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

 SUIS_RAT                Reviewed;        1841 AA.
P23739;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
23-MAY-2018, entry version 146.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Intestine;
PubMed=7821806; DOI=10.1016/0378-1119(94)90452-9;
Chandrasena G., Osterholm D.E., Sunitha I., Henning S.J.;
"Cloning and sequencing of a full-length rat sucrase-isomaltase-
encoding cDNA.";
Gene 150:355-360(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 87-362.
STRAIN=Fischer 344; TISSUE=Intestine;
PubMed=2268340; DOI=10.1016/S0006-291X(05)80853-8;
Traber P.G.;
"Regulation of sucrase-isomaltase gene expression along the crypt-
villus axis of rat small intestine.";
Biochem. Biophys. Res. Commun. 173:765-773(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 733-1373.
STRAIN=Sprague-Dawley; TISSUE=Duodenum;
PubMed=2400788; DOI=10.1016/0167-4781(90)90121-H;
Broyart J.-P., Hugot J.-P., Perret C., Porteu A.;
"Molecular cloning and characterization of a rat intestinal sucrase-
isomaltase cDNA. Regulation of sucrase-isomaltase gene expression by
sucrose feeding.";
Biochim. Biophys. Acta 1087:61-67(1990).
[4]
PROTEIN SEQUENCE OF N-TERMINUS OF ISOMALTASE AND SUCRASE.
PubMed=6802834;
Hauri H.-P., Wacker H., Rickli E.E., Bigler-Meier B., Quaroni A.,
Semenza G.;
"Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal
amino acid sequence of the rat sucrase-isomaltase precursor (pro-
sucrase-isomaltase) from fetal intestinal transplants.";
J. Biol. Chem. 257:4522-4528(1982).
-!- 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.
-!- 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.
-!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
membrane protein. Note=Brush border.
-!- PTM: The precursor is proteolytically cleaved when exposed to
pancreatic proteases in the intestinal lumen.
-!- PTM: Sulfated. {ECO:0000250}.
-!- 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; L25926; AAA65097.1; -; mRNA.
EMBL; M62889; AAA42144.1; -; mRNA.
EMBL; X15546; CAA33552.1; -; mRNA.
PIR; S11386; S11386.
PIR; T10799; T10799.
RefSeq; NP_037193.1; NM_013061.1.
UniGene; Rn.10057; -.
ProteinModelPortal; P23739; -.
SMR; P23739; -.
BindingDB; P23739; -.
ChEMBL; CHEMBL3114; -.
CAZy; GH31; Glycoside Hydrolase Family 31.
iPTMnet; P23739; -.
PhosphoSitePlus; P23739; -.
PRIDE; P23739; -.
GeneID; 497756; -.
KEGG; rno:497756; -.
UCSC; RGD:3675; rat.
CTD; 6476; -.
RGD; 3675; Si.
HOGENOM; HOG000067936; -.
HOVERGEN; HBG080721; -.
InParanoid; P23739; -.
KO; K01203; -.
PhylomeDB; P23739; -.
BRENDA; 3.2.1.10; 5301.
SABIO-RK; P23739; -.
PRO; PR:P23739; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005903; C:brush border; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0004564; F:beta-fructofuranosidase activity; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:RGD.
GO; GO:0004575; F:sucrose alpha-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0009750; P:response to fructose; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0042594; P:response to starvation; IEP:RGD.
GO; GO:0009744; P:response to sucrose; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
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; 1.
PROSITE; PS00025; P_TREFOIL_1; 1.
PROSITE; PS51448; P_TREFOIL_2; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
Multifunctional enzyme; Phosphoprotein; Reference proteome; Repeat;
Signal-anchor; Sulfation; Transmembrane; Transmembrane helix.
CHAIN 1 1841 Sucrase-isomaltase, intestinal.
/FTId=PRO_0000018559.
CHAIN 1 1013 Isomaltase.
/FTId=PRO_0000018560.
CHAIN 1014 1841 Sucrase.
/FTId=PRO_0000018561.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 1841 Lumenal. {ECO:0000255}.
DOMAIN 71 120 P-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
DOMAIN 936 984 P-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
REGION 120 1013 Isomaltase.
REGION 1014 1841 Sucrase.
COMPBIAS 43 70 Ser/Thr-rich.
ACT_SITE 514 514 Nucleophile; for isomaltase activity.
{ECO:0000255|PROSITE-ProRule:PRU10066}.
ACT_SITE 615 615 For isomaltase activity. {ECO:0000250}.
ACT_SITE 1399 1399 Nucleophile; for sucrase activity.
{ECO:0000255|PROSITE-ProRule:PRU10066}.
ACT_SITE 1402 1402 For sucrase activity. {ECO:0000250}.
ACT_SITE 1512 1512 Proton donor; for sucrase activity.
{ECO:0000250}.
BINDING 274 274 Substrate. {ECO:0000250}.
BINDING 398 398 Substrate. {ECO:0000250}.
BINDING 599 599 Substrate. {ECO:0000250}.
BINDING 673 673 Substrate. {ECO:0000250}.
MOD_RES 7 7 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P14410}.
MOD_RES 401 401 Sulfotyrosine. {ECO:0000255}.
MOD_RES 410 410 Sulfotyrosine. {ECO:0000255}.
MOD_RES 1387 1387 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 758 758 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 765 765 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 867 867 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 910 910 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1240 1240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1308 1308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1345 1345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1359 1359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1373 1373 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1485 1485 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1513 1513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1575 1575 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1762 1762 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1829 1829 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 73 104 {ECO:0000255|PROSITE-ProRule:PRU00779}.
DISULFID 87 103 {ECO:0000255|PROSITE-ProRule:PRU00779}.
DISULFID 98 116 {ECO:0000255|PROSITE-ProRule:PRU00779}.
DISULFID 646 657 {ECO:0000255|PROSITE-ProRule:PRU00779}.
CONFLICT 87 87 C -> W (in Ref. 1; AAA65097).
{ECO:0000305}.
CONFLICT 92 92 H -> S (in Ref. 2; AAA42144).
{ECO:0000305}.
CONFLICT 95 95 K -> Q (in Ref. 2; AAA42144).
{ECO:0000305}.
CONFLICT 736 736 E -> V (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 842 842 E -> Q (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 916 916 A -> T (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 924 924 A -> R (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 930 931 AG -> GT (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 938 939 CR -> SQ (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 959 962 GTCT -> ETDK (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 980 980 Y -> C (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 986 986 N -> H (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 997 998 LP -> SL (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1010 1010 P -> A (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1023 1023 T -> P (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1027 1027 G -> E (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1032 1032 P -> K (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1094 1094 R -> S (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1099 1099 G -> A (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1302 1302 A -> D (in Ref. 3; CAA33552).
{ECO:0000305}.
CONFLICT 1337 1340 PKVW -> AKWG (in Ref. 3; CAA33552).
{ECO:0000305}.
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


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