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P07768

- SUIS_RABIT

UniProt

P07768 - SUIS_RABIT

Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (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.

    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 – 2641SubstrateBy similarity
    Binding sitei388 – 3881SubstrateBy similarity
    Active sitei505 – 5051Nucleophile; for isomaltase activity
    Binding sitei588 – 5881SubstrateBy similarity
    Active sitei604 – 6041For isomaltase activityBy similarity
    Binding sitei662 – 6621SubstrateBy similarity
    Active sitei1394 – 13941Nucleophile; for sucrase activity
    Active sitei1397 – 13971For sucrase activity
    Active sitei1500 – 15001Proton 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

    BRENDAi3.2.1.10. 1749.

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    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 – 11Removed
    Chaini2 – 18271826Sucrase-isomaltase, intestinalPRO_0000018556Add
    BLAST
    Chaini2 – 10071006IsomaltasePRO_0000018557Add
    BLAST
    Chaini1008 – 1827820SucrasePRO_0000018558Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphoserine; by PKABy similarity
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi63 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi77 ↔ 93PROSITE-ProRule annotation
    Disulfide bondi88 ↔ 106PROSITE-ProRule annotation
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Modified residuei391 – 3911SulfotyrosineSequence Analysis
    Modified residuei400 – 4001SulfotyrosineSequence Analysis
    Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi520 ↔ 545PROSITE-ProRule annotation
    Disulfide bondi635 ↔ 646PROSITE-ProRule annotation
    Glycosylationi859 – 8591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi896 – 8961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi904 – 9041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1002 – 10021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1303 – 13031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1325 – 13251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1368 – 13681N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1382 – 13821SulfotyrosineSequence Analysis
    Modified residuei1385 – 13851SulfotyrosineSequence Analysis
    Glycosylationi1403 – 14031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1535 – 15351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1572 – 15721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1748 – 17481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1799 – 17991N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
    N- and O-glycosylated.
    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.

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000003372.

    Structurei

    3D structure databases

    ProteinModelPortaliP07768.
    SMRiP07768. Positions 73-931.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 18271795LumenalSequence 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
    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.

    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.

