotyrosineSequence Analysis
    Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi855 – 8551N-linked (GlcNAc...)1 Publication
    Glycosylationi904 – 9041N-linked (GlcNAc...)1 Publication
    Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1303 – 13031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1403 – 14031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1535 – 15351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1572 – 15721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1748 – 17481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1815 – 18151N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
    Sulfated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    MaxQBiP14410.
    PaxDbiP14410.
    PRIDEiP14410.

    PTM databases

    PhosphoSiteiP14410.

    Expressioni

    Tissue specificityi

    Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon.1 Publication

    Gene expression databases

    ArrayExpressiP14410.
    BgeeiP14410.
    CleanExiHS_SI.
    GenevestigatoriP14410.

    Organism-specific databases

    HPAiHPA011897.

    Interactioni

    Subunit structurei

    The resulting sucrase and isomaltase subunits stay associated with one another in a complex by non-covalent linkages.1 Publication

    Protein-protein interaction databases

    MINTiMINT-4998644.
    STRINGi9606.ENSP00000264382.

    Structurei

    Secondary structure

    1
    1827
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi65 – 684
    Helixi71 – 733
    Beta strandi75 – 773
    Helixi85 – 917
    Beta strandi99 – 1035
    Beta strandi105 – 1073
    Beta strandi114 – 1218
    Beta strandi123 – 13210
    Beta strandi138 – 1403
    Beta strandi144 – 15411
    Beta strandi157 – 1637
    Beta strandi175 – 1773
    Beta strandi189 – 1957
    Turni196 – 1994
    Beta strandi200 – 2056
    Turni206 – 2094
    Beta strandi210 – 2145
    Helixi215 – 2173
    Beta strandi221 – 2233
    Beta strandi226 – 2327
    Beta strandi234 – 2363
    Beta strandi238 – 2447
    Beta strandi247 – 2504
    Beta strandi254 – 2618
    Beta strandi278 – 2847
    Beta strandi291 – 2966
    Beta strandi302 – 3076
    Turni308 – 3103
    Beta strandi311 – 3199
    Beta strandi321 – 33010
    Helixi331 – 34212
    Helixi350 – 3534
    Helixi365 – 37713
    Beta strandi384 – 3874
    Helixi389 – 3913
    Helixi393 – 3953
    Turni402 – 4076
    Helixi408 – 41710
    Beta strandi421 – 4266
    Helixi442 – 4509
    Beta strandi459 – 4624
    Beta strandi465 – 4673
    Beta strandi470 – 4734
    Helixi480 – 49617
    Beta strandi500 – 5045
    Turni507 – 5093
    Beta strandi512 – 5154
    Turni524 – 5263
    Helixi535 – 5373
    Turni539 – 5424
    Helixi555 – 5584
    Helixi559 – 5613
    Helixi562 – 57716
    Beta strandi585 – 5884
    Helixi594 – 5963
    Beta strandi599 – 6013
    Beta strandi606 – 6083
    Helixi609 – 62416
    Beta strandi629 – 6313
    Beta strandi637 – 6393
    Helixi643 – 65311
    Beta strandi656 – 6583
    Helixi672 – 6754
    Helixi680 – 69415
    Helixi696 – 70914
    Beta strandi713 – 7153
    Helixi718 – 7214
    Helixi725 – 7295
    Beta strandi732 – 7365
    Turni737 – 7393
    Beta strandi740 – 7434
    Beta strandi751 – 7577
    Beta strandi762 – 7643
    Turni765 – 7673
    Beta strandi775 – 7817
    Beta strandi788 – 7925
    Beta strandi795 – 8006
    Helixi806 – 8094
    Beta strandi814 – 8196
    Beta strandi824 – 8329
    Beta strandi835 – 8373
    Helixi840 – 8434
    Beta strandi846 – 8549
    Beta strandi857 – 8659
    Helixi868 – 8725
    Beta strandi874 – 8829
    Beta strandi890 – 8945
    Beta strandi900 – 9023
    Beta strandi905 – 9084
    Turni909 – 9124
    Beta strandi913 – 9164
    Beta strandi927 – 9304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LPOX-ray3.20A/B/C/D62-931[»]
    3LPPX-ray2.15A/B/C/D62-931[»]
    ProteinModelPortaliP14410.
    SMRiP14410. Positions 62-931, 937-1818.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14410.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicAdd
    BLAST
    Topological domaini33 – 18271795LumenalAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 11050P-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini932 – 97847P-type 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1007898IsomaltaseAdd
    BLAST
    Regioni1008 – 1827820SucraseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi43 – 6018Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated
    Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000067936.
    HOVERGENiHBG080721.
    InParanoidiP14410.
    KOiK01203.
    OMAiKYHKNDM.
    OrthoDBiEOG7FJGZS.
    PhylomeDBiP14410.
    TreeFamiTF314577.

