AG10B_RAT
ID AG10B_RAT Reviewed; 474 AA.
AC O88788;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase {ECO:0000250|UniProtKB:P50076};
DE EC=2.4.1.256 {ECO:0000250|UniProtKB:P50076};
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10-A;
DE AltName: Full=Alpha-2-glucosyltransferase ALG10-B;
DE AltName: Full=Asparagine-linked glycosylation protein 10 homolog B;
DE AltName: Full=Potassium channel regulator 1;
GN Name=Alg10b; Synonyms=Kcr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KCNH1, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Cerebellum;
RX PubMed=9722534; DOI=10.1074/jbc.273.36.23080;
RA Hoshi N., Takahashi H., Shahidullah M., Yokoyama S., Higashida H.;
RT "KCR1, a membrane protein that facilitates functional expression of non-
RT inactivating K+ currents associates with rat EAG voltage-dependent K+
RT channels.";
RL J. Biol. Chem. 273:23080-23085(1998).
RN [2]
RP FUNCTION, INTERACTION WITH KCNH2, AND SUBCELLULAR LOCATION.
RX PubMed=14525949; DOI=10.1096/fj.02-1057fje;
RA Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S.,
RA Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R.;
RT "The IKr drug response is modulated by KCR1 in transfected cardiac and
RT noncardiac cell lines.";
RL FASEB J. 17:2263-2265(2003).
CC -!- FUNCTION: Putative alpha-1,2-glucosyltransferase, which adds the third
CC glucose residue to the lipid-linked oligosaccharide precursor for N-
CC linked glycosylation. Transfers glucose from dolichyl phosphate glucose
CC (Dol-P-Glc) onto the lipid-linked oligosaccharide
CC Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity). When coupled to KCNH2 may
CC reduce KCNH2 sensitivity to classic proarrhythmic drug blockade,
CC possibly by mediating glycosylation of KCNH2 (PubMed:9722534,
CC PubMed:14525949). Has a role in maintenance of cochlear outer hair cell
CC function (By similarity). {ECO:0000250|UniProtKB:P50076,
CC ECO:0000250|UniProtKB:Q3UGP8, ECO:0000269|PubMed:14525949,
CC ECO:0000269|PubMed:9722534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC Evidence={ECO:0000250|UniProtKB:P50076};
CC -!- SUBUNIT: Interacts with KCNH1 and KCNH2. {ECO:0000269|PubMed:14525949,
CC ECO:0000269|PubMed:9722534}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14525949};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14525949}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle, uterus,
CC small intestine and liver. Moderately expressed in lung and kidney.
CC Weakly expressed in heart and stomach. {ECO:0000269|PubMed:9722534}.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U78090; AAC34249.1; -; mRNA.
DR RefSeq; NP_620801.1; NM_139101.2.
DR AlphaFoldDB; O88788; -.
DR STRING; 10116.ENSRNOP00000019672; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR PhosphoSitePlus; O88788; -.
DR PaxDb; O88788; -.
DR PRIDE; O88788; -.
DR Ensembl; ENSRNOT00000019672; ENSRNOP00000019672; ENSRNOG00000014511.
DR GeneID; 245960; -.
DR KEGG; rno:245960; -.
DR CTD; 84920; -.
DR RGD; 708500; Alg10b.
DR eggNOG; KOG2642; Eukaryota.
DR GeneTree; ENSGT00390000012906; -.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; O88788; -.
DR OMA; FNCGNLY; -.
DR OrthoDB; 476469at2759; -.
DR PhylomeDB; O88788; -.
DR TreeFam; TF300150; -.
DR PRO; PR:O88788; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000014511; Expressed in duodenum and 18 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
FT alpha-1,2-glucosyltransferase"
FT /id="PRO_0000215449"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 55574 MW; 0901C1DEA9C7B9E9 CRC64;
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GRFSLSQWDP
MITTLPGLYL VSVGVVKPAS WILGWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFRKIQP
RNKASSSIQR ILSTLTLAVF PTLYFFNFLY YTEAGSVFFT LFAYLMCLYG NHRTSALLGF
CGFMFRQTNI IWAAFCAGHI IAQKCSEAWK TELQKKKEER LPPAKGPLSE LRRVLQFLLM
YSMSLKNLSM LFLLTWPYML LLLAFFVFVV VNGGIVVGDR SSHEACLHFP QLFYFFSFTA
FFSFPHLLSP TKVKTFLSLV WKRRVQFSVI TLVSVFLVWK FTYVHKYLLA DNRHYTFYVW
KRVFQRHEIV KYLLVPAYMF AGWAVADSLK SKSIFWNLMF FVCLVASTVP QKLLEFRYFI
LPYIIYRLNM PLPPISRLVC ELGCYAVVNF LTFYIFLNKT FQWSDSHDIQ RFMW
