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Sucrase-isomaltase, intestinal [Cleaved into: Sucrase (EC 3.2.1.48); Isomaltase (EC 3.2.1.10)]

 SUIS_HUMAN              Reviewed;        1827 AA.
P14410; A2RUC3; Q1JQ80; Q1RMC2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 6.
28-FEB-2018, entry version 184.
RecName: Full=Sucrase-isomaltase, intestinal;
Contains:
RecName: Full=Sucrase;
EC=3.2.1.48;
Contains:
RecName: Full=Isomaltase;
EC=3.2.1.10;
Name=SI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-231 AND ILE-1523.
TISSUE=Intestine;
PubMed=1353958; DOI=10.1042/bj2850915;
Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N.,
Edwards Y., Swallow D., Rousset M.;
"Sequence of the complete cDNA and the 5' structure of the human
sucrase-isomaltase gene. Possible homology with a yeast
glucoamylase.";
Biochem. J. 285:915-923(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PHE-15; ALA-231
AND ILE-1523.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-679, AND VARIANT ALA-231.
PubMed=2962903; DOI=10.1016/0378-1119(87)90181-8;
Green F., Edwards Y., Hauri H.-P., Povey S., Ho M.W., Pinto M.,
Swallow D.;
"Isolation of a cDNA probe for a human jejunal brush-border hydrolase,
sucrase-isomaltase, and assignment of the gene locus to chromosome
3.";
Gene 57:101-110(1987).
[5]
PROTEIN SEQUENCE OF 2-20 AND 1008-1024, TISSUE SPECIFICITY, AND
VARIANT PHE-15.
PubMed=1677636;
Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J.,
Maroux S.;
"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human
small intestine and colon.";
Gastroenterology 101:618-625(1991).
[6]
PHOSPHORYLATION AT SER-7.
PubMed=8521865; DOI=10.1111/j.1432-1033.1995.963_3.x;
Keller P., Semenza G., Shaltiel S.;
"Phosphorylation of the N-terminal intracellular tail of sucrase-
isomaltase by cAMP-dependent protein kinase.";
Eur. J. Biochem. 233:963-968(1995).
[7]
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, AND DISULFIDE BONDS.
PubMed=20356844; DOI=10.1074/jbc.M109.078980;
Sim L., Willemsma C., Mohan S., Naim H.Y., Pinto B.M., Rose D.R.;
"Structural basis for substrate selectivity in human maltase-
glucoamylase and sucrase-isomaltase N-terminal domains.";
J. Biol. Chem. 285:17763-17770(2010).
[8]
VARIANT CSID PRO-1098.
PubMed=8609217; DOI=10.1172/JCI118459;
Ouwendijk J., Moolenaar C.E.C., Peters W.J., Hollenberg C.P.,
Ginsel L.A., Fransen J.A.M., Naim H.Y.;
"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.";
J. Clin. Invest. 97:633-641(1996).
[9]
VARIANT CSID PRO-341, AND CHARACTERIZATION OF VARIANT CSID PRO-341.
PubMed=10903344; DOI=10.1172/JCI9677;
Jacob R., Zimmer K.P., Schmitz J., Naim H.Y.;
"Congenital sucrase-isomaltase deficiency arising from cleavage and
secretion of a mutant form of the enzyme.";
J. Clin. Invest. 106:281-287(2000).
[10]
VARIANT CSID ARG-117, AND CHARACTERIZATION OF VARIANT CSID ARG-117.
PubMed=11340066; DOI=10.1074/jbc.C100219200;
Spodsberg N., Jacob R., Alfalah M., Zimmer K.P., Naim H.Y.;
"Molecular basis of aberrant apical protein transport in an intestinal
enzyme disorder.";
J. Biol. Chem. 276:23506-23510(2001).
[11]
VARIANTS PHE-15 AND ALA-231, AND VARIANT CSID PRO-620.
PubMed=14724820; DOI=10.1053/j.gastro.2003.09.022;
Ritz V., Alfalah M., Zimmer K.P., Schmitz J., Jacob R., Naim H.Y.;
"Congenital sucrase-isomaltase deficiency because of an accumulation
of the mutant enzyme in the endoplasmic reticulum.";
Gastroenterology 125:1678-1685(2003).
