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Protein

Glycogen debranching enzyme

Gene

AGL

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.By similarity

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.
Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei527 – 5271By similarity
Active sitei530 – 5301By similarity
Active sitei628 – 6281By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Glycosyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen debranching enzyme
Alternative name(s):
Glycogen debrancher
Including the following 2 domains:
4-alpha-glucanotransferase (EC:2.4.1.25)
Alternative name(s):
Oligo-1,4-1,4-glucantransferase
Amylo-alpha-1,6-glucosidase (EC:3.2.1.33)
Short name:
Amylo-1,6-glucosidase
Alternative name(s):
Dextrin 6-alpha-D-glucosidase
Gene namesi
Name:AGL
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Under glycogenolytic conditions localizes to the nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Glycogen storage disease

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15331533Glycogen debranching enzymePRO_0000232710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ2PQH8.

Interactioni

Subunit structurei

Monomer. Interacts with NHLRC1/malin (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000039212.

Structurei

3D structure databases

ProteinModelPortaliQ2PQH8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1533Amylo-1,6-glucosidase
Regioni1 – ?4-alpha-glucanotransferase

Sequence similaritiesi

Belongs to the glycogen debranching enzyme family.Curated

Phylogenomic databases

eggNOGiCOG3408.
HOGENOMiHOG000212981.
HOVERGENiHBG005824.
InParanoidiQ2PQH8.
KOiK01196.

