FKTN_MACFA
ID FKTN_MACFA Reviewed; 461 AA.
AC Q60HG0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ribitol-5-phosphate transferase FKTN {ECO:0000250|UniProtKB:O75072};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:O75072};
DE AltName: Full=Fukutin {ECO:0000250|UniProtKB:O75072};
DE AltName: Full=Fukuyama-type congenital muscular dystrophy protein {ECO:0000250|UniProtKB:O75072};
DE AltName: Full=Ribitol-5-phosphate transferase {ECO:0000250|UniProtKB:O75072};
GN Name=FKTN {ECO:0000250|UniProtKB:O75072};
GN Synonyms=FCMD {ECO:0000250|UniProtKB:O75072}; ORFNames=QmoA-10950;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Medulla oblongata;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=29416295;
RA Haro C., Uribe M.L., Quereda C., Cruces J., Martin-Nieto J.;
RT "Expression in retinal neurons of fukutin and FKRP, the protein products of
RT two dystroglycanopathy-causative genes.";
RL Mol. Vis. 24:43-58(2018).
CC -!- FUNCTION: Catalyzes the transfer of CDP-ribitol to the distal N-
CC acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-
CC acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-
CC 6-)mannose), a carbohydrate structure present in alpha-dystroglycan
CC (DAG1) (By similarity). This constitutes the first step in the
CC formation of the ribitol 5-phosphate tandem repeat which links the
CC phosphorylated O-mannosyl trisaccharide to the ligand binding moiety
CC composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (By
CC similarity). May interact with and reinforce a large complex
CC encompassing the outside and inside of muscle membranes. Could be
CC involved in brain development (By similarity).
CC {ECO:0000250|UniProtKB:O75072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-
CC Man)]-Thr-[protein] + CDP-L-ribitol = 3-O-[Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + CMP
CC + H(+); Xref=Rhea:RHEA:36551, Rhea:RHEA-COMP:13309, Rhea:RHEA-
CC COMP:17480, ChEBI:CHEBI:15378, ChEBI:CHEBI:57608, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:136710, ChEBI:CHEBI:177331;
CC Evidence={ECO:0000250|UniProtKB:O75072};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36552;
CC Evidence={ECO:0000250|UniProtKB:O75072};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:O75072}.
CC -!- SUBUNIT: Forms a complex composed of FKTN/fukutin, FKRP and
CC RXYLT1/TMEM5 (By similarity). Interacts (via transmembrane domain) with
CC POMGNT1; the interaction is direct and is required for normal POMGNT1
CC location in Golgi membranes (By similarity).
CC {ECO:0000250|UniProtKB:O75072}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O75072}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O75072}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8R507}. Nucleus {ECO:0000250|UniProtKB:Q8R507}.
CC Note=In retinal tissue, does not localize with the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q8R507}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:29416295}.
CC -!- SIMILARITY: Belongs to the LicD transferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB125167; BAD51955.1; -; mRNA.
DR AlphaFoldDB; Q60HG0; -.
DR STRING; 9541.XP_005581187.1; -.
DR eggNOG; ENOG502QUDN; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR InterPro; IPR009644; FKTN-related.
DR InterPro; IPR045587; FKTN_N.
DR InterPro; IPR007074; LicD_fam.
DR PANTHER; PTHR15407; PTHR15407; 1.
DR Pfam; PF19737; FKTN_N; 1.
DR Pfam; PF04991; LicD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..461
FT /note="Ribitol-5-phosphate transferase FKTN"
FT /id="PRO_0000204721"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..461
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 6..27
FT /note="Required and sufficient for interaction with
FT POMGNT1"
FT /evidence="ECO:0000250|UniProtKB:O75072"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 461 AA; 53774 MW; 3D64D652CB4DBCC0 CRC64;
MSRINKNVVL ALLTLTSSAF LLFQLYYYKH YLSTRNGAGL SKSKGSRIGF DSTQWRAVKK
FIMLTSNQNV PVFLIDPLIL ELINKNFEQV KNTSQGSISQ CTFFCVPRDF TAFALQYHLW
KNEEGWFRIA ENMGFQCLKI ESKDPRLDGI DSLSGTEIPL HYICKLAAHA IHLVVFHERS
SNYLWHGHLR LKEHIDRKFV PFRKLQFGRY PGAFDRPELQ QVTVDGLEVL IPKDPMHFVE
EVPHSRFIEC RYKEARAFFQ QYLDDNTVEA MAFRKSAKEL LQLAAKTLNK LGVPFWLSSG
TCLGWYRQCN IIPYSKDVDL GIFIQDYKSD IILAFQDAGL PLKHKFGKVE DSLELSFQGK
DDVKLDIFFF YEETDHMWNG GTQAKTGKKF KYLFPKFTLC WTEFVDMKVH VPCETLEYIE
ANYGKTWKIP VKTWDWKRSP PNVQPNGIWP ISEWDEVIQL Y
