LOCUS NP_001032 1827 aa linear PRI 28-AUG-2024
DEFINITION sucrase-isomaltase, intestinal [Homo sapiens].
ACCESSION NP_001032
VERSION NP_001032.2
DBSOURCE REFSEQ: accession NM_001041.4
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 1827)
AUTHORS Iryanci,F.I., Guven,B. and Cakir,M.
TITLE Congenital Sucrase-Isomaltase Deficiency: Same Mutation with
Different Clinical Presentations
JOURNAL Turk J Gastroenterol 35 (4), 343-349 (2024)
PUBMED 39128102
REMARK GeneRIF: Congenital Sucrase-Isomaltase Deficiency: Same Mutation
with Different Clinical Presentations.
REFERENCE 2 (residues 1 to 1827)
AUTHORS Zamfir-Taranu,A., Loscher,B.S., Husein,D.M., Hoter,A.,
Garcia-Etxebarria,K., Etxeberria,U., Gayoso,L., Mayr,G.,
Nilholm,C., Gustafsson,R.J., Ozaydin,O., Zheng,T.,
Esteban-Blanco,C., Bozzarelli,I., Bonfiglio,F., Rizk,S., Franke,A.,
Bujanda,L., Naim,H.Y., Ohlsson,B. and D'Amato,M.
TITLE Sucrase-isomaltase genotype and response to a starch-reduced and
sucrose-reduced diet in IBS-D patients
JOURNAL Gut 73 (4), 706-708 (2024)
PUBMED 36878682
REMARK GeneRIF: Sucrase-isomaltase genotype and response to a
starch-reduced and sucrose-reduced diet in IBS-D patients.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 1827)
AUTHORS Tannous,S., Stellbrinck,T., Hoter,A. and Naim,H.Y.
TITLE Interaction between the alpha-glucosidases, sucrase-isomaltase and
maltase-glucoamylase, in human intestinal brush border membranes
and its potential impact on disaccharide digestion
JOURNAL Front Mol Biosci 10, 1160860 (2023)
PUBMED 36968271
REMARK Publication Status: Online-Only
REFERENCE 4 (residues 1 to 1827)
AUTHORS Taskin,D.G., Civan,H.A., Sari,E.E., Altuntas,C., Ersoy,M.,
Tuncel,T., Onay,H. and Selimoglu,A.
TITLE Prevalence of congenital sucrase-isomaltase deficiency in Turkey
may be much higher than the estimates
JOURNAL J Genet 102 (2023)
PUBMED 37349966
REMARK GeneRIF: Prevalence of congenital sucrase-isomaltase deficiency in
Turkey may be much higher than the estimates.
REFERENCE 5 (residues 1 to 1827)
AUTHORS Hoter,A. and Naim,H.Y.
TITLE The glucose-regulated protein GRP94 interacts avidly in the
endoplasmic reticulum with sucrase-isomaltase isoforms that are
associated with congenital sucrase-isomaltase deficiency
JOURNAL Int J Biol Macromol 186, 237-243 (2021)
PUBMED 34242650
REMARK GeneRIF: The glucose-regulated protein GRP94 interacts avidly in
the endoplasmic reticulum with sucrase-isomaltase isoforms that are
associated with congenital sucrase-isomaltase deficiency.
REFERENCE 6 (residues 1 to 1827)
AUTHORS Chantret,I., Lacasa,M., Chevalier,G., Ruf,J., Islam,I., Mantei,N.,
Edwards,Y., Swallow,D. and Rousset,M.
TITLE Sequence of the complete cDNA and the 5' structure of the human
sucrase-isomaltase gene. Possible homology with a yeast
glucoamylase
JOURNAL Biochem J 285 (Pt 3) (Pt 3), 915-923 (1992)
PUBMED 1353958
REFERENCE 7 (residues 1 to 1827)
AUTHORS Wu,G.D., Wang,W. and Traber,P.G.
TITLE Isolation and characterization of the human sucrase-isomaltase gene
and demonstration of intestine-specific transcriptional elements
JOURNAL J Biol Chem 267 (11), 7863-7870 (1992)
PUBMED 1560017
REFERENCE 8 (residues 1 to 1827)
AUTHORS Fransen,J.A., Hauri,H.P., Ginsel,L.A. and Naim,H.Y.
TITLE Naturally occurring mutations in intestinal sucrase-isomaltase
provide evidence for the existence of an intracellular sorting
signal in the isomaltase subunit
JOURNAL J Cell Biol 115 (1), 45-57 (1991)
PUBMED 1717481
REMARK Erratum:[J Cell Biol 1991 Dec;115(5):following 1473]
REFERENCE 9 (residues 1 to 1827)
AUTHORS Gorvel,J.P., Ferrero,A., Chambraud,L., Rigal,A., Bonicel,J. and
Maroux,S.