[12]
VARIANTS CSID GLY-577; PRO-594; PRO-694; ASP-1073; TYR-1229; GLY-1367
AND CYS-1745, AND VARIANTS PHE-15; ALA-231 AND ILE-1523.
PubMed=16329100; DOI=10.1002/humu.9392;
Sander P., Alfalah M., Keiser M., Korponay-Szabo I., Kovacs J.B.,
Leeb T., Naim H.Y.;
"Novel mutations in the human sucrase-isomaltase gene (SI) that cause
congenital carbohydrate malabsorption.";
Hum. Mutat. 27:119-119(2006).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:20356844}.
-!- CATALYTIC ACTIVITY: Hydrolysis of sucrose and maltose by an alpha-
D-glucosidase-type action.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->6)-alpha-D-glucosidic
linkages in some oligosaccharides produced from starch and
glycogen by alpha-amylase, and in isomaltose.
-!- SUBUNIT: The resulting sucrase and isomaltase subunits stay
associated with one another in a complex by non-covalent linkages.
{ECO:0000269|PubMed:20356844}.
-!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
membrane protein. Note=Brush border.
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:1677636}.
-!- PTM: The precursor is proteolytically cleaved when exposed to
pancreatic proteases in the intestinal lumen.
-!- PTM: Sulfated. {ECO:0000250}.
-!- DISEASE: 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. {ECO:0000269|PubMed:10903344, ECO:0000269|PubMed:11340066,
ECO:0000269|PubMed:14724820, ECO:0000269|PubMed:16329100,
ECO:0000269|PubMed:8609217}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
{ECO:0000305}.
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EMBL; X63597; CAA45140.1; -; mRNA.
EMBL; AC092695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC144561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC115034; AAI15035.1; -; mRNA.
EMBL; BC116452; AAI16453.1; -; mRNA.
EMBL; BC132834; AAI32835.1; -; mRNA.
EMBL; BC132860; AAI32861.1; -; mRNA.
EMBL; M22616; AAA60551.1; -; mRNA.
CCDS; CCDS3196.1; -.
PIR; S36082; UUHU.
RefSeq; NP_001032.2; NM_001041.3.
UniGene; Hs.429596; -.
PDB; 3LPO; X-ray; 3.20 A; A/B/C/D=62-931.
PDB; 3LPP; X-ray; 2.15 A; A/B/C/D=62-931.
PDBsum; 3LPO; -.
PDBsum; 3LPP; -.
ProteinModelPortal; P14410; -.
SMR; P14410; -.
STRING; 9606.ENSP00000264382; -.
BindingDB; P14410; -.
ChEMBL; CHEMBL2748; -.
DrugBank; DB00284; Acarbose.
DrugBank; DB00747; Scopolamine.
CAZy; GH31; Glycoside Hydrolase Family 31.
iPTMnet; P14410; -.
PhosphoSitePlus; P14410; -.
BioMuta; SI; -.
DMDM; 317373594; -.
MaxQB; P14410; -.
PaxDb; P14410; -.
PeptideAtlas; P14410; -.
PRIDE; P14410; -.
Ensembl; ENST00000264382; ENSP00000264382; ENSG00000090402.
GeneID; 6476; -.
KEGG; hsa:6476; -.
UCSC; uc003fei.3; human.
CTD; 6476; -.
DisGeNET; 6476; -.
EuPathDB; HostDB:ENSG00000090402.7; -.
GeneCards; SI; -.
H-InvDB; HIX0030867; -.
HGNC; HGNC:10856; SI.
HPA; HPA011897; -.
MalaCards; SI; -.
MIM; 222900; phenotype.
MIM; 609845; gene.
neXtProt; NX_P14410; -.
OpenTargets; ENSG00000090402; -.
Orphanet; 306446; Congenital sucrase-isomaltase deficiency with minimal starch tolerance.
Orphanet; 306474; Congenital sucrase-isomaltase deficiency with starch and lactose intolerance.
Orphanet; 306436; Congenital sucrase-isomaltase deficiency with starch intolerance.
Orphanet; 306462; Congenital sucrase-isomaltase deficiency without starch intolerance.
Orphanet; 306486; Congenital sucrase-isomaltase deficiency without sucrose intolerance.
PharmGKB; PA35758; -.
eggNOG; KOG1065; Eukaryota.
eggNOG; COG1501; LUCA.
GeneTree; ENSGT00760000119229; -.
