SUIS_RABIT
ID SUIS_RABIT Reviewed; 1827 AA.
AC P07768;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3755079; DOI=10.1016/0092-8674(86)90739-7;
RA Hunziker W., Spiess M., Semenza G., Lodish H.F.;
RT "The sucrase-isomaltase complex: primary structure, membrane-orientation,
RT and evolution of a stalked, intrinsic brush border protein.";
RL Cell 46:227-234(1986).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-38 AND 1008-1015.
RX PubMed=7152027; DOI=10.1016/0014-5793(82)80833-8;
RA Sjoestroem H., Noren O., Christiansen L.A., Wacker H., Spiess M.,
RA Bigler-Meier B., Rickli E.E., Semenza G.;
RT "N-terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase-
RT isomaltase. Implications for the biosynthesis and membrane insertion of
RT pro-sucrase-isomaltase.";
RL FEBS Lett. 148:321-325(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: N- and O-glycosylated.
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; M14046; AAA31459.1; -; mRNA.
DR PIR; A23945; A23945.
DR RefSeq; NP_001075735.1; NM_001082266.1.
DR AlphaFoldDB; P07768; -.
DR SMR; P07768; -.
DR STRING; 9986.ENSOCUP00000003372; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PRIDE; P07768; -.
DR GeneID; 100009093; -.
DR KEGG; ocu:100009093; -.
DR CTD; 6476; -.
DR eggNOG; KOG1065; Eukaryota.
DR InParanoid; P07768; -.
DR OrthoDB; 151244at2759; -.
DR BRENDA; 3.2.1.10; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 2.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1827
FT /note="Sucrase-isomaltase, intestinal"
FT /id="PRO_0000018556"
FT CHAIN 2..1007
FT /note="Isomaltase"
FT /id="PRO_0000018557"
FT CHAIN 1008..1827
FT /note="Sucrase"
FT /id="PRO_0000018558"
FT TOPO_DOM 2..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..1827
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 61..110
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 932..978
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..1007
FT /note="Isomaltase"
FT REGION 1008..1827
FT /note="Sucrase"
FT ACT_SITE 505
FT /note="Nucleophile; for isomaltase activity"
FT ACT_SITE 604
FT /note="For isomaltase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1394
FT /note="Nucleophile; for sucrase activity"
FT ACT_SITE 1397
FT /note="For sucrase activity"
FT ACT_SITE 1500
FT /note="Proton donor; for sucrase activity"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 662
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 391
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 400
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1382
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1385
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 77..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 88..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 520..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 635..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 1827 AA; 210140 MW; 2CEFFE3109AC8917 CRC64;
MAKRKFSGLE ITLIVLFVIV FIIAIALIAV LATKTPAVEE VNPSSSTPTT TSTTTSTSGS
VSCPSELNEV VNERINCIPE QSPTQAICAQ RNCCWRPWNN SDIPWCFFVD NHGYNVEGMT
TTSTGLEARL NRKSTPTLFG NDINNVLLTT ESQTANRLRF KLTDPNNKRY EVPHQFVTEF
AGPAATETLY DVQVTENPFS IKVIRKSNNR ILFDSSIGPL VYSDQYLQIS TRLPSEYMYG
FGEHVHKRFR HDLYWKTWPI FTRDQHTDDN NNNLYGHQTF FMCIEDTTGK SFGVFLMNSN
AMEIFIQPTP IVTYRVIGGI LDFYIFLGDT PEQVVQQYQE LIGRPAMPAY WSLGFQLSRW
NYNSLDVVKE VVRRNREALI PFDTQVSDID YMEDKKDFTY DRVAYNGLPD FVQDLHDHGQ
KYVIILDPAI SINRRASGEA YESYDRGNAQ NVWVNESDGT TPIVGEVWPG DTVYPDFTSP
NCIEWWANEC NIFHQEVNYD GLWIDMNEVS SFVQGSNKGC NDNTLNYPPY IPDIVDKLMY
SKTLCMDSVQ YWGKQYDVHS LYGYSMAIAT ERAVERVFPN KRSFILTRST FAGSGRHAAH
WLGDNTATWE QMEWSITGML EFGLFGMPLV GADICGFLAE TTEELCRRWM QLGAFYPFSR
NHNADGFEHQ DPAFFGQDSL LVKSSRHYLN IRYTLLPFLY TLFYKAHAFG ETVARPVLHE
FYEDTNSWVE DREFLWGPAL LITPVLTQGA ETVSAYIPDA VWYDYETGAK RPWRKQRVEM
SLPADKIGLH LRGGYIIPIQ QPAVTTTASR MNPLGLIIAL NDDNTAVGDF FWDDGETKDT
VQNDNYILYT FAVSNNNLNI TCTHELYSEG TTLAFQTIKI LGVTETVTQV TVAENNQSMS
THSNFTYDPS NQVLLIENLN FNLGRNFRVQ WDQTFLESEK ITCYPDADIA TQEKCTQRGC
IWDTNTVNPR APECYFPKTD NPYSVSSTQY SPTGITADLQ LNPTRTRITL PSEPITNLRV
EVKYHKNDMV QFKIFDPQNK RYEVPVPLDI PATPTSTQEN RLYDVEIKEN PFGIQIRRRS
TGKVIWDSCL PGFAFNDQFI QISTRLPSEY IYGFGEAEHT AFKRDLNWHT WGMFTRDQPP
GYKLNSYGFH PYYMALEDEG NAHGVLLLNS NAMDVTFMPT PALTYRVIGG ILDFYMFLGP
TPEVATQQYH EVIGHPVMPP YWSLGFQLCR YGYRNTSEII ELYEGMVAAD IPYDVQYTDI
DYMERQLDFT IDENFRELPQ FVDRIRGEGM RYIIILDPAI SGNETRPYPA FDRGEAKDVF
VKWPNTSDIC WAKVWPDLPN ITIDESLTED EAVNASRAHA AFPDFFRNST AEWWTREILD
FYNNYMKFDG LWIDMNEPSS FVNGTTTNVC RNTELNYPPY FPELTKRTDG LHFRTMCMET
EHILSDGSSV LHYDVHNLYG WSQAKPTYDA LQKTTGKRGI VISRSTYPTA GRWAGHWLGD
NYARWDNMDK SIIGMMEFSL FGISYTGADI CGFFNDSEYH LCTRWTQLGA FYPFARNHNI
QFTRRQDPVS WNQTFVEMTR NVLNIRYTLL PYFYTQLHEI HAHGGTVIRP LMHEFFDDRT
TWDIFLQFLW GPAFMVTPVL EPYTTVVRGY VPNARWFDYH TGEDIGIRGQ VQDLTLLMNA
INLHVRGGHI LPCQEPARTT FLSRQKYMKL IVAADDNHMA QGSLFWDDGD TIDTYERDLY
LSVQFNLNKT TLTSTLLKTG YINKTEIRLG YVHVWGIGNT LINEVNLMYN EINYPLIFNQ
TQAQEILNID LTAHEVTLDD PIEISWS
