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RFT1_DICDI
ID   RFT1_DICDI              Reviewed;         540 AA.
AC   Q54IV7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein RFT1 homolog;
GN   Name=rft1; ORFNames=DDB_G0288491;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: May be involved in N-linked oligosaccharide assembly.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RFT1 family. {ECO:0000305}.
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DR   EMBL; AAFI02000112; EAL63194.1; -; Genomic_DNA.
DR   RefSeq; XP_636696.1; XM_631604.1.
DR   AlphaFoldDB; Q54IV7; -.
DR   SMR; Q54IV7; -.
DR   STRING; 44689.DDB0305027; -.
DR   PaxDb; Q54IV7; -.
DR   EnsemblProtists; EAL63194; EAL63194; DDB_G0288491.
DR   GeneID; 8626653; -.
DR   KEGG; ddi:DDB_G0288491; -.
DR   dictyBase; DDB_G0288491; rft1.
DR   eggNOG; KOG2864; Eukaryota.
DR   HOGENOM; CLU_023360_5_0_1; -.
DR   InParanoid; Q54IV7; -.
DR   OMA; WPGKLFG; -.
DR   PhylomeDB; Q54IV7; -.
DR   PRO; PR:Q54IV7; -.
DR   Proteomes; UP000002195; Chromosome 5.
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: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   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..540
FT                   /note="Protein RFT1 homolog"
FT                   /id="PRO_0000328237"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          321..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   540 AA;  61896 MW;  D5EB7F70479D067D CRC64;
     MKQPQTESNV LKNGLVGAFY LIGLQIISRL FTFIINTLVI VGVDDSIFGV SAIQYQLLSS
     IILFLSREAI RRACTRVNIT DKLNNDNNLK SVINLSWLVL PIGIGLSIIF ENFFLYTSTK
     ETLEILNYHY GLRLFTISSI LELLSEPMYI LAQNLLLFKI RTTVEGFALF FKTFSTYYFI
     VILNMGLIGF GYAQILYSLT LVIGYFGYFL INIINNNKNK DNKEFSNCFK SIDQLFPKFS
     TRIDRNLIKL SLLYTWQSIY KLLLQEGEKF VLFFSETNQG QAIFAIVSNL GSLIVRFLFL
     PIEETCFLMF PKLFPTINNN NNNNNNNNNN NNNNNKNQEN NNNNDDFKNG ANVLIVIMKF
     LILVSLVFTC FGPGFSHLLL NLLYNNKFRD TNAGVLLGFY CIYVGFLAIN GVSESFVHSV
     AKEDQLKTVN WVLIIIGFIY LLFTLIFCKL FQNIGIILAN CLNIKLSNMI PNKMVLLSFI
     ISFIITNLSN KYIYNAVSFK STCIHLLIGI ICFIQTCTFI YLKEWVSIKE FKKILSNKNK
 
 
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