HOGENOM; HOG000067936; -.
HOVERGEN; HBG080721; -.
InParanoid; P14410; -.
KO; K01203; -.
OMA; PLVYSDQ; -.
OrthoDB; EOG091G01E3; -.
PhylomeDB; P14410; -.
TreeFam; TF314577; -.
BioCyc; MetaCyc:HS01688-MONOMER; -.
BRENDA; 3.2.1.10; 2681.
BRENDA; 3.2.1.48; 2681.
Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
Reactome; R-HSA-5659898; Intestinal saccharidase deficiencies.
ChiTaRS; SI; human.
EvolutionaryTrace; P14410; -.
GenomeRNAi; 6476; -.
PRO; PR:P14410; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000090402; -.
CleanEx; HS_SI; -.
ExpressionAtlas; P14410; baseline and differential.
Genevisible; P14410; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005903; C:brush border; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004558; F:alpha-1,4-glucosidase activity; EXP:Reactome.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0004574; F:oligo-1,6-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0004575; F:sucrose alpha-glucosidase activity; TAS:Reactome.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0044245; P:polysaccharide digestion; TAS:Reactome.
CDD; cd00111; Trefoil; 2.
Gene3D; 2.60.40.1180; -; 4.
InterPro; IPR031727; Gal_mutarotase_N.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR000322; Glyco_hydro_31.
InterPro; IPR030458; Glyco_hydro_31_AS.
InterPro; IPR030459; Glyco_hydro_31_CS.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR017957; P_trefoil_CS.
InterPro; IPR000519; P_trefoil_dom.
Pfam; PF01055; Glyco_hydro_31; 2.
Pfam; PF16863; NtCtMGAM_N; 2.
Pfam; PF00088; Trefoil; 2.
SMART; SM00018; PD; 2.
SUPFAM; SSF51445; SSF51445; 4.
SUPFAM; SSF74650; SSF74650; 2.
PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 2.
PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 2.
PROSITE; PS00025; P_TREFOIL_1; 1.
PROSITE; PS51448; P_TREFOIL_2; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Membrane;
Multifunctional enzyme; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal-anchor; Sulfation; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1677636}.
CHAIN 2 1827 Sucrase-isomaltase, intestinal.
/FTId=PRO_0000018551.
CHAIN 2 1007 Isomaltase.
/FTId=PRO_0000018552.
CHAIN 1008 1827 Sucrase.
/FTId=PRO_0000018553.
TOPO_DOM 2 12 Cytoplasmic.
TRANSMEM 13 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 1827 Lumenal.
DOMAIN 61 110 P-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
DOMAIN 932 978 P-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
REGION 110 1007 Isomaltase.
REGION 1008 1827 Sucrase.
COMPBIAS 43 60 Ser/Thr-rich.
ACT_SITE 505 505 Nucleophile; for isomaltase activity.
{ECO:0000255|PROSITE-ProRule:PRU10066,
ECO:0000269|PubMed:20356844}.
ACT_SITE 604 604 For isomaltase activity.
{ECO:0000269|PubMed:20356844}.
ACT_SITE 1394 1394 Nucleophile; for sucrase activity.
{ECO:0000255|PROSITE-ProRule:PRU10066,
ECO:0000269|PubMed:20356844}.
ACT_SITE 1397 1397 For sucrase activity. {ECO:0000250}.
ACT_SITE 1500 1500 Proton donor; for isomaltase activity.
{ECO:0000250}.
BINDING 264 264 Substrate.
BINDING 388 388 Substrate.
BINDING 588 588 Substrate.
BINDING 662 662 Substrate.
MOD_RES 7 7 Phosphoserine; by PKA.
{ECO:0000269|PubMed:8521865}.
MOD_RES 237 237 Sulfotyrosine. {ECO:0000255}.
MOD_RES 239 239 Sulfotyrosine. {ECO:0000255}.
MOD_RES 391 391 Sulfotyrosine. {ECO:0000255}.
MOD_RES 400 400 Sulfotyrosine. {ECO:0000255}.
MOD_RES 667 667 Sulfotyrosine. {ECO:0000255}.
MOD_RES 763 763 Sulfotyrosine. {ECO:0000255}.
MOD_RES 765 765 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20356844}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20356844}.