    Family and domain databases

    Gene3Di4.10.110.10. 2 hits.
    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000519. P_trefoil.
    IPR017957. P_trefoil_CS.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 2 hits.
    PF00088. Trefoil. 2 hits.
    [Graphical view]
    SMARTiSM00018. PD. 2 hits.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 4 hits.
    SSF57492. SSF57492. 1 hit.
    SSF74650. SSF74650. 2 hits.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
    PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
    PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14410-1 [UniParc]FASTAAdd to Basket

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    MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT     50
    TRVTTNPSDS GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND 100
    SLIPWCFFVD NHGYNVQDMT TTSIGVEAKL NRIPSPTLFG NDINSVLFTT 150
    QNQTPNRFRF KITDPNNRRY EVPHQYVKEF TGPTVSDTLY DVKVAQNPFS 200
    IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG IGEQVHKRFR 250
    HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN 300
    AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY 350
    WNLGFQLSRW NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY 400
    DQVAFNGLPQ FVQDLHDHGQ KYVIILDPAI SIGRRANGTT YATYERGNTQ 450
    HVWINESDGS TPIIGEVWPG LTVYPDFTNP NCIDWWANEC SIFHQEVQYD 500
    GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY SKTICMDAVQ 550
    NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH 600
    WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM 650
    QLGAFYPFSR NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY 700
    TLFYKAHVFG ETVARPVLHE FYEDTNSWIE DTEFLWGPAL LITPVLKQGA 750
    DTVSAYIPDA IWYDYESGAK RPWRKQRVDM YLPADKIGLH LRGGYIIPIQ 800
    EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT IQNGNYILYT 850
    FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN 900
    AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA 950
    TEQKCTQRGC VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ 1000
    LNTANARIKL PSDPISTLRV EVKYHKNDML QFKIYDPQKK RYEVPVPLNI 1050
    PTTPISTYED RLYDVEIKEN PFGIQIRRRS SGRVIWDSWL PGFAFNDQFI 1100
    QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP GYKLNSYGFH 1150
    PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP 1200
    TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN 1250
    IPYDVQYTDI DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI 1300
    SGNETKTYPA FERGQQNDVF VKWPNTNDIC WAKVWPDLPN ITIDKTLTED 1350
    EAVNASRAHV AFPDFFRTST AEWWAREIVD FYNEKMKFDG LWIDMNEPSS 1400
    FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA EQILSDGTSV 1450
    LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD 1500
    NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA 1550
    FYPYSRNHNI ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI 1600
    HANGGTVIRP LLHEFFDEKP TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY 1650
    VPNARWFDYH TGKDIGVRGQ FQTFNASYDT INLHVRGGHI LPCQEPAQNT 1700
    FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY LSVQFNLNQT 1750
    TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE 1800
    DTTNMILRID LTTHNVTLEE PIEINWS 1827
    Length:1,827
    Mass (Da):209,453
    Last modified:January 11, 2011 - v6
    Checksum:iDCB93F068AEEF83E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3001N → D in AAI16453. (PubMed:15489334)Curated
    Sequence conflicti460 – 4601S → I in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti475 – 4751P → S in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti548 – 5481A → V in AAI16453. (PubMed:15489334)Curated
    Sequence conflicti584 – 5841F → L in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti588 – 5881R → C in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti633 – 6331D → A in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti687 – 6871Q → R in AAI16453. (PubMed:15489334)Curated
    Sequence conflicti884 – 8841T → A in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti1016 – 10161S → E AA sequence (PubMed:1677636)Curated
    Sequence conflicti1022 – 10221V → T AA sequence (PubMed:1677636)Curated
    Sequence conflicti1155 – 11551A → V in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti1203 – 12031E → Q in CAA45140. (PubMed:1353958)Curated
    Sequence conflicti1782 – 17821V → I in AAI15035. (PubMed:15489334)Curated
    Sequence conflicti1825 – 18251N → S in AAI16453. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151V → F.4 Publications
    Corresponds to variant rs9290264 [ dbSNP | Ensembl ].
    VAR_025367
    Natural varianti117 – 1171Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 Publication
    VAR_025368
    Natural varianti231 – 2311T → A.5 Publications
    Corresponds to variant rs9283633 [ dbSNP | Ensembl ].
    VAR_025369
    Natural varianti341 – 3411L → P in CSID; causes loss of anchored SI from the membrane. 1 Publication
    VAR_025370
    Natural varianti577 – 5771V → G in CSID. 1 Publication
    Corresponds to variant rs121912615 [ dbSNP | Ensembl ].
    VAR_025371
    Natural varianti594 – 5941S → P in CSID. 1 Publication
    VAR_025372
    Natural varianti620 – 6201L → P in CSID; SI accumulates predominantly in the ER. 1 Publication
    VAR_025373
    Natural varianti694 – 6941T → P in CSID. 1 Publication
    VAR_025374
    Natural varianti1073 – 10731G → D in CSID. 1 Publication
    VAR_025375
    Natural varianti1098 – 10981Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 Publication
    VAR_007854
    Natural varianti1229 – 12291C → Y in CSID. 1 Publication
    VAR_025376
    Natural varianti1367 – 13671R → G in CSID. 1 Publication
    VAR_025377
    Natural varianti1523 – 15231M → I.3 Publications
    Corresponds to variant rs4855271 [ dbSNP | Ensembl ].
    VAR_025378
    Natural varianti1745 – 17451F → C in CSID. 1 Publication
    Corresponds to variant rs79717168 [ dbSNP | Ensembl ].
    VAR_025379
    Natural varianti1802 – 18021T → S.
    Corresponds to variant rs9917722 [ dbSNP | Ensembl ].
    VAR_034522

