RFT1_HUMAN
ID RFT1_HUMAN Reviewed; 541 AA.
AC Q96AA3; Q96J03;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein RFT1 homolog;
GN Name=RFT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=12200473; DOI=10.1093/oxfordjournals.molbev.a004208;
RA Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.;
RT "Common origin and evolution of glycosyltransferases using Dol-P-
RT monosaccharides as donor substrate.";
RL Mol. Biol. Evol. 19:1451-1463(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND VARIANT CDG1N CYS-67.
RX PubMed=18313027; DOI=10.1016/j.ajhg.2007.12.021;
RA Haeuptle M.A., Pujol F.M., Neupert C., Winchester B., Kastaniotis A.J.,
RA Aebi M., Hennet T.;
RT "Human RFT1 deficiency leads to a disorder of N-linked glycosylation.";
RL Am. J. Hum. Genet. 82:600-606(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [6]
RP VARIANTS CDG1N CYS-67; GLU-152 AND LYS-298.
RX PubMed=19701946; DOI=10.1002/humu.21085;
RA Vleugels W., Haeuptle M.A., Ng B.G., Michalski J.-C., Battini R.,
RA Dionisi-Vici C., Ludman M.D., Jaeken J., Foulquier F., Freeze H.H.,
RA Matthijs G., Hennet T.;
RT "RFT1 deficiency in three novel CDG patients.";
RL Hum. Mutat. 30:1428-1434(2009).
CC -!- FUNCTION: May be involved in N-linked oligosaccharide assembly. May
CC participate in the translocation of oligosaccharide from the
CC cytoplasmic side to the lumenal side of the endoplasmic reticulum
CC membrane. {ECO:0000269|PubMed:18313027}.
CC -!- INTERACTION:
CC Q96AA3; Q13520: AQP6; NbExp=3; IntAct=EBI-6269616, EBI-13059134;
CC Q96AA3; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-6269616, EBI-19947314;
CC Q96AA3; P34972: CNR2; NbExp=3; IntAct=EBI-6269616, EBI-2835940;
CC Q96AA3; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6269616, EBI-6942903;
CC Q96AA3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-6269616, EBI-781551;
CC Q96AA3; P15941-11: MUC1; NbExp=3; IntAct=EBI-6269616, EBI-17263240;
CC Q96AA3; P50876: RNF144A; NbExp=3; IntAct=EBI-6269616, EBI-2340657;
CC Q96AA3; Q9Y320: TMX2; NbExp=3; IntAct=EBI-6269616, EBI-6447886;
CC Q96AA3; O95859: TSPAN12; NbExp=3; IntAct=EBI-6269616, EBI-2466403;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISEASE: Congenital disorder of glycosylation 1N (CDG1N) [MIM:612015]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:18313027,
CC ECO:0000269|PubMed:19701946}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RFT1 family. {ECO:0000305}.
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DR EMBL; AJ318099; CAC69544.1; -; mRNA.
DR EMBL; CH471055; EAW65277.1; -; Genomic_DNA.
DR EMBL; BC006846; AAH06846.1; -; mRNA.
DR EMBL; BC043595; AAH43595.1; -; mRNA.
DR CCDS; CCDS2869.1; -.
DR RefSeq; NP_443091.1; NM_052859.3.
DR AlphaFoldDB; Q96AA3; -.
DR SMR; Q96AA3; -.
DR BioGRID; 124888; 99.
DR IntAct; Q96AA3; 27.
DR MINT; Q96AA3; -.
DR STRING; 9606.ENSP00000296292; -.
DR TCDB; 2.A.66.3.2; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q96AA3; -.
DR PhosphoSitePlus; Q96AA3; -.
DR SwissPalm; Q96AA3; -.
DR BioMuta; RFT1; -.
DR DMDM; 74731102; -.
DR EPD; Q96AA3; -.
DR jPOST; Q96AA3; -.
DR MassIVE; Q96AA3; -.
DR MaxQB; Q96AA3; -.
DR PaxDb; Q96AA3; -.
DR PeptideAtlas; Q96AA3; -.
DR PRIDE; Q96AA3; -.
DR ProteomicsDB; 75941; -.
DR Antibodypedia; 31369; 90 antibodies from 21 providers.
DR DNASU; 91869; -.
DR Ensembl; ENST00000296292.8; ENSP00000296292.3; ENSG00000163933.10.
DR GeneID; 91869; -.
DR KEGG; hsa:91869; -.
DR MANE-Select; ENST00000296292.8; ENSP00000296292.3; NM_052859.4; NP_443091.1.