CARBOHYD 823 823 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 855 855 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20356844}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20356844}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1235 1235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1303 1303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1340 1340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1403 1403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1535 1535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1572 1572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1675 1675 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1748 1748 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1763 1763 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1815 1815 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 63 94 {ECO:0000255|PROSITE-ProRule:PRU00779,
ECO:0000269|PubMed:20356844}.
DISULFID 77 93 {ECO:0000255|PROSITE-ProRule:PRU00779,
ECO:0000269|PubMed:20356844}.
DISULFID 88 106 {ECO:0000255|PROSITE-ProRule:PRU00779,
ECO:0000269|PubMed:20356844}.
DISULFID 520 545 {ECO:0000255|PROSITE-ProRule:PRU00779,
ECO:0000269|PubMed:20356844}.
DISULFID 635 646 {ECO:0000255|PROSITE-ProRule:PRU00779,
ECO:0000269|PubMed:20356844}.
VARIANT 15 15 V -> F (in dbSNP:rs9290264).
{ECO:0000269|PubMed:14724820,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16329100,
ECO:0000269|PubMed:1677636}.
/FTId=VAR_025367.
VARIANT 117 117 Q -> R (in CSID; missorting of the enzyme
to the basolateral membrane;
dbSNP:rs121912612).
{ECO:0000269|PubMed:11340066}.
/FTId=VAR_025368.
VARIANT 231 231 T -> A (in dbSNP:rs9283633).
{ECO:0000269|PubMed:1353958,
ECO:0000269|PubMed:14724820,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16329100,
ECO:0000269|PubMed:2962903}.
/FTId=VAR_025369.
VARIANT 341 341 L -> P (in CSID; causes loss of anchored
SI from the membrane; dbSNP:rs267607049).
{ECO:0000269|PubMed:10903344}.
/FTId=VAR_025370.
VARIANT 577 577 V -> G (in CSID; dbSNP:rs121912615).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025371.
VARIANT 594 594 S -> P (in CSID; dbSNP:rs765433197).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025372.
VARIANT 620 620 L -> P (in CSID; SI accumulates
predominantly in the ER;
dbSNP:rs121912613).
{ECO:0000269|PubMed:14724820}.
/FTId=VAR_025373.
VARIANT 694 694 T -> P (in CSID).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025374.
VARIANT 1073 1073 G -> D (in CSID; dbSNP:rs121912616).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025375.
VARIANT 1098 1098 Q -> P (in CSID; exhibits intracellular
accumulation of mannose-rich SI in the
Golgi; dbSNP:rs121912611).
{ECO:0000269|PubMed:8609217}.
/FTId=VAR_007854.
VARIANT 1229 1229 C -> Y (in CSID; dbSNP:rs121912614).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025376.
VARIANT 1367 1367 R -> G (in CSID; dbSNP:rs143388292).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025377.
VARIANT 1523 1523 M -> I (in dbSNP:rs4855271).
{ECO:0000269|PubMed:1353958,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16329100}.
/FTId=VAR_025378.
VARIANT 1745 1745 F -> C (in CSID; dbSNP:rs79717168).
{ECO:0000269|PubMed:16329100}.
/FTId=VAR_025379.
VARIANT 1802 1802 T -> S (in dbSNP:rs9917722).
/FTId=VAR_034522.
CONFLICT 300 300 N -> D (in Ref. 3; AAI16453).
{ECO:0000305}.
CONFLICT 460 460 S -> I (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 475 475 P -> S (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 548 548 A -> V (in Ref. 3; AAI16453).
{ECO:0000305}.
CONFLICT 584 584 F -> L (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 588 588 R -> C (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 633 633 D -> A (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 687 687 Q -> R (in Ref. 3; AAI16453).
{ECO:0000305}.
CONFLICT 884 884 T -> A (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 1016 1016 S -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 1022 1022 V -> T (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 1155 1155 A -> V (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 1203 1203 E -> Q (in Ref. 1; CAA45140).
{ECO:0000305}.
CONFLICT 1782 1782 V -> I (in Ref. 3; AAI15035).
{ECO:0000305}.
CONFLICT 1825 1825 N -> S (in Ref. 3; AAI16453).
{ECO:0000305}.
STRAND 65 68 {ECO:0000244|PDB:3LPP}.
HELIX 71 73 {ECO:0000244|PDB:3LPP}.
STRAND 75 77 {ECO:0000244|PDB:3LPO}.
