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P23739

- SUIS_RAT

UniProt

P23739 - SUIS_RAT

Protein

Sucrase-isomaltase, intestinal

Gene

Si

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 5 (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.

    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 sitei274 – 2741SubstrateBy similarity
    Binding sitei398 – 3981SubstrateBy similarity
    Active sitei514 – 5141Nucleophile; for isomaltase activityPROSITE-ProRule annotation
    Binding sitei599 – 5991SubstrateBy similarity
    Active sitei615 – 6151For isomaltase activityBy similarity
    Binding sitei673 – 6731SubstrateBy similarity
    Active sitei1399 – 13991Nucleophile; for sucrase activityPROSITE-ProRule annotation
    Active sitei1402 – 14021For sucrase activityBy similarity
    Active sitei1512 – 15121Proton donor; for sucrase activityBy similarity

    GO - Molecular functioni

    1. beta-fructofuranosidase activity Source: RGD
    2. carbohydrate binding Source: InterPro
    3. oligo-1,6-glucosidase activity Source: RGD
    4. protein binding Source: RGD
    5. sucrose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. aging Source: RGD
    2. carbohydrate metabolic process Source: InterPro
    3. response to fructose Source: RGD
    4. response to glucocorticoid Source: RGD
    5. response to insulin Source: RGD
    6. response to nutrient Source: RGD
    7. response to starvation Source: RGD
    8. response to sucrose Source: RGD
    9. response to vitamin A Source: RGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.10. 5301.
    SABIO-RKP23739.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3675. Si.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. brush border Source: RGD
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane raft Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 18411840Sucrase-isomaltase, intestinalPRO_0000018559Add
    BLAST
    Chaini2 – 10131012IsomaltasePRO_0000018560Add
    BLAST
    Chaini1014 – 1841828SucrasePRO_0000018561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphoserine; by PKABy similarity
    Disulfide bondi73 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi87 ↔ 103PROSITE-ProRule annotation
    Disulfide bondi98 ↔ 116PROSITE-ProRule annotation
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Modified residuei401 – 4011SulfotyrosineSequence Analysis
    Modified residuei410 – 4101SulfotyrosineSequence Analysis
    Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi646 ↔ 657PROSITE-ProRule annotation
    Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi867 – 8671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi910 – 9101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1240 – 12401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1308 – 13081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1345 – 13451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1359 – 13591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1373 – 13731N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1387 – 13871SulfotyrosineSequence Analysis
    Glycosylationi1485 – 14851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1513 – 15131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1575 – 15751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1762 – 17621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1829 – 18291N-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

    PRIDEiP23739.

    PTM databases

    PhosphoSiteiP23739.

    Expressioni

    Gene expression databases

    GenevestigatoriP23739.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000045106.

    Structurei

    3D structure databases

    ProteinModelPortaliP23739.
    SMRiP23739. Positions 83-937.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 18411809LumenalSequence 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
    Domaini71 – 12050P-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini936 – 98449P-type 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni120 – 1013894IsomaltaseAdd
    BLAST
    Regioni1014 – 1841828SucraseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi43 – 7028Ser/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.
    KOiK01203.
    PhylomeDBiP23739.

    Family and domain databases

    Gene3Di4.10.110.10. 1 hit.
    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. 1 hit.
    [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. 1 hit.
    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.

