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Table 1 Sequence comparison of various members of the solute carrier family

From: Lack of Plasma Membrane Targeting of a G172D Mutant Thiamine Transporter Derived from Rogers Syndrome Family

  THTR-1     
  N-glycosylation Family a.a. N -glycosylation  
A. Consensus Site Member Position Sequence Domain
  N63 (63–65) hTHTR-1 59–70 GPDKNLTEREVF Extracellular loop 2 (EL2)
   mTHTR-1 59–70 GPDKNLTERQVY  
   hTHTR-2 41–52 GPDKNLTSAEIT  
   mTHTR-2 42–53 EPSKNLTSPEMT  
   haRFC1 52–63 LLQQNFTIEQVT  
   hRFC1 54–65 GPDKNFTREQVT  
   mRFC1 52–63 LLERKFTKEQVT  
   rRFC-1 52–63 LLERNFTKEQVT  
  N314 (314–316) hTHTR-1 311–322 QVVNNYTQGLWE Transmembrane
   mTHTR-1 311–322 FQVVNYAQGLWE domain 7 (TMD7)
   hTHTR-2 293–304 NQVLNYVQILWD  
   mTHTR-2 287–298 NQILNYVQVLWE  
   haRFC1 284–295 YLIVYYVHVLWS  
   hRFC1 282–293 YLVVYYVHILWN  
   mRFC1 282–293 YLITYYVHVLWR  
   rRFC-1 285–296 YLITYYVHVLWL  
  N413 (413–415) hTHTR-1 410–421 QIAANLSMERYA Transmembrane
   mTHTR-1 411–422 QIAANLSMERYA domain 10 (TMD10)
   hTHTR-2 393–404 QIAVNLNVERYA  
   mTHTR-2 387–398 QIAVNLSLERYA  
   haRFC1 386–397 QIASSLSKELCA  
   hRFC1 386–397 QIASSLSKELCA  
   mRFC1 379–390 QIASSLSKELCA  
   rRFC-1 379–390 QIASSLSKELCA  
   Family a.a.   
B.   Member Position TMD5  
   hTHTR-1 165–186 TLVGFTVGSVLGQILVSVAGWS
   mTHTR-1 165–186 TLVGFTVGSVLGGILVSVVGWS
   hTHTR-2 147–168 TLAAYTAGSVLAQLLVSLANMS
   mTHTR-2 148–169 TLVAYTAGSVLAQLLVSLTNLP
   haRFC1 158–179 VLLGVFTSSVLGQVLWPLEQKS
   hRFC1 159–180 VLLGVFTSSVLGQLLVTVGRVS
   mRFC1 158–179 VLLGVFISSVLGQALVTVGHIS
   rRFC1 158–179 VLLGVFISSVLGQVLVTLGGIS
  1. (A) Sequence comparison of the putative THTR-1 N-glycosylation consensus sites (Asn-X-Ser/Thr) based on scan prosite analysis with various members of the solute carrier family. The conserved consensus motif (NXT) are indicated by light shading. Transmembrane topology is based on Diaz et al. 1999 [4]. The asparagine 63 and 46 of THTR-1 and THTR-2 respectively are indicated in bold. (B) Amino acid alignment of the glycine 172 human THTR-1 vicinity in TMD5 of the various members of the solute carrier family. The conserved glycine 172 and 154 in THTR-1 and THTR-2 respectively are indicated in bold. Light shading indicates the amino acids showing conservation in all members of the solute carrier family.