HELIX 85 91 {ECO:0000244|PDB:3LPP}.
STRAND 99 103 {ECO:0000244|PDB:3LPP}.
STRAND 105 107 {ECO:0000244|PDB:3LPP}.
STRAND 114 121 {ECO:0000244|PDB:3LPP}.
STRAND 123 132 {ECO:0000244|PDB:3LPP}.
STRAND 138 140 {ECO:0000244|PDB:3LPP}.
STRAND 144 154 {ECO:0000244|PDB:3LPP}.
STRAND 157 163 {ECO:0000244|PDB:3LPP}.
STRAND 175 177 {ECO:0000244|PDB:3LPP}.
STRAND 189 195 {ECO:0000244|PDB:3LPP}.
TURN 196 199 {ECO:0000244|PDB:3LPP}.
STRAND 200 205 {ECO:0000244|PDB:3LPP}.
TURN 206 209 {ECO:0000244|PDB:3LPP}.
STRAND 210 214 {ECO:0000244|PDB:3LPP}.
HELIX 215 217 {ECO:0000244|PDB:3LPP}.
STRAND 221 223 {ECO:0000244|PDB:3LPP}.
STRAND 226 232 {ECO:0000244|PDB:3LPP}.
STRAND 234 236 {ECO:0000244|PDB:3LPP}.
STRAND 238 244 {ECO:0000244|PDB:3LPP}.
STRAND 247 250 {ECO:0000244|PDB:3LPP}.
STRAND 254 261 {ECO:0000244|PDB:3LPP}.
STRAND 278 284 {ECO:0000244|PDB:3LPP}.
STRAND 291 296 {ECO:0000244|PDB:3LPP}.
STRAND 302 307 {ECO:0000244|PDB:3LPP}.
TURN 308 310 {ECO:0000244|PDB:3LPP}.
STRAND 311 319 {ECO:0000244|PDB:3LPP}.
STRAND 321 330 {ECO:0000244|PDB:3LPP}.
HELIX 331 342 {ECO:0000244|PDB:3LPP}.
HELIX 350 353 {ECO:0000244|PDB:3LPP}.
HELIX 365 377 {ECO:0000244|PDB:3LPP}.
STRAND 384 387 {ECO:0000244|PDB:3LPP}.
HELIX 389 391 {ECO:0000244|PDB:3LPP}.
HELIX 393 395 {ECO:0000244|PDB:3LPO}.
TURN 402 407 {ECO:0000244|PDB:3LPP}.
HELIX 408 417 {ECO:0000244|PDB:3LPP}.
STRAND 421 426 {ECO:0000244|PDB:3LPP}.
HELIX 442 450 {ECO:0000244|PDB:3LPP}.
STRAND 459 462 {ECO:0000244|PDB:3LPP}.
STRAND 465 467 {ECO:0000244|PDB:3LPP}.
STRAND 470 473 {ECO:0000244|PDB:3LPP}.
HELIX 480 496 {ECO:0000244|PDB:3LPP}.
STRAND 500 504 {ECO:0000244|PDB:3LPP}.
TURN 507 509 {ECO:0000244|PDB:3LPP}.
STRAND 512 515 {ECO:0000244|PDB:3LPP}.
TURN 524 526 {ECO:0000244|PDB:3LPP}.
HELIX 535 537 {ECO:0000244|PDB:3LPP}.
TURN 539 542 {ECO:0000244|PDB:3LPP}.
HELIX 555 558 {ECO:0000244|PDB:3LPP}.
HELIX 559 561 {ECO:0000244|PDB:3LPP}.
HELIX 562 577 {ECO:0000244|PDB:3LPP}.
STRAND 585 588 {ECO:0000244|PDB:3LPP}.
HELIX 594 596 {ECO:0000244|PDB:3LPP}.
STRAND 599 601 {ECO:0000244|PDB:3LPP}.
STRAND 606 608 {ECO:0000244|PDB:3LPP}.
HELIX 609 624 {ECO:0000244|PDB:3LPP}.
STRAND 629 631 {ECO:0000244|PDB:3LPP}.
STRAND 637 639 {ECO:0000244|PDB:3LPP}.
HELIX 643 653 {ECO:0000244|PDB:3LPP}.
STRAND 656 658 {ECO:0000244|PDB:3LPP}.
