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O62653

- SUIS_SUNMU

UniProt

O62653 - SUIS_SUNMU

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Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Suncus murinus (Asian house shrew) (Musk shrew)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei250 – 2501SubstrateBy similarity
Binding sitei374 – 3741SubstrateBy similarity
Active sitei491 – 4911Nucleophile; for isomaltase activityPROSITE-ProRule annotation
Binding sitei574 – 5741SubstrateBy similarity
Active sitei590 – 5901For isomaltase activityBy similarity
Binding sitei648 – 6481SubstrateBy similarity
Active sitei1380 – 13801Nucleophile; for sucrase activityPROSITE-ProRule annotation
Active sitei1383 – 13831For sucrase activityBy similarity
Active sitei1486 – 14861Proton donor; for sucrase activityBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. oligo-1,6-glucosidase activity Source: UniProtKB-EC
  3. sucrose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

SABIO-RKO62653.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrase-isomaltase, intestinal
Cleaved into the following 2 chains:
Gene namesi
Name:SI
OrganismiSuncus murinus (Asian house shrew) (Musk shrew)
Taxonomic identifieri9378 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaInsectivoraSoricidaeCrocidurinaeSuncus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 18131781LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 18131812Sucrase-isomaltase, intestinalPRO_0000018562Add
BLAST
Chaini2 – 991990IsomaltaseBy similarityPRO_0000018563Add
BLAST
Chaini992 – 1813822SucraseBy similarityPRO_0000018564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by PKABy similarity
Disulfide bondi48 ↔ 79PROSITE-ProRule annotation
Disulfide bondi62 ↔ 78PROSITE-ProRule annotation
Disulfide bondi73 ↔ 91PROSITE-ProRule annotation
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Modified residuei377 – 3771SulfotyrosineSequence Analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi506 ↔ 531PROSITE-ProRule annotation
Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi896 – 8961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi911 – 9111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1221 – 12211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1289 – 12891N-linked (GlcNAc...)Sequence Analysis
Modified residuei1294 – 12941SulfotyrosineSequence Analysis
Glycosylationi1326 – 13261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
Modified residuei1368 – 13681SulfotyrosineSequence Analysis
Modified residuei1371 – 13711SulfotyrosineSequence Analysis
Glycosylationi1432 – 14321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1521 – 15211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1545 – 15451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1558 – 15581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1703 – 17031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1772 – 17721N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.By similarity
Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Interactioni

Subunit structurei

The resulting sucrase and isomaltase subunits stay associated with one another in a complex by non-covalent linkages.By similarity

Structurei

3D structure databases

ProteinModelPortaliO62653.
SMRiO62653. Positions 56-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 9550P-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini917 – 96246P-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 991897IsomaltaseAdd
BLAST
Regioni992 – 1813822SucraseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 454Ser/Thr-rich

