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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.