    P23739-1 [UniParc]FASTAAdd to Basket

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    MAKKKFSALE ISLIVLFIIV TAIAIALVTV LATKVPAVEE IKSPTPTSNS     50
    TPTSTPTSTS TPTSTSTPSP GKCPPEQGEP INERINCIPE QHPTKAICEE 100
    RGCCWRPWNN TVIPWCFFAD NHGYNAESIT NENAGLKATL NRIPSPTLFG 150
    EDIKSVILTT QTQTGNRFRF KITDPNNKRY EVPHQFVKEE TGIPAADTLY 200
    DVQVSENPFS IKVIRKSNNK VLCDTSVGPL LYSNQYLQIS TRLPSEYIYG 250
    FGGHIHKRFR HDLYWKTWPI FTRDEIPGDN NHNLYGHQTF FMGIGDTSGK 300
    SYGVFLMNSN AMEVFIQPTP IITYRVTGGI LDFYIFLGDT PEQVVQQYQE 350
    VHWRPAMPAY WNLGFQLSRW NYGSLDTVSE VVRRNREAGI PYDAQVTDID 400
    YMEDHKEFTY DRVKFNGLPE FAQDLHNHGK YIIILDPAIS INKRANGAEY 450
    QTYVRGNEKN VWVNESDGTT PLIGEVWPGL TVYPDFTNPQ TIEWWANECN 500
    LFHQQVEYDG LWIDMNEVSS FIQGSLNLKG VLLIVLNYPP FTPGILDKVM 550
    YSKTLCMDAV QHWGKQYDVH SLYGYSMAIA TEQAVERVFP NKRSFILTRS 600
    TFGGSGRHAN HWLGDNTASW EQMEWSITGM LEFGIFGMPL VGATSCGFLA 650
    DTTEELCRRW MQLGAFYPFS RNHNAEGYME QDPAYFGQDS SRHYLTIRYT 700
    LLPFLYTLFY RAHMFGETVA RPFLYEFYDD TNSWIEDTQF LWGPALLITP 750
    VLRPGVENVS AYIPNATWYD YETGIKRPWR KERINMYLPG DKIGLHLRGG 800
    YIIPTQEPDV TTTASRKNPL GLIVALDDNQ AAKGELFWDD GESKDSIEKK 850
    MYILYTFSVS NNELVLNCTH SSYAEGTSLA FKTIKVLGLR EDVRSITVGE 900
    NDQQMATHTN FTFDSANKIL SITALNFNLA GSFIVRWCRT FSDNEKFTCY 950
    PDVGTATEGT CTQRGCLWQP VSGLSNVPPY YFPPENNPYT LTSIQPLPTG 1000
    ITAELQLNPP NARIKLPSNP ISTLRVGVKY HPNDMLQFKI YDAQHKRYEV 1050
    PVPLNIPDTP TSSNERLYDV EIKENPFGIQ VRRRSSGKLI WDSRLPGFGF 1100
    NDQFIQISTR LPSNYLYGFG EVEHTAFKRD LNWHTWGMFT RDQPPGYKLN 1150
    SYGFHPYYMA LENEGNAHGV LLLNSNGMDV TFQPTPALTY RTIGGILDFY 1200
    MFLGPTPEIA TRQYHEVIGF PVMPPYWALG FQLCRYGYRN TSEIEQLYND 1250
    MVAANIPYDV QYTDINYMER QLDFTIGERF KTLPEFVDRI RKDGMKYIVI 1300
    LAPAISGNET QPYPAFERGI QKDVFVKWPN TNDICWPKVW PDLPNVTIDE 1350
    TITEDEAVNA SRAHVAFPDF FRNSTLEWWA REIYDFYNEK MKFDGLWIDM 1400
    NEPSSFGIQM GGKVLNECRR MMTLNYPPVF SPELRVKEGE GASISEAMCM 1450
    ETEHILIDGS SVLQYDVHNL YGWSQVKPTL DALQNTTGLR GIVISRSTYP 1500
    TTGRWGGHWL GDNYTTWDNL EKSLIGMLEL NLFGIPYIGA DICGVFHDSG 1550
    YPSLYFVGIQ VGAFYPYPRE SPTINFTRSQ DPVSWMKLLL QMSKKVLEIR 1600
    YTLLPYFYTQ MHEAHAHGGT VIRPLMHEFF DDKETWEIYK QFLWGPAFMV 1650
    TPVVEPFRTS VTGYVPKARW FDYHTGADIK LKGILHTFSA PFDTINLHVR 1700
    GGYILPCQEP ARNTHLSRQN YMKLIVAADD NQMAQGTLFG DDGESIDTYE 1750
    RGQYTSIQFN LNQTTLTSTV LANGYKNKQE MRLGSIHIWG KGTLRISNAN 1800
    LVYGGRKHQP PFTQEEAKET LIFDLKNMNV TLDEPIQITW S 1841
    Length:1,841
    Mass (Da):210,350
    Last modified:January 23, 2007 - v5
    Checksum:iE186B8632475EE09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871C → W in AAA65097. (PubMed:7821806)Curated
    Sequence conflicti92 – 921H → S in AAA42144. (PubMed:2268340)Curated
    Sequence conflicti95 – 951K → Q in AAA42144. (PubMed:2268340)Curated
    Sequence conflicti736 – 7361E → V in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti842 – 8421E → Q in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti916 – 9161A → T in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti924 – 9241A → R in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti930 – 9312AG → GT in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti938 – 9392CR → SQ in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti959 – 9624GTCT → ETDK in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti980 – 9801Y → C in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti986 – 9861N → H in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti997 – 9982LP → SL in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1010 – 10101P → A in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1023 – 10231T → P in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1027 – 10271G → E in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1032 – 10321P → K in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1094 – 10941R → S in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1099 – 10991G → A in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1302 – 13021A → D in CAA33552. (PubMed:2400788)Curated
    Sequence conflicti1337 – 13404PKVW → AKWG in CAA33552. (PubMed:2400788)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25926 mRNA. Translation: AAA65097.1.
    M62889 mRNA. Translation: AAA42144.1.
    X15546 mRNA. Translation: CAA33552.1.
    PIRiS11386.
    T10799.
    RefSeqiNP_037193.1. NM_013061.1.
    UniGeneiRn.10057.