DR UCSC; uc003dgj.4; human.
DR CTD; 91869; -.
DR DisGeNET; 91869; -.
DR GeneCards; RFT1; -.
DR GeneReviews; RFT1; -.
DR HGNC; HGNC:30220; RFT1.
DR HPA; ENSG00000163933; Low tissue specificity.
DR MalaCards; RFT1; -.
DR MIM; 611908; gene.
DR MIM; 612015; phenotype.
DR neXtProt; NX_Q96AA3; -.
DR OpenTargets; ENSG00000163933; -.
DR Orphanet; 244310; RFT1-CDG.
DR PharmGKB; PA134960002; -.
DR VEuPathDB; HostDB:ENSG00000163933; -.
DR eggNOG; KOG2864; Eukaryota.
DR GeneTree; ENSGT00390000011390; -.
DR HOGENOM; CLU_023360_5_0_1; -.
DR InParanoid; Q96AA3; -.
DR OMA; WPGKLFG; -.
DR OrthoDB; 582756at2759; -.
DR PhylomeDB; Q96AA3; -.
DR TreeFam; TF313129; -.
DR PathwayCommons; Q96AA3; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR Reactome; R-HSA-4570571; Defective RFT1 causes CDG-1n.
DR SignaLink; Q96AA3; -.
DR BioGRID-ORCS; 91869; 600 hits in 1076 CRISPR screens.
DR ChiTaRS; RFT1; human.
DR GeneWiki; RFT1; -.
DR GenomeRNAi; 91869; -.
DR Pharos; Q96AA3; Tbio.
DR PRO; PR:Q96AA3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96AA3; protein.
DR Bgee; ENSG00000163933; Expressed in body of pancreas and 137 other tissues.
DR ExpressionAtlas; Q96AA3; baseline and differential.
DR Genevisible; Q96AA3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034202; F:glycolipid floppase activity; TAS:Reactome.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0034203; P:glycolipid translocation; IBA:GO_Central.
DR InterPro; IPR007594; RFT1.
DR PANTHER; PTHR13117; PTHR13117; 1.
DR Pfam; PF04506; Rft-1; 1.
PE 1: Evidence at protein level;
KW Congenital disorder of glycosylation; Disease variant; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..541
FT /note="Protein RFT1 homolog"
FT /id="PRO_0000311286"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 67
FT /note="R -> C (in CDG1N; dbSNP:rs118203913)"
FT /evidence="ECO:0000269|PubMed:18313027,
FT ECO:0000269|PubMed:19701946"
FT /id="VAR_044334"
FT VARIANT 152
FT /note="K -> E (in CDG1N; dbSNP:rs763862849)"
FT /evidence="ECO:0000269|PubMed:19701946"
FT /id="VAR_062572"
FT VARIANT 185
FT /note="A -> T (in dbSNP:rs35221142)"
FT /id="VAR_037215"
FT VARIANT 298
FT /note="E -> K (in CDG1N; dbSNP:rs796053521)"
FT /evidence="ECO:0000269|PubMed:19701946"
FT /id="VAR_062573"
SQ SEQUENCE 541 AA; 60335 MW; 2988BA1A2EB769E0 CRC64;
MGSQEVLGHA ARLASSGLLL QVLFRLITFV LNAFILRFLS KEIVGVVNVR LTLLYSTTLF
LAREAFRRAC LSGGTQRDWS QTLNLLWLTV PLGVFWSLFL GWIWLQLLEV PDPNVVPHYA
TGVVLFGLSA VVELLGEPFW VLAQAHMFVK LKVIAESLSV ILKSVLTAFL VLWLPHWGLY
IFSLAQLFYT TVLVLCYVIY FTKLLGSPES TKLQTLPVSR ITDLLPNITR NGAFINWKEA
KLTWSFFKQS FLKQILTEGE RYVMTFLNVL NFGDQGVYDI VNNLGSLVAR LIFQPIEESF
YIFFAKVLER GKDATLQKQE DVAVAAAVLE SLLKLALLAG LTITVFGFAY SQLALDIYGG
TMLSSGSGPV LLRSYCLYVL LLAINGVTEC FTFAAMSKEE VDRYNFVMLA LSSSFLVLSY
LLTRWCGSVG FILANCFNMG IRITQSLCFI HRYYRRSPHR PLAGLHLSPV LLGTFALSGG
VTAVSEVFLC CEQGWPARLA HIAVGAFCLG ATLGTAFLTE TKLIHFLRTQ LGVPRRTDKM
T
