Skip to main content
. 2020 Oct 7;18:3230–3242. doi: 10.1016/j.csbj.2020.09.035

Table 1.

Interface residues of the homotypic TMD dataset.

# Protein (acca) [ref] TMD sequenceb
ETRA TMDs
1 Ire1 (O75460)f ATIILSTFLLIGWVAFIITY
2 ATP1B1 (P05026)[38]f LLFYVIFYGCLAGIFIGTIQVMLLTI
3 PTPRG (P23470)[39] IIPLIVVSALTFVCLILLIAVLV
4 Tie1 (P35590)[37] LILAVVGSVSATCLTILAALLTLV
5 DDR1 (Q08345)[37] ILIGCLVAIILLLLLIIALML
6 PTPRO (Q16827)[39] VVVISVLAILSTLLIGLLLVTLIIL
7 Armcx6 (Q7L4S7)[35] REVGWMAAGLMIGAGACYCV
8 PTPRU (Q92729)[39] LILGICAGGLAVLILLLGAIIVII
9 Siglec7 (Q9Y286)[35] VLLGAVGGAGATALVFLSFC
10 GpA (P02724) [7] LIIFGVMAGVIGTIL
11 ErbB2 (P04626) [7], [56] LTSIISAVVGILLVVVLGVVFGIL
12 ITGB3 (P05106) [57] VLLSVMGAILLIGLAALLI
13 ITGA2B (P08514) [58]f WVLVGVLGGLLLLTILVLAMW
14 FtsB (P0A6S5) [59] TLLLLAILVWLQYSLWF
15 GP1BB (P13224) [60] GALAAQLALLGLGLLHALLL
16 MPZ (P25189) [61] YGVVLGAVIGGVLGVVLLLLLLFYVV
17 PTPRJ (Q12913) [39] ICGAVFGCIFGALVIVTVGG
18 BNIP3 (Q12983) [62]f LLSHLLAIGLGIYIG
19 QSOX2 (Q6ZRP7) [63] CVVLYVASSLFLMVMY
20 ADCK3 (Q8NI60) [64] LANFGGLAVGLGFGALA
21 NS4A (Q99IB8) [65] TWVLAGGVLAAVAAYCLAT



NMR TMDs
22 CD3ζζ (P20963, 2hac)f LCYLLDGILFIYGVILTALFL
23 EphA1 (P21709, 2k1k) IVAVIFGLLLGAALLLGILVF
24 TYROBP (O43914, 2l34) LAGIVMGDLVLTVLIALAVYFL
25 APP (P05067, 2loh) AIIGLMVGGVVIATVIVITLVML
26 PDGFRB (P09619, 2l6w) VVVISAILALVVLTIISLIILIMLW
27 FGFR3 (P22607, 2lzl) VYAGILSYGVGFFLFLLVVAAVTLC
28 TLR3 (O15455, 2mk9)f FFMINTSILLI̲FIFIVLL
29 DR5 (O14763, 6nhw) SGIIIGVTVAAVVLIVAVFVCKSLL



X-ray TMDs
30 KvAP (P01837, 1orqC4) GKVIGIAVMLTGISALTLLIGTVSNMFQ
31 Bacteriorhodopsin (Q8YSC4, 1xioA4) GFLMSTQIVVITSGLIADL
32 PSII-M (Q8DHA7, 2axtM1) d ATALFVLVPSVFLIILYV
33 Mgst1 (P08011, 2h8aA2) HLNDLENIVPFLGIGLLYSL
34 Wza (Q9X4B7, 2j58A1)fd SQLVPTISGVHDMTETVRYI
35 p2X purinoceptor (Q6NYR1, 3h9vA2) KFNIIPTLLNIGAGLALLGLVNVICDWIV
36 GluCl α (G5EBR3, 3rifA2) IPARVTLGVTTLLTMTAQSAGIN
37 KCNJ12 (F1NHE9, 3spcA2) PLAVFMVVVQSIVGCIIDSFMIGAIMAKM
38 fn ATPase F0 c-ring (Q8RGD7, 3zk1A1)f LGCSAVGAGLAMIAGLGPGIGEG
39 CRCM1 (Q9U6B8, 4hksA1) SWTSALLSGFAMVAMVE
40 CorA (Q9WZ31, 4i0uA1) TIIATIFMPLTFIAGIYGMNF
41 pntAB (Q72GR9, 4o9pC1) WSALYI̲FVL̲T̲AF̲L̲GYE̲L̲
42 AbgT (Q0VR69, 4r0cA7) ITAMEVTMASMAGYLVLMFF̲AAQFVAWF
43 TspO (Q81BL7, 4ryiA2)f PGMTIGMIWAVLFGLIALSVA
44 TMEM16 (C7Z7K1, 4wisA1) LKAWGLLLSILFAEHFYLVVQLAVR
45 Trpv1 (O35433, 5irzD6)e KAVFIILLLAYVILTYILLLNMLIALM
46 CRCB TM1 (Q7VYU0, 5nkqA1)f F̲IAI̲G̲IGAT̲LGAW̲LRW̲VLG
47 CRCB TM3 (Q7VYU1, 5nkqA3) AAVTGFLGGLTTFSTFSAETV
48 PC2 (Q13563, 5t4dA6)e RVLGPIYFTTFVFFMFFILLNMFLAIIN
49 BCNG-1 (O60741, 5u6oA6)e ITMLSMIVGATCYAMFVGHATALI
50 NadC (Q9KNE0, 5uldA9) WKEIQKTADWGILLLFGGGLCL

aAccession number (acc) from the UniProt database. The X-ray identification code (e.g. 1orqC4) consists of the PDB accession (e.g. 1orq), the protein chain (e.g. C), and the TMD number in the protein (e.g. 4).

bHomotypic interface residues in the TMD sequences are underlined.

cBold text indicates new interfaces identified in the current study. In these cases, the reference indicates the ETRA study in which the TMD was first tested, rather than the source of the mutagenesis data.

dTMDs in the X-ray dataset derived from bitopic proteins.

eTMD investigated by high-resolution electron microscopy.

fTMDs included in the blind test data for THOIPA validation.