    Genome annotation databases

    GeneIDi497756.
    KEGGirno:497756.
    UCSCiRGD:3675. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25926 mRNA. Translation: AAA65097.1 .
    M62889 mRNA. Translation: AAA42144.1 .
    X15546 mRNA. Translation: CAA33552.1 .
    PIRi S11386.
    T10799.
    RefSeqi NP_037193.1. NM_013061.1.
    UniGenei Rn.10057.

    3D structure databases

    ProteinModelPortali P23739.
    SMRi P23739. Positions 83-937.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000045106.

    Chemistry

    BindingDBi P23739.
    ChEMBLi CHEMBL3114.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    PTM databases

    PhosphoSitei P23739.

    Proteomic databases

    PRIDEi P23739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 497756.
    KEGGi rno:497756.
    UCSCi RGD:3675. rat.

    Organism-specific databases

    CTDi 6476.
    RGDi 3675. Si.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000067936.
    HOVERGENi HBG080721.
    KOi K01203.
    PhylomeDBi P23739.

    Enzyme and pathway databases

    BRENDAi 3.2.1.10. 5301.
    SABIO-RK P23739.

    Miscellaneous databases

    NextBioi 697744.
    PROi P23739.

    Gene expression databases

    Genevestigatori P23739.

    Family and domain databases

    Gene3Di 4.10.110.10. 1 hit.
    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. 1 hit.
    [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. 1 hit.
    PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a full-length rat sucrase-isomaltase-encoding cDNA."
      Chandrasena G., Osterholm D.E., Sunitha I., Henning S.J.
      Gene 150:355-360(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Intestine.
    2. "Regulation of sucrase-isomaltase gene expression along the crypt-villus axis of rat small intestine."
      Traber P.G.
      Biochem. Biophys. Res. Commun. 173:765-773(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-362.
      Strain: Fischer 344.
      Tissue: Intestine.
    3. "Molecular cloning and characterization of a rat intestinal sucrase-isomaltase cDNA. Regulation of sucrase-isomaltase gene expression by sucrose feeding."
      Broyart J.-P., Hugot J.-P., Perret C., Porteu A.
      Biochim. Biophys. Acta 1087:61-67(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 733-1373.
      Strain: Sprague-Dawley.
      Tissue: Duodenum.
    4. "Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal amino acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-isomaltase) from fetal intestinal transplants."
      Hauri H.-P., Wacker H., Rickli E.E., Bigler-Meier B., Quaroni A., Semenza G.
      J. Biol. Chem. 257:4522-4528(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS OF ISOMALTASE AND SUCRASE.

    Entry informationi

    Entry nameiSUIS_RAT
    AccessioniPrimary (citable) accession number: P23739
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 5 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

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    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