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63597 mRNA. Translation: CAA45140.1.
    AC092695 Genomic DNA. No translation available.
    AC140119 Genomic DNA. No translation available.
    AC144561 Genomic DNA. No translation available.
    BC115034 mRNA. Translation: AAI15035.1.
    BC116452 mRNA. Translation: AAI16453.1.
    BC132834 mRNA. Translation: AAI32835.1.
    BC132860 mRNA. Translation: AAI32861.1.
    M22616 mRNA. Translation: AAA60551.1.
    CCDSiCCDS3196.1.
    PIRiS36082. UUHU.
    RefSeqiNP_001032.2. NM_001041.3.
    UniGeneiHs.429596.

    Genome annotation databases

    EnsembliENST00000264382; ENSP00000264382; ENSG00000090402.
    GeneIDi6476.
    KEGGihsa:6476.
    UCSCiuc003fei.3. human.

    Polymorphism databases

    DMDMi317373594.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63597 mRNA. Translation: CAA45140.1 .
    AC092695 Genomic DNA. No translation available.
    AC140119 Genomic DNA. No translation available.
    AC144561 Genomic DNA. No translation available.
    BC115034 mRNA. Translation: AAI15035.1 .
    BC116452 mRNA. Translation: AAI16453.1 .
    BC132834 mRNA. Translation: AAI32835.1 .
    BC132860 mRNA. Translation: AAI32861.1 .
    M22616 mRNA. Translation: AAA60551.1 .
    CCDSi CCDS3196.1.
    PIRi S36082. UUHU.
    RefSeqi NP_001032.2. NM_001041.3.
    UniGenei Hs.429596.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LPO X-ray 3.20 A/B/C/D 62-931 [» ]
    3LPP X-ray 2.15 A/B/C/D 62-931 [» ]
    ProteinModelPortali P14410.
    SMRi P14410. Positions 62-931, 937-1818.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4998644.
    STRINGi 9606.ENSP00000264382.

    Chemistry

    BindingDBi P14410.
    ChEMBLi CHEMBL2748.
    DrugBanki DB00284. Acarbose.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    PTM databases

    PhosphoSitei P14410.

    Polymorphism databases

    DMDMi 317373594.

    Proteomic databases

    MaxQBi P14410.
    PaxDbi P14410.
    PRIDEi P14410.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264382 ; ENSP00000264382 ; ENSG00000090402 .
    GeneIDi 6476.
    KEGGi hsa:6476.
    UCSCi uc003fei.3. human.