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated
Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG080721.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O62653-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARKKSSGLK ITLIVLLAIV TIIAIALVAI LPTKTPAVEL VSTIPGKCPS
60 70 80 90 100
AENDRLDEKI NCIPDQFPTQ ALCAMQGCCW NPRNESPTPW CSFANNHGYE
110 120 130 140 150
FEKISNPNIN FEPNLKKNSP PTLFGDNITN LLLTTQSQTA NRFRFKITDP
160 170 180 190 200
NNQRYEVPHQ FVNKDFSGPP ASNPLYDVKI TENPFSIKVI RKSNNKILFD
210 220 230 240 250
TSIGPLVYSN QYLQISTKLP SKYIYGLGEH VHKRFRHDLY WKTWPIFTRD
260 270 280 290 300
QLPGDNNNNL YGHQTFFMSI EDTSGKSFGV FLMNSNAMEV FIQPTPIVTY
310 320 330 340 350
RVIGGILDFY IFLGDTPGQV VQQYQELTGR PAMPSYWSLG FQLSRWNYGS
360 370 380 390 400
LDAVKEVVKR NRDARIPFDA QVTDIDYMED KKDFTYNNKT FYGLPEFVKD
410 420 430 440 450
LHDHGQKYII ILDPAISITS LANGNHYKTY ERGNEQKVWV YQSDGTTPLI
460 470 480 490 500
GEVWPGLTVY PDFTNPKCLD WWTNECSIFH EEIKYDGLWI DMNEVSSFVH
510 520 530 540 550
GSTKGCSDNK LNYPPFIPDI LDKLMYAKTI CMDAIQHWGK QYDVHSLYGY
560 570 580 590 600
SMAIATEKAI EKVFPNKRSF ILTRSTFAGT GKHATHWLGD NTPSWEHMEW
610 620 630 640 650
SITPMLEFGL FGMPFIGADI CGFVVDTTEE LCRRWMQIGA FYPYFRDHNA
660 670 680 690 700
GGYMPQDPAY FGQDSLLVNT SRHYLDIWYT LLPYLYNLLY KAYVYGETVA
710 720 730 740 750
RPFLYEFYED TNSWIEDLQF LWGSALLITP VLRQGADRMS AYIPDATWYD
760 770 780 790 800
YETGGKRTWR KQRVEMYLPG DKIGLHVRGG YIIPTQQPAV NTTASRKNPL
810 820 830 840 850
GLIIALDNNA AKGDFFWDDG ESKDSIEKGK YILYTFSVLN NELDIICTHS
860 870 880 890 900
SYQEGTTLAF ETIKILGLAN TVTQVQVAEN NQQTIIHNSF TYHASNQSLI
910 920 930 940 950
IDNLKLNLGK NFTVQWNQVS LDSEKIDCFP DNNPENKQNC EERGCLWEPN
960 970 980 990 1000
SAAEGPRCYF PKQYNPYLVK STQYSSMGIT VDLELNTATA RIKMPSNPIS
1010 1020 1030 1040 1050
VLRLEVKYHK NDMLQFKIYD PQNKRYEVPI PMDIPTTPTS TYENRLYDVN
1060 1070 1080 1090 1100
IKGNPFGIQI RRRSTGRIFW DSCLPWGLLL MNQFIQISTR LPSEYVYGFG
1110 1120 1130 1140 1150
GVGHRQFKQD LNWHKWGMFN RDQPSGYKIS SYGFQPYIYM ALGDGGNAHG
1160 1170 1180 1190 1200
VFLLNSNAMD VTFQPNPALT YRTIGGILDF YMFLGPNPEV ATKQYHEVIG
1210 1220 1230 1240 1250
RPVKPPYWAL GFHLCRYGYE NTSEIRQLYE DMVSAQIPYD VQYTDIDYME
1260 1270 1280 1290 1300
RQLDFTIGKG FQDLPEFVDK IRDEGMKYII ILDPAISGNE TQDYLAFQRG
1310 1320 1330 1340 1350
IEKDVFVKWP NTQDICWAKV WPDLPNITID DSLTEDEAVN ASRAHVAFPD
1360 1370 1380 1390 1400
FLKTSTAEWW ATEIEDFYNT YMKFDGLWID MNEPSSFVHG SVDNKCRNEI
1410 1420 1430 1440 1450
LNYPPYMPAL TKRNEGLHFR TMCMETQQTL SNGSSVLHYD VHNLYGWSQA
1460 1470 1480 1490 1500
KPTYDALQKT TGKRGIVISR STYPSAGRWA GHWLGDNYAN WDKIGKSIIG
1510 1520 1530 1540 1550
MMEFSLFGIS FTGADICGFF NNSDYELCAR WMQVGAFYPY SRNHNITDTR
1560 1570 1580 1590 1600
RQDPVSWNET FASMSTDILN IRYNLLPYFY TQMHDIHANG GTVIRPLLHE
1610 1620 1630 1640 1650
FFSETGTWDI YKQFLWGPAF MVTPVVEPYS ESVTGYVPDG RWLDYHTGQD
1660 1670 1680 1690 1700
IGLRKRLHTL DAPLYKINLH VCGGHILPCQ EPAQNTYFSR QNYMKLIVAA
1710 1720 1730 1740 1750
DDNQTAQGYL FWDDGESIDT YEKGQYLLVQ FNLNKATLTS TILKNGYINT
1760 1770 1780 1790 1800
REMRLGFINV WGKGNTVVQE VNITYKGNKE SVKFSQEANK QILNIDLTAN
1810
NIVLDEPIEI SWT
Length:1,813
Mass (Da):208,305
Last modified:January 23, 2007 - v3
Checksum:i93DAE1B3952C7AD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011401 mRNA. Translation: BAA25370.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011401 mRNA. Translation: BAA25370.1 .

3D structure databases

ProteinModelPortali O62653.
SMRi O62653. Positions 56-917.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG080721.

Enzyme and pathway databases

SABIO-RK O62653.

Family and domain databases

Gene3Di 4.10.110.10. 2 hits.
InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view ]
SMARTi SM00018. PD. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 4 hits.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of sucrase-isomaltase cDNA in the house musk shrew Suncus murinus and identification of a mutation responsible for isolated sucrase deficiency."
    Ito T., Hayashi Y., Ohmori S., Oda S., Seo H.
    J. Biol. Chem. 273:16464-16469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiSUIS_SUNMU
AccessioniPrimary (citable) accession number: O62653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3