    P07768-1 [UniParc]FASTAAdd to Basket

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    MAKRKFSGLE ITLIVLFVIV FIIAIALIAV LATKTPAVEE VNPSSSTPTT     50
    TSTTTSTSGS VSCPSELNEV VNERINCIPE QSPTQAICAQ RNCCWRPWNN 100
    SDIPWCFFVD NHGYNVEGMT TTSTGLEARL NRKSTPTLFG NDINNVLLTT 150
    ESQTANRLRF KLTDPNNKRY EVPHQFVTEF AGPAATETLY DVQVTENPFS 200
    IKVIRKSNNR ILFDSSIGPL VYSDQYLQIS TRLPSEYMYG FGEHVHKRFR 250
    HDLYWKTWPI FTRDQHTDDN NNNLYGHQTF FMCIEDTTGK SFGVFLMNSN 300
    AMEIFIQPTP IVTYRVIGGI LDFYIFLGDT PEQVVQQYQE LIGRPAMPAY 350
    WSLGFQLSRW NYNSLDVVKE VVRRNREALI PFDTQVSDID YMEDKKDFTY 400
    DRVAYNGLPD FVQDLHDHGQ KYVIILDPAI SINRRASGEA YESYDRGNAQ 450
    NVWVNESDGT TPIVGEVWPG DTVYPDFTSP NCIEWWANEC NIFHQEVNYD 500
    GLWIDMNEVS SFVQGSNKGC NDNTLNYPPY IPDIVDKLMY SKTLCMDSVQ 550
    YWGKQYDVHS LYGYSMAIAT ERAVERVFPN KRSFILTRST FAGSGRHAAH 600
    WLGDNTATWE QMEWSITGML EFGLFGMPLV GADICGFLAE TTEELCRRWM 650
    QLGAFYPFSR NHNADGFEHQ DPAFFGQDSL LVKSSRHYLN IRYTLLPFLY 700
    TLFYKAHAFG ETVARPVLHE FYEDTNSWVE DREFLWGPAL LITPVLTQGA 750
    ETVSAYIPDA VWYDYETGAK RPWRKQRVEM SLPADKIGLH LRGGYIIPIQ 800
    QPAVTTTASR MNPLGLIIAL NDDNTAVGDF FWDDGETKDT VQNDNYILYT 850
    FAVSNNNLNI TCTHELYSEG TTLAFQTIKI LGVTETVTQV TVAENNQSMS 900
    THSNFTYDPS NQVLLIENLN FNLGRNFRVQ WDQTFLESEK ITCYPDADIA 950
    TQEKCTQRGC IWDTNTVNPR APECYFPKTD NPYSVSSTQY SPTGITADLQ 1000
    LNPTRTRITL PSEPITNLRV EVKYHKNDMV QFKIFDPQNK RYEVPVPLDI 1050
    PATPTSTQEN RLYDVEIKEN PFGIQIRRRS TGKVIWDSCL PGFAFNDQFI 1100
    QISTRLPSEY IYGFGEAEHT AFKRDLNWHT WGMFTRDQPP GYKLNSYGFH 1150
    PYYMALEDEG NAHGVLLLNS NAMDVTFMPT PALTYRVIGG ILDFYMFLGP 1200
    TPEVATQQYH EVIGHPVMPP YWSLGFQLCR YGYRNTSEII ELYEGMVAAD 1250
    IPYDVQYTDI DYMERQLDFT IDENFRELPQ FVDRIRGEGM RYIIILDPAI 1300
    SGNETRPYPA FDRGEAKDVF VKWPNTSDIC WAKVWPDLPN ITIDESLTED 1350
    EAVNASRAHA AFPDFFRNST AEWWTREILD FYNNYMKFDG LWIDMNEPSS 1400
    FVNGTTTNVC RNTELNYPPY FPELTKRTDG LHFRTMCMET EHILSDGSSV 1450
    LHYDVHNLYG WSQAKPTYDA LQKTTGKRGI VISRSTYPTA GRWAGHWLGD 1500
    NYARWDNMDK SIIGMMEFSL FGISYTGADI CGFFNDSEYH LCTRWTQLGA 1550
    FYPFARNHNI QFTRRQDPVS WNQTFVEMTR NVLNIRYTLL PYFYTQLHEI 1600
    HAHGGTVIRP LMHEFFDDRT TWDIFLQFLW GPAFMVTPVL EPYTTVVRGY 1650
    VPNARWFDYH TGEDIGIRGQ VQDLTLLMNA INLHVRGGHI LPCQEPARTT 1700
    FLSRQKYMKL IVAADDNHMA QGSLFWDDGD TIDTYERDLY LSVQFNLNKT 1750
    TLTSTLLKTG YINKTEIRLG YVHVWGIGNT LINEVNLMYN EINYPLIFNQ 1800
    TQAQEILNID LTAHEVTLDD PIEISWS 1827
    Length:1,827
    Mass (Da):210,140
    Last modified:January 23, 2007 - v3
    Checksum:i2CEFFE3109AC8917
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14046 mRNA. Translation: AAA31459.1.
    PIRiA23945.
    RefSeqiNP_001075735.1. NM_001082266.1.
    UniGeneiOcu.1958.

    Genome annotation databases

    GeneIDi100009093.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14046 mRNA. Translation: AAA31459.1 .
    PIRi A23945.
    RefSeqi NP_001075735.1. NM_001082266.1.
    UniGenei Ocu.1958.

    3D structure databases

    ProteinModelPortali P07768.
    SMRi P07768. Positions 73-931.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000003372.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009093.

    Organism-specific databases

    CTDi 6476.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000067936.
    HOVERGENi HBG080721.

    Enzyme and pathway databases

    BRENDAi 3.2.1.10. 1749.

    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. "The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein."
      Hunziker W., Spiess M., Semenza G., Lodish H.F.
      Cell 46:227-234(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "N-terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase-isomaltase. Implications for the biosynthesis and membrane insertion of pro-sucrase-isomaltase."
      Sjoestroem H., Noren O., Christiansen L.A., Wacker H., Spiess M., Bigler-Meier B., Rickli E.E., Semenza G.
      FEBS Lett. 148:321-325(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-38 AND 1008-1015.

    Entry informationi

    Entry nameiSUIS_RABIT
    AccessioniPrimary (citable) accession number: P07768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 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

    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