SUIS_RAT
ID SUIS_RAT Reviewed; 1841 AA.
AC P23739;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sucrase-isomaltase, intestinal;
DE Contains:
DE RecName: Full=Sucrase;
DE EC=3.2.1.48;
DE Contains:
DE RecName: Full=Isomaltase;
DE EC=3.2.1.10;
GN Name=Si;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX PubMed=7821806; DOI=10.1016/0378-1119(94)90452-9;
RA Chandrasena G., Osterholm D.E., Sunitha I., Henning S.J.;
RT "Cloning and sequencing of a full-length rat sucrase-isomaltase-encoding
RT cDNA.";
RL Gene 150:355-360(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-362.
RC STRAIN=Fischer 344; TISSUE=Intestine;
RX PubMed=2268340; DOI=10.1016/s0006-291x(05)80853-8;
RA Traber P.G.;
RT "Regulation of sucrase-isomaltase gene expression along the crypt-villus
RT axis of rat small intestine.";
RL Biochem. Biophys. Res. Commun. 173:765-773(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 733-1373.
RC STRAIN=Sprague-Dawley; TISSUE=Duodenum;
RX PubMed=2400788; DOI=10.1016/0167-4781(90)90121-h;
RA Broyart J.-P., Hugot J.-P., Perret C., Porteu A.;
RT "Molecular cloning and characterization of a rat intestinal sucrase-
RT isomaltase cDNA. Regulation of sucrase-isomaltase gene expression by
RT sucrose feeding.";
RL Biochim. Biophys. Acta 1087:61-67(1990).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS OF ISOMALTASE AND SUCRASE.
RX PubMed=6802834; DOI=10.1016/s0021-9258(18)34754-9;
RA Hauri H.-P., Wacker H., Rickli E.E., Bigler-Meier B., Quaroni A.,
RA Semenza G.;
RT "Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal amino
RT acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-
RT isomaltase) from fetal intestinal transplants.";
RL J. Biol. Chem. 257:4522-4528(1982).
CC -!- FUNCTION: Plays an important role in the final stage of carbohydrate
CC digestion. Isomaltase activity is specific for both alpha-1,4- and
CC alpha-1,6-oligosaccharides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-
CC type action.; EC=3.2.1.48;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC oligosaccharides produced from starch and glycogen by alpha-amylase,
CC and in isomaltose.; EC=3.2.1.10;
CC -!- SUBUNIT: The resulting sucrase and isomaltase subunits stay associated
CC with one another in a complex by non-covalent linkages.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
CC membrane protein. Note=Brush border.
CC -!- PTM: The precursor is proteolytically cleaved when exposed to
CC pancreatic proteases in the intestinal lumen.
CC -!- PTM: Sulfated. {ECO:0000250}.
CC -!- MISCELLANEOUS: There is a high degree of homology between the
CC isomaltase and sucrase portions (41% of amino acid identity) indicating
CC that this protein is evolved by partial gene duplication.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; L25926; AAA65097.1; -; mRNA.
DR EMBL; M62889; AAA42144.1; -; mRNA.
DR EMBL; X15546; CAA33552.1; -; mRNA.
DR PIR; S11386; S11386.
DR PIR; T10799; T10799.
DR RefSeq; NP_037193.1; NM_013061.1.
DR AlphaFoldDB; P23739; -.
DR SMR; P23739; -.
DR STRING; 10116.ENSRNOP00000045106; -.
DR BindingDB; P23739; -.
DR ChEMBL; CHEMBL3114; -.
DR DrugCentral; P23739; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyGen; P23739; 16 sites.
DR iPTMnet; P23739; -.
DR PhosphoSitePlus; P23739; -.
DR PRIDE; P23739; -.
DR GeneID; 497756; -.
DR UCSC; RGD:3675; rat.
DR CTD; 6476; -.
DR RGD; 3675; Si.
DR eggNOG; KOG1065; Eukaryota.
DR InParanoid; P23739; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; P23739; -.
DR BRENDA; 3.2.1.10; 5301.
DR Reactome; R-RNO-189085; Digestion of dietary carbohydrate.
DR SABIO-RK; P23739; -.
DR PRO; PR:P23739; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:RGD.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009750; P:response to fructose; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009744; P:response to sucrose; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0005987; P:sucrose catabolic process; ISO:RGD.
DR CDD; cd00111; Trefoil; 2.
DR Gene3D; 2.60.40.1180; -; 4.
DR Gene3D; 4.10.110.10; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR Pfam; PF01055; Glyco_hydro_31; 2.
DR Pfam; PF16863; NtCtMGAM_N; 2.
DR Pfam; PF00088; Trefoil; 2.
DR SMART; SM00018; PD; 2.
DR SUPFAM; SSF51445; SSF51445; 2.
DR SUPFAM; SSF57492; SSF57492; 1.
