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. 2016 Jun 14;9:45. doi: 10.3389/fnmol.2016.00045

Table 2.

GLRA1 matching peptide sequences identified by mass spectrometry.

>sp|P23415|GLRA1_HUMAN
MYSFNTLRLY LWETIVFFSL AASKEAEAAR SAPKPMSPSD FLDKLMGRTS GYDARIRPNF 60
KGPPVNVSCN IFINSFGSIA ETTMDYRVNI FLRQQWNDPR LAYNEYPDDS LDLDPSMLDS 120
IWKPDLFFAN EKGAHFHEIT TDNKLLRISR NGNVLYSIRI TLTLACPMDL KNFPMDVQTC 180
IMQLESFGYT MNDLIFEWQE QGAVQVADGL TLPQFILKEE KDLRYCTKHY NTGKFTCIEA 240
RFHLERQMGY YLIQMYIPSL LIVILSWISF WINMDAAPAR VGLGITTVLT MTTQSSGSRA 300
SLPKVSYVKA IDIWMAVCLL FVFSALLEYA AVNFVSRQHK ELLRFRRKRR HHKSPMLNLF 360
QEDEAGEGRF NFSAYGMGPA CLQAKDGISV KGANNSNTTN PPPAPSKSPEEMRKLFIQRA 420
KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNQ
# Start–End Domain Peptide Sequence and PTM
aO 31–44 Extracellular loop SAPKPMSPSDFLDK
b 94–100 Extracellular loop QQWNDPR
c 133–144 Extracellular loop GAHFHEITTDNK
dO 151–171 Extracellular loop NGNVLYSIRITLTLACPMDLK
dCO 151–171 Extracellular loop NGNVLYSIRITLTLACPMDLK
e 160–171 Extracellular loop ITLTLACPMDLK
f 225–234 Extracellular loop, Cys-Loop YCTKHYNTGK
fC 225–234 Extracellular loop, Cys-Loop YCTKHYNTGK
g 229–241 Extracellular loop HYNTGKFTCIEAR
gC 229–241 Extracellular loop HYNTGKFTCIEAR
hC 235–246 Extracellular loop, Cys-Loop FTCIEARFHLER
i 281–299 TM2 VGLGITTVLTMTTQSSGSR
jO 351–369 Cytoplasmic loop HHKSPMLNLFQEDEAGEGR
k 370–385 Cytoplasmic loop FNFSAYGMGPACLQAK
l 392–407 Cytoplasmic loop GANNSNTTNPPPAPSK
m 408–414 Cytoplasmic loop SPEEMRK
mO 408–414 Cytoplasmic loop SPEEMRK

Human GLRA1 protein sequence in FASTA format. Matching peptides identified by mass spectrometry experiments are highlighted. Note that the numbering for all amino acid positions cited in the text is relative to a shorter sequence lacking the first 28 amino acids, for consistency with previous homology and modeling studies. Hence I229, S267, and A288 correspond to I257, S295, and A316 in the FASTA sequence; Y410 corresponds to Y446. These four amino acids are in bold text. In the columns, peptides matching GLRA1 sequence identified with the MASCOT search engine following mass spectrometry. Sequences with amino acid residues, locations, and post translational modifications (PTM) of peptides are indicated. Specific information on peptide sequence matches for each gel band is included in Table 1. Superscripts O and C denote Oxidation and Carbamidomethylation, respectively, in the highlighted amino acid.