Table 2.
>sp|P23415|GLRA1_HUMAN | |||
MYSFNTLRLY LWETIVFFSL AASKEAEAAR LMGRTS GYDARIRPNF 60 | |||
KGPPVNVSCN IFINSFGSIA ETTMDYRVNI FLR LAYNEYPDDS LDLDPSMLDS 120 | |||
IWKPDLFFAN EKLLRISR NFPMDVQTC 180 | |||
IMQLESFGYT MNDLIFEWQE QGAVQVADGL TLPQFILKEE KDLR 240 | |||
QMGY YLIQMYIPSL LIVILSWISF WINMDAAPAR A 300 | |||
SLPKVSYVKA IDIWMAVCLL FVFSALLEYA AVNFVSRQHK ELLRFRRKRR 360 | |||
DGISV KLFIQRA 420 | |||
KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNQ | |||
# | Start–End | Domain | Peptide Sequence and PTM |
aO | 31–44 | Extracellular loop | SAPKPSPSDFLDK |
b | 94–100 | Extracellular loop | QQWNDPR |
c | 133–144 | Extracellular loop | GAHFHEITTDNK |
dO | 151–171 | Extracellular loop | NGNVLYSIRITLTLACPDLK |
dCO | 151–171 | Extracellular loop | NGNVLYSIRITLTLAPDLK |
e | 160–171 | Extracellular loop | ITLTLACPMDLK |
f | 225–234 | Extracellular loop, Cys-Loop | YCTKHYNTGK |
fC | 225–234 | Extracellular loop, Cys-Loop | YTKHYNTGK |
g | 229–241 | Extracellular loop | HYNTGKFTCIEAR |
gC | 229–241 | Extracellular loop | HYNTGKFTIEAR |
hC | 235–246 | Extracellular loop, Cys-Loop | FTIEARFHLER |
i | 281–299 | TM2 | VGLGITTVLTMTTQSSGSR |
jO | 351–369 | Cytoplasmic loop | HHKSPLNLFQEDEAGEGR |
k | 370–385 | Cytoplasmic loop | FNFSAYGMGPACLQAK |
l | 392–407 | Cytoplasmic loop | GANNSNTTNPPPAPSK |
m | 408–414 | Cytoplasmic loop | SPEEMRK |
mO | 408–414 | Cytoplasmic loop | SPEERK |
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.