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P23739

- SUIS_RAT

UniProt

P23739 - SUIS_RAT

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Protein
Sucrase-isomaltase, intestinal
Gene
Si
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2741Substrate By similarity
Binding sitei398 – 3981Substrate By similarity
Active sitei514 – 5141Nucleophile; for isomaltase activity By similarity
Binding sitei599 – 5991Substrate By similarity
Active sitei615 – 6151For isomaltase activity By similarity
Binding sitei673 – 6731Substrate By similarity
Active sitei1399 – 13991Nucleophile; for sucrase activity By similarity
Active sitei1402 – 14021For sucrase activity By similarity
Active sitei1512 – 15121Proton donor; for sucrase activity By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – 18411809Lumenal Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 18411840Sucrase-isomaltase, intestinal
PRO_0000018559Add
BLAST
Chaini2 – 10131012Isomaltase
PRO_0000018560Add
BLAST
Chaini1014 – 1841828Sucrase
PRO_0000018561Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 12050P-type 1
Add
BLAST
Domaini936 – 98449P-type 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1013894Isomaltase
Add
BLAST
Regioni1014 – 1841828Sucrase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 7028Ser/Thr-rich
Add
BLAST

Sequence similaritiesi

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871C → W in AAA65097. 1 Publication
Sequence conflicti92 – 921H → S in AAA42144. 1 Publication
Sequence conflicti95 – 951K → Q in AAA42144. 1 Publication
Sequence conflicti736 – 7361E → V in CAA33552. 1 Publication
Sequence conflicti842 – 8421E → Q in CAA33552. 1 Publication
Sequence conflicti916 – 9161A → T in CAA33552. 1 Publication
Sequence conflicti924 – 9241A → R in CAA33552. 1 Publication
Sequence conflicti930 – 9312AG → GT in CAA33552. 1 Publication
Sequence conflicti938 – 9392CR → SQ in CAA33552. 1 Publication
Sequence conflicti959 – 9624GTCT → ETDK in CAA33552. 1 Publication
Sequence conflicti980 – 9801Y → C in CAA33552. 1 Publication
Sequence conflicti986 – 9861N → H in CAA33552. 1 Publication
Sequence conflicti997 – 9982LP → SL in CAA33552. 1 Publication
Sequence conflicti1010 – 10101P → A in CAA33552. 1 Publication
Sequence conflicti1023 – 10231T → P in CAA33552. 1 Publication
Sequence conflicti1027 – 10271G → E in CAA33552. 1 Publication
Sequence conflicti1032 – 10321P → K in CAA33552. 1 Publication
Sequence conflicti1094 – 10941R → S in CAA33552. 1 Publication
Sequence conflicti1099 – 10991G → A in CAA33552. 1 Publication
Sequence conflicti1302 – 13021A → D in CAA33552. 1 Publication
Sequence conflicti1337 – 13404PKVW → AKWG in CAA33552. 1 Publication

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: June 11, 2014
This is version 122 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

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