TITLE Expression of sucrase-isomaltase and dipeptidylpeptidase IV in
human small intestine and colon
JOURNAL Gastroenterology 101 (3), 618-625 (1991)
PUBMED 1677636
REFERENCE 10 (residues 1 to 1827)
AUTHORS Green,F., Edwards,Y., Hauri,H.P., Povey,S., Ho,M.W., Pinto,M. and
Swallow,D.
TITLE Isolation of a cDNA probe for a human jejunal brush-border
hydrolase, sucrase-isomaltase, and assignment of the gene locus to
chromosome 3
JOURNAL Gene 57 (1), 101-110 (1987)
PUBMED 2962903
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AC140119.3, DA919374.1,
BC132860.1, AC092695.8 and BG187733.1.
This sequence is a reference standard in the RefSeqGene project.
On Sep 19, 2007 this sequence version replaced NP_001032.1.
Summary: This gene encodes a sucrase-isomaltase enzyme that is
expressed in the intestinal brush border. The encoded protein is
synthesized as a precursor protein that is cleaved by pancreatic
proteases into two enzymatic subunits sucrase and isomaltase. These
two subunits heterodimerize to form the sucrose-isomaltase complex.
This complex is essential for the digestion of dietary
carbohydrates including starch, sucrose and isomaltose. Mutations
in this gene are the cause of congenital sucrase-isomaltase
deficiency.[provided by RefSeq, Apr 2010].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: X63597.1, BC132834.1 [ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1966682,
SAMEA1968189 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000264382.8/ ENSP00000264382.3
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..1827
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="3"
/map="3q26.1"
Protein 1..1827
/product="sucrase-isomaltase, intestinal"
/EC_number="3.2.1.10"
/EC_number="3.2.1.48"
/note="oligosaccharide alpha-1,6-glucosidase;
alpha-glucosidase; Oligo-1,6-glucosidase;
Alpha-methylglucosidase"
/calculated_mol_wt=209323
mat_peptide 2..1007
/product="isomaltase"
/calculated_mol_wt=114207
Site 7
/site_type="phosphorylation"
/note="Phosphoserine, by PKA.
/evidence=ECO:0000269|PubMed:8521865; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 13..32
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
Region 40..61
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
Region 63..108
/region_name="Trefoil"
/note="Trefoil (P-type) domain; pfam00088"
/db_xref="CDD:459666"
Site order(81,104..105)
/site_type="other"
/note="putative ligand binding site [chemical binding]"
/db_xref="CDD:238059"
Site order(96,104)
/site_type="active"
/note="putative binding specificity loop [active]"
/db_xref="CDD:238059"
Site 99
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:20356844; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Region 110..1007
/region_name="Isomaltase"
/note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
Region 125..235
/region_name="NtCtMGAM_N"
/note="N-terminal barrel of NtMGAM and CtMGAM,
maltase-glucoamylase; pfam16863"
/db_xref="CDD:465286"
Region 227..333
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 237
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 239
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 264
/site_type="active"
/db_xref="CDD:270212"
Region 343..707
/region_name="GH31_MGAM_SI_GAA"
/note="maltase-glucoamylase, sucrase-isomaltase, lysosomal
acid alpha-glucosidase; cd06602"
/db_xref="CDD:269888"
Site order(360,388..389,425,468,503,505..506,588,601,604,637,
662)
/site_type="active"
/db_xref="CDD:269888"
Site 391
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 400
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 437
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 455
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:20356844; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 667
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 763
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 765
/site_type="sulfatation"
/note="Sulfotyrosine. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (P14410.6)"
Site 823
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 855
