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sucrase-isomaltase, intestinal [Homo sapiens]

NCBI Reference Sequence: NP_001032.2

Identical Proteins FASTA Graphics 

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
//
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Protein 3D Structure

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Reference sequence information

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