HELIX 672 675 {ECO:0000244|PDB:3LPP}.
HELIX 680 694 {ECO:0000244|PDB:3LPP}.
HELIX 696 709 {ECO:0000244|PDB:3LPP}.
STRAND 713 715 {ECO:0000244|PDB:3LPP}.
HELIX 718 721 {ECO:0000244|PDB:3LPP}.
HELIX 725 729 {ECO:0000244|PDB:3LPP}.
STRAND 732 736 {ECO:0000244|PDB:3LPP}.
TURN 737 739 {ECO:0000244|PDB:3LPP}.
STRAND 740 743 {ECO:0000244|PDB:3LPP}.
STRAND 751 757 {ECO:0000244|PDB:3LPP}.
STRAND 762 764 {ECO:0000244|PDB:3LPP}.
TURN 765 767 {ECO:0000244|PDB:3LPP}.
STRAND 775 781 {ECO:0000244|PDB:3LPP}.
STRAND 788 792 {ECO:0000244|PDB:3LPP}.
STRAND 795 800 {ECO:0000244|PDB:3LPP}.
HELIX 806 809 {ECO:0000244|PDB:3LPP}.
STRAND 814 819 {ECO:0000244|PDB:3LPP}.
STRAND 824 832 {ECO:0000244|PDB:3LPP}.
STRAND 835 837 {ECO:0000244|PDB:3LPP}.
HELIX 840 843 {ECO:0000244|PDB:3LPP}.
STRAND 846 854 {ECO:0000244|PDB:3LPP}.
STRAND 857 865 {ECO:0000244|PDB:3LPP}.
HELIX 868 872 {ECO:0000244|PDB:3LPP}.
STRAND 874 882 {ECO:0000244|PDB:3LPP}.
STRAND 890 894 {ECO:0000244|PDB:3LPP}.
STRAND 900 902 {ECO:0000244|PDB:3LPP}.
STRAND 905 908 {ECO:0000244|PDB:3LPP}.
TURN 909 912 {ECO:0000244|PDB:3LPP}.
STRAND 913 916 {ECO:0000244|PDB:3LPP}.
STRAND 927 930 {ECO:0000244|PDB:3LPP}.
SEQUENCE 1827 AA; 209453 MW; DCB93F068AEEF83E CRC64;
MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT TRVTTNPSDS
GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND SLIPWCFFVD NHGYNVQDMT
TTSIGVEAKL NRIPSPTLFG NDINSVLFTT QNQTPNRFRF KITDPNNRRY EVPHQYVKEF
TGPTVSDTLY DVKVAQNPFS IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG
IGEQVHKRFR HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN
AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY WNLGFQLSRW
NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY DQVAFNGLPQ FVQDLHDHGQ
KYVIILDPAI SIGRRANGTT YATYERGNTQ HVWINESDGS TPIIGEVWPG LTVYPDFTNP
NCIDWWANEC SIFHQEVQYD GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY
SKTICMDAVQ NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH
WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM QLGAFYPFSR
NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY TLFYKAHVFG ETVARPVLHE
FYEDTNSWIE DTEFLWGPAL LITPVLKQGA DTVSAYIPDA IWYDYESGAK RPWRKQRVDM
YLPADKIGLH LRGGYIIPIQ EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT
IQNGNYILYT FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN
AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA TEQKCTQRGC
VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ LNTANARIKL PSDPISTLRV
EVKYHKNDML QFKIYDPQKK RYEVPVPLNI PTTPISTYED RLYDVEIKEN PFGIQIRRRS
SGRVIWDSWL PGFAFNDQFI QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP
GYKLNSYGFH PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP
TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN IPYDVQYTDI
DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI SGNETKTYPA FERGQQNDVF
VKWPNTNDIC WAKVWPDLPN ITIDKTLTED EAVNASRAHV AFPDFFRTST AEWWAREIVD
FYNEKMKFDG LWIDMNEPSS FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA
EQILSDGTSV LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD
NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA FYPYSRNHNI
ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI HANGGTVIRP LLHEFFDEKP
TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY VPNARWFDYH TGKDIGVRGQ FQTFNASYDT
INLHVRGGHI LPCQEPAQNT FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY
LSVQFNLNQT TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE
DTTNMILRID LTTHNVTLEE PIEINWS


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