Family and domain databases

Gene3Di3.20.20.80. 5 hits.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR010401. AGL/Gdb1.
IPR029436. AGL_euk_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR006421. Glycogen_debranch_met.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10569. PTHR10569. 1 hit.
PfamiPF06202. GDE_C. 1 hit.
PF14699. hGDE_N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR01531. glyc_debranch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2PQH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGHSKQIRIL LLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKAVTVYTNY
60 70 80 90 100
PFPGETFNRE KFRSLEWENP TEREDDSDKY CKLNLQQAGS FQYYFLQGNE
110 120 130 140 150
KSGGGYIVVD PILYVGADNH VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA
160 170 180 190 200
KESGYNMIHF TPLQTLGLSR SCYSLANQLE LNPDFSRPNK KYTWSDVGQL
210 220 230 240 250
VEKMKKEWNV LCITDVVYNH TAANSKWIQE HPESAYNLVN SPHLKPAWVL
260 270 280 290 300
DRALWHLSCD VAEGKYKEKG VPALIENDHQ MNCIRKIIWE DIFPKIQLWE
310 320 330 340 350
FFQVDVYKAV EQFRRLLTQE NRKITTKPDP KEHLKIIQDP EYRRLGCTVD
360 370 380 390 400
MNIALATFIP HDKGPAAIDE CCNWFRKRIE ELNSEKHQLV NYHQEQAVNC
410 420 430 440 450
LLGNVFYERM AGHGPKLGPV TRKHPLVTRY FTFPFEEMTV STEESMIHNP
460 470 480 490 500
NKACFLMAHN GWVMGDDPLR NFAEPGSEVY LRRELICWGD SVKLRYGNKP
510 520 530 540 550
EDCPYLWAHM KKYTEITATY FQGVRLDNCH STPLHVAEYM LDAARKLQPN
560 570 580 590 600
LYVVAELFTG SEDLDNIFVT RLGISSLIRE AMSAYNSHEE GRLVYRYGGE
610 620 630 640 650
PVGSFVQPCL RPLMPAIAHA LFMDITHDNE CPIVHRSEYD ALPSTTIVSM
660 670 680 690 700
ACCASGSTKG YDELVPHQIS VVSEERFYTK WNPGASPSNT GEVNFQSGII
710 720 730 740 750
AARCAINKLH QELGAQGFIQ VYVDQVDEDI VAVTRHSPSI HQSVVSVSRT
760 770 780 790 800
AFRNPKTSFY SKEVPQMCIP GKIEEVVLEA RTIERNTKPY QKDKNSINGM
810 820 830 840 850
PNITVEIREH IQLSESKIVK QAGVATKGPN EYIQEIEFEN LSPGSVIIFR
860 870 880 890 900
VSLDPHAQVA VGILRNHLTQ FSPHFKSGSL AVENSDPILK IPFAFIASKL
910 920 930 940 950
TLAELNQVLY RCEAEEQEDG GGCYDIPNWS SLKYAGLQGL MSVLAEIRPK
960 970 980 990 1000
NDLGHPFCDN LRSGDWMIDY VSNRLISRSG TIAEVGKWFQ AMFFYLKQIP
1010 1020 1030 1040 1050
RYLIPCYFDA ILIGAYTTLL DIAWKQMSSF VQNGSTFVKH LSLGSVQMCG
1060 1070 1080 1090 1100
VGKCPSLPLL SPSLMDVPYR LNEITKEKEQ CCVSLAAGLP HFSSGIFRCW
1110 1120 1130 1140 1150
GRDTFIALRG LLLITGRYLE ARNIILAFAG TLRHGLIPNL LGEGTYARYN
1160 1170 1180 1190 1200
CRDAVWWWLQ CIQDYCKMVP NGLDILKCPV SRMYPTDDSV PLSAGTLDQP
1210 1220 1230 1240 1250
LFEVIQEVMQ RHIQGIQFRE RNAGPQIDRN MKDEGFNITA GVDEETGFVY
1260 1270 1280 1290 1300
GGNRLNCGTW MDKMGESDRA RNRGIPATPR DGSAVEIVGL SKSTVRWLLE
1310 1320 1330 1340 1350
LSKKRIFPYH EVRVKRHGKV VTISYDEWNK KIQDNFEKLF HVSEDPXDFN
1360 1370 1380 1390 1400
EKHPNLVHKR GIYKDSYGAS SPWCDYQLRP NFTIAMVVAP ELFTAEKAWK
1410 1420 1430 1440 1450
ALEIAEKKLL GPLGMKTLDP DDMVYCGIYD NALDNDNYNL AKGFNYHQGP
1460 1470 1480 1490 1500
EWLWPVGYFL RAKLYFSKLM GPEANAKTVF LVKNILSRHY VHLERSPWKG
1510 1520 1530
LPELTNENGQ YCPFSCETQA WSIATVLETL YDL
Length:1,533
Mass (Da):174,828
Last modified:January 24, 2006 - v1
Checksum:i8A6E8A11F2252087
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ307574 mRNA. Translation: ABC25005.1.
RefSeqiNP_001041561.1. NM_001048096.1.
UniGeneiCfa.18682.

Genome annotation databases

GeneIDi479931.
KEGGicfa:479931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ307574 mRNA. Translation: ABC25005.1.
RefSeqiNP_001041561.1. NM_001048096.1.
UniGeneiCfa.18682.

3D structure databases

ProteinModelPortaliQ2PQH8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000039212.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiQ2PQH8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi479931.
KEGGicfa:479931.

Organism-specific databases

CTDi178.

Phylogenomic databases

eggNOGiCOG3408.
HOGENOMiHOG000212981.
HOVERGENiHBG005824.
InParanoidiQ2PQH8.
KOiK01196.

Miscellaneous databases

NextBioi20855039.

Family and domain databases

Gene3Di3.20.20.80. 5 hits.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR010401. AGL/Gdb1.
IPR029436. AGL_euk_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR006421. Glycogen_debranch_met.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10569. PTHR10569. 1 hit.
PfamiPF06202. GDE_C. 1 hit.
PF14699. hGDE_N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR01531. glyc_debranch. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Glycogen storage disease type IIIa in curly-coated retrievers."
    Gregory B.L., Shelton G.D., Bali D.S., Chen Y.T., Fyfe J.C.
    J. Vet. Intern. Med. 21:40-46(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGDE_CANFA
AccessioniPrimary (citable) accession number: Q2PQH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 24, 2006
Last modified: June 24, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.