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O62653

- SUIS_SUNMU

UniProt

O62653 - SUIS_SUNMU

Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Suncus murinus (Asian house shrew) (Musk shrew)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 By similarity.By similarity

    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 sitei250 – 2501SubstrateBy similarity
    Binding sitei374 – 3741SubstrateBy similarity
    Active sitei491 – 4911Nucleophile; for isomaltase activityPROSITE-ProRule annotation
    Binding sitei574 – 5741SubstrateBy similarity
    Active sitei590 – 5901For isomaltase activityBy similarity
    Binding sitei648 – 6481SubstrateBy similarity
    Active sitei1380 – 13801Nucleophile; for sucrase activityPROSITE-ProRule annotation
    Active sitei1383 – 13831For sucrase activityBy similarity
    Active sitei1486 – 14861Proton donor; for sucrase activityBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    SABIO-RKO62653.

    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
    OrganismiSuncus murinus (Asian house shrew) (Musk shrew)
    Taxonomic identifieri9378 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaInsectivoraSoricidaeCrocidurinaeSuncus

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 18131812Sucrase-isomaltase, intestinalPRO_0000018562Add
    BLAST
    Chaini2 – 991990IsomaltaseBy similarityPRO_0000018563Add
    BLAST
    Chaini992 – 1813822SucraseBy similarityPRO_0000018564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphoserine; by PKABy similarity
    Disulfide bondi48 ↔ 79PROSITE-ProRule annotation
    Disulfide bondi62 ↔ 78PROSITE-ProRule annotation
    Disulfide bondi73 ↔ 91PROSITE-ProRule annotation
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Modified residuei377 – 3771SulfotyrosineSequence Analysis
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi506 ↔ 531PROSITE-ProRule annotation
    Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
    Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi896 – 8961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi911 – 9111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1221 – 12211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1289 – 12891N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1294 – 12941SulfotyrosineSequence Analysis
    Glycosylationi1326 – 13261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1368 – 13681SulfotyrosineSequence Analysis
    Modified residuei1371 – 13711SulfotyrosineSequence Analysis
    Glycosylationi1432 – 14321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1521 – 15211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1545 – 15451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1558 – 15581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1703 – 17031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1772 – 17721N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliO62653.
    SMRiO62653. Positions 56-917.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 18131781LumenalSequence AnalysisAdd
    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
    Domaini46 – 9550P-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 96246P-type 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 991897IsomaltaseAdd
    BLAST
    Regioni992 – 1813822SucraseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 454Ser/Thr-rich

    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

    HOVERGENiHBG080721.

    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.
    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.