    Organism-specific databases

    CTDi 6476.
    GeneCardsi GC03M164696.
    H-InvDB HIX0030867.
    HGNCi HGNC:10856. SI.
    HPAi HPA011897.
    MIMi 222900. phenotype.
    609845. gene.
    neXtProti NX_P14410.
    Orphaneti 306446. Congenital sucrase-isomaltase deficiency with minimal starch tolerance.
    306474. Congenital sucrase-isomaltase deficiency with starch and lactose intolerance.
    306436. Congenital sucrase-isomaltase deficiency with starch intolerance.
    306462. Congenital sucrase-isomaltase deficiency without starch intolerance.
    306486. Congenital sucrase-isomaltase deficiency without sucrose intolerance.
    PharmGKBi PA35758.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000067936.
    HOVERGENi HBG080721.
    InParanoidi P14410.
    KOi K01203.
    OMAi KYHKNDM.
    OrthoDBi EOG7FJGZS.
    PhylomeDBi P14410.
    TreeFami TF314577.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01688-MONOMER.
    BRENDAi 3.2.1.10. 2681.
    Reactomei REACT_9472. Digestion of dietary carbohydrate.

    Miscellaneous databases

    EvolutionaryTracei P14410.
    GenomeRNAii 6476.
    NextBioi 25157.
    PROi P14410.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14410.
    Bgeei P14410.
    CleanExi HS_SI.
    Genevestigatori P14410.

    Family and domain databases

    Gene3Di 4.10.110.10. 2 hits.
    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000519. P_trefoil.
    IPR017957. P_trefoil_CS.
    [Graphical view ]
    Pfami PF01055. Glyco_hydro_31. 2 hits.
    PF00088. Trefoil. 2 hits.
    [Graphical view ]
    SMARTi SM00018. PD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 4 hits.
    SSF57492. SSF57492. 1 hit.
    SSF74650. SSF74650. 2 hits.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
    PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
    PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase."
      Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N., Edwards Y., Swallow D., Rousset M.
      Biochem. J. 285:915-923(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-231 AND ILE-1523.
      Tissue: Intestine.
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PHE-15; ALA-231 AND ILE-1523.
    4. "Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3."
      Green F., Edwards Y., Hauri H.-P., Povey S., Ho M.W., Pinto M., Swallow D.
      Gene 57:101-110(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-679, VARIANT ALA-231.
    5. "Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon."
      Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.
      Gastroenterology 101:618-625(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20 AND 1008-1024, TISSUE SPECIFICITY, VARIANT PHE-15.
    6. "Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase by cAMP-dependent protein kinase."
      Keller P., Semenza G., Shaltiel S.
      Eur. J. Biochem. 233:963-968(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-7.
    7. "Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains."
      Sim L., Willemsma C., Mohan S., Naim H.Y., Pinto B.M., Rose D.R.
      J. Biol. Chem. 285:17763-17770(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 62-931 ALONE AND IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-99; ASN-455; ASN-855 AND ASN-904, FUNCTION, ACTIVE SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.
    8. "Congenital sucrase-isomaltase deficiency: identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment."
      Ouwendijk J., Moolenaar C.E.C., Peters W.J., Hollenberg C.P., Ginsel L.A., Fransen J.A.M., Naim H.Y.
      J. Clin. Invest. 97:633-641(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CSID PRO-1098.
    9. "Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme."
      Jacob R., Zimmer K.P., Schmitz J., Naim H.Y.
      J. Clin. Invest. 106:281-287(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CSID PRO-341, CHARACTERIZATION OF VARIANT CSID PRO-341.
    10. "Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder."
      Spodsberg N., Jacob R., Alfalah M., Zimmer K.P., Naim H.Y.
      J. Biol. Chem. 276:23506-23510(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CSID ARG-117, CHARACTERIZATION OF VARIANT CSID ARG-117.
    11. "Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum."
      Ritz V., Alfalah M., Zimmer K.P., Schmitz J., Jacob R., Naim H.Y.
      Gastroenterology 125:1678-1685(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PHE-15 AND ALA-231, VARIANT CSID PRO-620.
    12. "Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption."
      Sander P., Alfalah M., Keiser M., Korponay-Szabo I., Kovacs J.B., Leeb T., Naim H.Y.
      Hum. Mutat. 27:119-119(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CSID GLY-577; PRO-594; PRO-694; ASP-1073; TYR-1229; GLY-1367 AND CYS-1745, VARIANTS PHE-15; ALA-231 AND ILE-1523.

    Entry informationi

    Entry nameiSUIS_HUMAN
    AccessioniPrimary (citable) accession number: P14410
    Secondary accession number(s): A2RUC3, Q1JQ80, Q1RMC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 156 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    There is a high degree of homology between the isomaltase and sucrase portions (41% of amino acid identity) indicating that this protein is evolved by partial gene duplication.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3