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:20356844; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 904
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:20356844; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 926
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Region 935..980
/region_name="PD"
/note="P or trefoil or TFF domain; smart00018"
/db_xref="CDD:197472"
Site order(946,972..973)
/site_type="other"
/note="putative ligand binding site [chemical binding]"
/db_xref="CDD:238059"
Site order(963,972)
/site_type="active"
/note="putative binding specificity loop [active]"
/db_xref="CDD:238059"
Region 994..1108
/region_name="NtCtMGAM_N"
/note="N-terminal barrel of NtMGAM and CtMGAM,
maltase-glucoamylase; pfam16863"
/db_xref="CDD:465286"
mat_peptide 1008..1827
/product="sucrase"
/calculated_mol_wt=95134
Region 1008..1827
/region_name="Sucrase"
/note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
Region 1100..1214
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 1137
/site_type="active"
/db_xref="CDD:270212"
Region 1195..1691
/region_name="Glyco_hydro_31"
/note="Glycosyl hydrolases family 31; pfam01055"
/db_xref="CDD:460044"
Site 1235
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1303
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1340
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1354
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1403
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1535
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1572
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1675
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1748
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1763
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
Site 1815
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P14410.6)"
CDS 1..1827
/gene="SI"
/coded_by="NM_001041.4:65..5548"
/db_xref="CCDS:CCDS3196.1"
/db_xref="GeneID:6476"
/db_xref="HGNC:HGNC:10856"
/db_xref="MIM:609845"
ORIGIN
1 markkfsgle islivlfviv tiiaialivv latktpavde isdststpat trvttnpsds
61 gkcpnvlndp vnvrincipe qfptegicaq rgccwrpwnd slipwcffvd nhgynvqdmt
121 ttsigveakl nripsptlfg ndinsvlftt qnqtpnrfrf kitdpnnrry evphqyvkef
181 tgptvsdtly dvkvaqnpfs iqvirksngk tlfdtsigpl vysdqylqis trlpsdyiyg
241 igeqvhkrfr hdlswktwpi ftrdqlpgdn nnnlyghqtf fmciedtsgk sfgvflmnsn
301 ameifiqptp ivtyrvtggi ldfyillgdt peqvvqqyqq lvglpampay wnlgfqlsrw
361 nyksldvvke vvrrnreagi pfdtqvtdid ymedkkdfty dqvafnglpq fvqdlhdhgq
421 kyviildpai sigrrangtt yatyergntq hvwinesdgs tpiigevwpg ltvypdftnp
481 ncidwwanec sifhqevqyd glwidmnevs sfiqgstkgc nvnklnyppf tpdildklmy
541 skticmdavq nwgkqydvhs lygysmaiat eqavqkvfpn krsfiltrst fagsgrhaah
601 wlgdntaswe qmewsitgml efslfgiplv gadicgfvae tteelcrrwm qlgafypfsr
661 nhnsdgyehq dpaffgqnsl lvkssrqylt irytllpfly tlfykahvfg etvarpvlhe
721 fyedtnswie dteflwgpal litpvlkqga dtvsayipda iwydyesgak rpwrkqrvdm
781 ylpadkiglh lrggyiipiq epdvtttasr knplglival genntakgdf fwddgetkdt
841 iqngnyilyt fsvsnntldi vcthssyqeg ttlafqtvki lgltdsvtev rvaennqpmn
901 ahsnftydas nqvlliadlk lnlgrnfsvq wnqifsener fncypdadla teqkctqrgc
961 vwrtgsslsk apecyfprqd nsysvnsary ssmgitadlq lntanarikl psdpistlrv
1021 evkyhkndml qfkiydpqkk ryevpvplni pttpistyed rlydveiken pfgiqirrrs
1081 sgrviwdswl pgfafndqfi qistrlpsey iygfgeveht afkrdlnwnt wgmftrdqpp
1141 gyklnsygfh pyymaleeeg nahgvfllns namdvtfqpt paltyrtvgg ildfymflgp
1201 tpevatkqyh evighpvmpa ywalgfqlcr ygyantsevr elydamvaan ipydvqytdi
1261 dymerqldft igeafqdlpq fvdkirgegm ryiiildpai sgnetktypa fergqqndvf
1321 vkwpntndic wakvwpdlpn itidktlted eavnasrahv afpdffrtst aewwareivd
1381 fynekmkfdg lwidmnepss fvngtttnqc rndelnyppy fpeltkrtdg lhfrticmea
1441 eqilsdgtsv lhydvhnlyg wsqmkpthda lqkttgkrgi visrstypts grwgghwlgd
1501 nyarwdnmdk siigmmefsl fgmsytgadi cgffnnseyh lctrwmqlga fypysrnhni
1561 antrrqdpas wnetfaemsr nilnirytll pyfytqmhei hanggtvirp llheffdekp
1621 twdifkqflw gpafmvtpvl epyvqtvnay vpnarwfdyh tgkdigvrgq fqtfnasydt
1681 inlhvrgghi lpcqepaqnt fysrqkhmkl ivaaddnqma qgslfwddge sidtyerdly
1741 lsvqfnlnqt tltstilkrg yinksetrlg slhvwgkgtt pvnavtltyn gnknslpfne
1801 dttnmilrid ltthnvtlee pieinws
//