    O62653-1 [UniParc]FASTAAdd to Basket

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    MARKKSSGLK ITLIVLLAIV TIIAIALVAI LPTKTPAVEL VSTIPGKCPS     50
    AENDRLDEKI NCIPDQFPTQ ALCAMQGCCW NPRNESPTPW CSFANNHGYE 100
    FEKISNPNIN FEPNLKKNSP PTLFGDNITN LLLTTQSQTA NRFRFKITDP 150
    NNQRYEVPHQ FVNKDFSGPP ASNPLYDVKI TENPFSIKVI RKSNNKILFD 200
    TSIGPLVYSN QYLQISTKLP SKYIYGLGEH VHKRFRHDLY WKTWPIFTRD 250
    QLPGDNNNNL YGHQTFFMSI EDTSGKSFGV FLMNSNAMEV FIQPTPIVTY 300
    RVIGGILDFY IFLGDTPGQV VQQYQELTGR PAMPSYWSLG FQLSRWNYGS 350
    LDAVKEVVKR NRDARIPFDA QVTDIDYMED KKDFTYNNKT FYGLPEFVKD 400
    LHDHGQKYII ILDPAISITS LANGNHYKTY ERGNEQKVWV YQSDGTTPLI 450
    GEVWPGLTVY PDFTNPKCLD WWTNECSIFH EEIKYDGLWI DMNEVSSFVH 500
    GSTKGCSDNK LNYPPFIPDI LDKLMYAKTI CMDAIQHWGK QYDVHSLYGY 550
    SMAIATEKAI EKVFPNKRSF ILTRSTFAGT GKHATHWLGD NTPSWEHMEW 600
    SITPMLEFGL FGMPFIGADI CGFVVDTTEE LCRRWMQIGA FYPYFRDHNA 650
    GGYMPQDPAY FGQDSLLVNT SRHYLDIWYT LLPYLYNLLY KAYVYGETVA 700
    RPFLYEFYED TNSWIEDLQF LWGSALLITP VLRQGADRMS AYIPDATWYD 750
    YETGGKRTWR KQRVEMYLPG DKIGLHVRGG YIIPTQQPAV NTTASRKNPL 800
    GLIIALDNNA AKGDFFWDDG ESKDSIEKGK YILYTFSVLN NELDIICTHS 850
    SYQEGTTLAF ETIKILGLAN TVTQVQVAEN NQQTIIHNSF TYHASNQSLI 900
    IDNLKLNLGK NFTVQWNQVS LDSEKIDCFP DNNPENKQNC EERGCLWEPN 950
    SAAEGPRCYF PKQYNPYLVK STQYSSMGIT VDLELNTATA RIKMPSNPIS 1000
    VLRLEVKYHK NDMLQFKIYD PQNKRYEVPI PMDIPTTPTS TYENRLYDVN 1050
    IKGNPFGIQI RRRSTGRIFW DSCLPWGLLL MNQFIQISTR LPSEYVYGFG 1100
    GVGHRQFKQD LNWHKWGMFN RDQPSGYKIS SYGFQPYIYM ALGDGGNAHG 1150
    VFLLNSNAMD VTFQPNPALT YRTIGGILDF YMFLGPNPEV ATKQYHEVIG 1200
    RPVKPPYWAL GFHLCRYGYE NTSEIRQLYE DMVSAQIPYD VQYTDIDYME 1250
    RQLDFTIGKG FQDLPEFVDK IRDEGMKYII ILDPAISGNE TQDYLAFQRG 1300
    IEKDVFVKWP NTQDICWAKV WPDLPNITID DSLTEDEAVN ASRAHVAFPD 1350
    FLKTSTAEWW ATEIEDFYNT YMKFDGLWID MNEPSSFVHG SVDNKCRNEI 1400
    LNYPPYMPAL TKRNEGLHFR TMCMETQQTL SNGSSVLHYD VHNLYGWSQA 1450
    KPTYDALQKT TGKRGIVISR STYPSAGRWA GHWLGDNYAN WDKIGKSIIG 1500
    MMEFSLFGIS FTGADICGFF NNSDYELCAR WMQVGAFYPY SRNHNITDTR 1550
    RQDPVSWNET FASMSTDILN IRYNLLPYFY TQMHDIHANG GTVIRPLLHE 1600
    FFSETGTWDI YKQFLWGPAF MVTPVVEPYS ESVTGYVPDG RWLDYHTGQD 1650
    IGLRKRLHTL DAPLYKINLH VCGGHILPCQ EPAQNTYFSR QNYMKLIVAA 1700
    DDNQTAQGYL FWDDGESIDT YEKGQYLLVQ FNLNKATLTS TILKNGYINT 1750
    REMRLGFINV WGKGNTVVQE VNITYKGNKE SVKFSQEANK QILNIDLTAN 1800
    NIVLDEPIEI SWT 1813
    Length:1,813
    Mass (Da):208,305
    Last modified:January 23, 2007 - v3
    Checksum:i93DAE1B3952C7AD6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011401 mRNA. Translation: BAA25370.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011401 mRNA. Translation: BAA25370.1 .

    3D structure databases

    ProteinModelPortali O62653.
    SMRi O62653. Positions 56-917.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG080721.

    Enzyme and pathway databases

    SABIO-RK O62653.

    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.
    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. "Molecular cloning of sucrase-isomaltase cDNA in the house musk shrew Suncus murinus and identification of a mutation responsible for isolated sucrase deficiency."
      Ito T., Hayashi Y., Ohmori S., Oda S., Seo H.
      J. Biol. Chem. 273:16464-16469(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiSUIS_SUNMU
    AccessioniPrimary (citable) accession number: O62653
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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

    Multifunctional enzyme

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3