DR SUPFAM; SSF74650; SSF74650; 2.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 2.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Membrane; Multifunctional enzyme; Phosphoprotein;
KW Reference proteome; Repeat; Signal-anchor; Sulfation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1841
FT /note="Sucrase-isomaltase, intestinal"
FT /id="PRO_0000018559"
FT CHAIN 1..1013
FT /note="Isomaltase"
FT /id="PRO_0000018560"
FT CHAIN 1014..1841
FT /note="Sucrase"
FT /id="PRO_0000018561"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..1841
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 71..120
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 936..984
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 42..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..1013
FT /note="Isomaltase"
FT REGION 1014..1841
FT /note="Sucrase"
FT COMPBIAS 42..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 514
FT /note="Nucleophile; for isomaltase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 615
FT /note="For isomaltase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1399
FT /note="Nucleophile; for sucrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 1402
FT /note="For sucrase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1512
FT /note="Proton donor; for sucrase activity"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 673
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P14410"
FT MOD_RES 401
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 410
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1387
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 87..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 98..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 646..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT CONFLICT 87
FT /note="C -> W (in Ref. 1; AAA65097)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="H -> S (in Ref. 2; AAA42144)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="K -> Q (in Ref. 2; AAA42144)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="E -> V (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="E -> Q (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="A -> T (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="A -> R (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 930..931
FT /note="AG -> GT (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 938..939
FT /note="CR -> SQ (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 959..962
FT /note="GTCT -> ETDK (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="Y -> C (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="N -> H (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 997..998
FT /note="LP -> SL (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="P -> A (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="T -> P (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1027
FT /note="G -> E (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="P -> K (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094
FT /note="R -> S (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1099
FT /note="G -> A (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302
FT /note="A -> D (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1337..1340
FT /note="PKVW -> AKWG (in Ref. 3; CAA33552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1841 AA; 210350 MW; E186B8632475EE09 CRC64;
MAKKKFSALE ISLIVLFIIV TAIAIALVTV LATKVPAVEE IKSPTPTSNS TPTSTPTSTS
TPTSTSTPSP GKCPPEQGEP INERINCIPE QHPTKAICEE RGCCWRPWNN TVIPWCFFAD
NHGYNAESIT NENAGLKATL NRIPSPTLFG EDIKSVILTT QTQTGNRFRF KITDPNNKRY
EVPHQFVKEE TGIPAADTLY DVQVSENPFS IKVIRKSNNK VLCDTSVGPL LYSNQYLQIS
TRLPSEYIYG FGGHIHKRFR HDLYWKTWPI FTRDEIPGDN NHNLYGHQTF FMGIGDTSGK
SYGVFLMNSN AMEVFIQPTP IITYRVTGGI LDFYIFLGDT PEQVVQQYQE VHWRPAMPAY
WNLGFQLSRW NYGSLDTVSE VVRRNREAGI PYDAQVTDID YMEDHKEFTY DRVKFNGLPE
FAQDLHNHGK YIIILDPAIS INKRANGAEY QTYVRGNEKN VWVNESDGTT PLIGEVWPGL
TVYPDFTNPQ TIEWWANECN LFHQQVEYDG LWIDMNEVSS FIQGSLNLKG VLLIVLNYPP
FTPGILDKVM YSKTLCMDAV QHWGKQYDVH SLYGYSMAIA TEQAVERVFP NKRSFILTRS
TFGGSGRHAN HWLGDNTASW EQMEWSITGM LEFGIFGMPL VGATSCGFLA DTTEELCRRW
MQLGAFYPFS RNHNAEGYME QDPAYFGQDS SRHYLTIRYT LLPFLYTLFY RAHMFGETVA
RPFLYEFYDD TNSWIEDTQF LWGPALLITP VLRPGVENVS AYIPNATWYD YETGIKRPWR
KERINMYLPG DKIGLHLRGG YIIPTQEPDV TTTASRKNPL GLIVALDDNQ AAKGELFWDD
GESKDSIEKK MYILYTFSVS NNELVLNCTH SSYAEGTSLA FKTIKVLGLR EDVRSITVGE
NDQQMATHTN FTFDSANKIL SITALNFNLA GSFIVRWCRT FSDNEKFTCY PDVGTATEGT
CTQRGCLWQP VSGLSNVPPY YFPPENNPYT LTSIQPLPTG ITAELQLNPP NARIKLPSNP
ISTLRVGVKY HPNDMLQFKI YDAQHKRYEV PVPLNIPDTP TSSNERLYDV EIKENPFGIQ
VRRRSSGKLI WDSRLPGFGF NDQFIQISTR LPSNYLYGFG EVEHTAFKRD LNWHTWGMFT
RDQPPGYKLN SYGFHPYYMA LENEGNAHGV LLLNSNGMDV TFQPTPALTY RTIGGILDFY
MFLGPTPEIA TRQYHEVIGF PVMPPYWALG FQLCRYGYRN TSEIEQLYND MVAANIPYDV
QYTDINYMER QLDFTIGERF KTLPEFVDRI RKDGMKYIVI LAPAISGNET QPYPAFERGI
QKDVFVKWPN TNDICWPKVW PDLPNVTIDE TITEDEAVNA SRAHVAFPDF FRNSTLEWWA
REIYDFYNEK MKFDGLWIDM NEPSSFGIQM GGKVLNECRR MMTLNYPPVF SPELRVKEGE
GASISEAMCM ETEHILIDGS SVLQYDVHNL YGWSQVKPTL DALQNTTGLR GIVISRSTYP
TTGRWGGHWL GDNYTTWDNL EKSLIGMLEL NLFGIPYIGA DICGVFHDSG YPSLYFVGIQ
VGAFYPYPRE SPTINFTRSQ DPVSWMKLLL QMSKKVLEIR YTLLPYFYTQ MHEAHAHGGT
VIRPLMHEFF DDKETWEIYK QFLWGPAFMV TPVVEPFRTS VTGYVPKARW FDYHTGADIK
LKGILHTFSA PFDTINLHVR GGYILPCQEP ARNTHLSRQN YMKLIVAADD NQMAQGTLFG
DDGESIDTYE RGQYTSIQFN LNQTTLTSTV LANGYKNKQE MRLGSIHIWG KGTLRISNAN
LVYGGRKHQP PFTQEEAKET LIFDLKNMNV TLDEPIQITW S
