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Entry version 113 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Suncus murinus (Asian house shrew) (Musk shrew)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action. EC:3.2.1.48
  • Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose. EC:3.2.1.10

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei250SubstrateBy similarity1
Binding sitei374SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei491Nucleophile; for isomaltase activityPROSITE-ProRule annotation1
Binding sitei574SubstrateBy similarity1
Active sitei590For isomaltase activityBy similarity1
Binding sitei648SubstrateBy similarity1
Active sitei1380Nucleophile; for sucrase activityPROSITE-ProRule annotation1
Active sitei1383For sucrase activityBy similarity1
Active sitei1486Proton donor; for sucrase activityBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase, Multifunctional enzyme

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O62653

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH31 Glycoside Hydrolase Family 31

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sucrase-isomaltase, intestinal
Cleaved into the following 2 chains:
Sucrase (EC:3.2.1.48)
Isomaltase (EC:3.2.1.10)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SI
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSuncus murinus (Asian house shrew) (Musk shrew)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9378 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaEulipotyphlaSoricidaeCrocidurinaeSuncus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei13 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini33 – 1813LumenalSequence analysisAdd BLAST1781

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000185621 – 1813Sucrase-isomaltase, intestinalAdd BLAST1813
ChainiPRO_00000185631 – 991IsomaltaseBy similarityAdd BLAST991
ChainiPRO_0000018564992 – 1813SucraseBy similarityAdd BLAST822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei7Phosphoserine; by PKABy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi48 ↔ 79PROSITE-ProRule annotation
Disulfide bondi62 ↔ 78PROSITE-ProRule annotation
Disulfide bondi73 ↔ 91PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei377SulfotyrosineSequence analysis1
Glycosylationi388N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi506 ↔ 531PROSITE-ProRule annotation
Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
Glycosylationi669N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi791N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi896N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi911N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1221N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1289N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1294SulfotyrosineSequence analysis1
Glycosylationi1326N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1340N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1368SulfotyrosineSequence analysis1
Modified residuei1371SulfotyrosineSequence analysis1
Glycosylationi1432N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1521N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1545N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1558N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1703N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1772N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O62653

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O62653

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini46 – 95P-type 1PROSITE-ProRule annotationAdd BLAST50
Domaini917 – 962P-type 2PROSITE-ProRule annotationAdd BLAST46

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni95 – 991IsomaltaseAdd BLAST897
Regioni992 – 1813SucraseAdd BLAST822

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi42 – 45Ser/Thr-rich4

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00111 Trefoil, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031727 Gal_mutarotase_N
IPR011013 Gal_mutarotase_sf_dom
IPR000322 Glyco_hydro_31
IPR030458 Glyco_hydro_31_AS
IPR030459 Glyco_hydro_31_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR017957 P_trefoil_CS
IPR000519 P_trefoil_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01055 Glyco_hydro_31, 2 hits
PF16863 NtCtMGAM_N, 2 hits
PF00088 Trefoil, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00018 PD, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 2 hits
SSF74650 SSF74650, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i93DAE1B3952C7AD6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB011401 mRNA Translation: BAA25370.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

SMRiO62653
ModBaseiSearch...

Protein family/group databases

CAZyiGH31 Glycoside Hydrolase Family 31

Proteomic databases

PRIDEiO62653

Enzyme and pathway databases

SABIO-RKiO62653

Family and domain databases

CDDicd00111 Trefoil, 2 hits
Gene3Di2.60.40.1180, 4 hits
InterProiView protein in InterPro
IPR031727 Gal_mutarotase_N
IPR011013 Gal_mutarotase_sf_dom
IPR000322 Glyco_hydro_31
IPR030458 Glyco_hydro_31_AS
IPR030459 Glyco_hydro_31_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR017957 P_trefoil_CS
IPR000519 P_trefoil_dom
PfamiView protein in Pfam
PF01055 Glyco_hydro_31, 2 hits
PF16863 NtCtMGAM_N, 2 hits
PF00088 Trefoil, 2 hits
SMARTiView protein in SMART
SM00018 PD, 2 hits
SUPFAMiSSF51445 SSF51445, 2 hits
SSF74650 SSF74650, 2 hits
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSUIS_SUNMU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O62653
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 113 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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