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. Author manuscript; available in PMC: 2021 Aug 24.
Published in final edited form as: Dev Cell. 2020 Jul 29;54(4):471–487.e7. doi: 10.1016/j.devcel.2020.07.001

Table 1.

Stretch of residues assigned to the defined regions of each predicted hairpin motif

Predicted hairpins N-terminus H1 top H1 mid Hinge H2 mid H2 top C-terminus
LiveDrop HYE FISWKITSI WVFGFFIRY VILMPLRVL VCFVGVVWL TVCTAAVG YLKDGPFKR
ALG14 hp QS WLSSIFTSL WALLWSCYLV WRDRPQLILCN GPGTCVPFCYAA YLWRLLGRL PS
Spastin hp GYSSSVHKQN LYVVSF PIIFLF NVLRSLI YQLFCI FRYLYG ASTKVIYRPH
LDAH hp MMESPNG WVFTKVA MPLYSVFGYIF FSFFNFLPVWLR LMLIQIYFLIF SIPRQFL GTALKYS
AGPAT3 hp RLCS LVNFVCW AVFSLSCIFY YVITSLLAANW TAFITALSVL GLFYWLM GQAINK
DGAT2 hp RLQ ILVTAFF TSMLLILLSVS FLLVAGSLIYGG LLVRSLMVTY LAYVFVH HKKTQS
FATP hp QRRRRQR FLVIFRFFC ATVAFGLAIACV IYTLHTMGW IFAVLVALVALL LTKPGWRWF YIAGATA
SelT hp DPPGLNYYLS KMIFALKII IIVSVVSAVSPF TFLGLNTPSWW SHMQANKIYACM MIFFLGNML EAQLISSGA

The amino acid sequence of each of the predicted hairpin motifs was divided into five regions. In each case, the predicted α-helices (H1 and H2) were divided into top (H1 top, H2 top) and middle (H1 mid, H2 mid) regions. The residues predicted to connect the α-helices were defined as the hinge region. Short sequence overhangs at the N- and C-termini were included when expressing these motifs in cells. The tryptophan and positively charged residues are underlined.