Cleft lip and palate transmembrane protein 1
1_MAAAQ 6_ EADGA 11_ RSAVV 16_ AAGGG 21_ SSGQV 26_ TSNGS 31_ IGRDP 36_ PAETQ 41_ PQNPP 46_ AQPAP 51_ NAWQV 56_ IKGVL 61_ FRIFI 66_ IWAIS 71_ SWFRR 76_ GPAPQ 81_ DQAGP 86_ GGAPR 91_ VASRN 96_ LFPKD 101_ TLMNL 106_ HVYIS 111_ EHEHF 116_ TDFNA 121_ TSALF 126_ WEQHD 131_ LVYGD 136_ WTSGE 141_ NSDGC 146_ YEHFA 151_ ELDIP 156_ QSVQQ 161_ NGSIY 166_ IHVYF 171_ TKSGF 176_ HPDPR 181_ QKALY 186_ RRLAT 191_ VHMSR 196_ MINKY 201_ KRRRF 206_ QKTKN 211_ LLTGE 216_ TEADP 221_ EMIKR 226_ AEDYG 231_ PVEVI 236_ SHWHP 241_ NITIN 246_ IVDDH 251_ TPWVK 256_ GSVPP 261_ PLDQY 266_ VKFDA 271_ VSGDY 276_ YPIIY 281_ FNDYW 286_ NLQKD 291_ YYPIN 296_ ESLAS 301_ LPLRV 306_ SFCPL 311_ SLWRW 316_ QLYAA 321_ QSTKS 326_ PWNFL 331_ GDELY 336_ EQSDE 341_ EQDSV 346_ KVALL 351_ ETNPY 356_ LLALT 361_ IIVSI 366_ VHSVF 371_ EFLAF 376_ KNDIQ 381_ FWNSR 386_ QSLEG 391_ LSVRS 396_ VFFGV 401_ FQSFV 406_ VLLYI 411_ LDNET 416_ NFVVQ 421_ VSVFI 426_ GVLID 431_ LWKIT 436_ KVMDV 441_ RLDRE 446_ HRVAG 451_ IFPRL 456_ SFKDK 461_ STYIE 466_ SSTKV 471_ YDDMA 476_ FRYLS 481_ WILFP 486_ LLGCY 491_ AVYSL 496_ LYLEH 501_ KGWYS 506_ WVLSM 511_ LYGFL 516_ LTFGF 521_ ITMTP 526_ QLFIN 531_ YKLKS 536_ VAHLP 541_ WRMLT 546_ YKALN 551_ TFIDD 556_ LFAFV 561_ IKMPV 566_ MYRIG 571_ CLRDD 576_ VVFFI 581_ YLYQR 586_ WIYRV 591_ DPTRV 596_ NEFGM 601_ SGEDP 606_ TAAAP 611_ VAEVP 616_ TAAGA 621_ LTPTP 626_ APTTT 631_ TATRE 636_ EASTS 641_ LPTKP 646_ TQGAS 651_ SASEP 656_ QEAPP 661_KPAED
1: Involved in GABAergic but not glutamatergic transmission. Binds and traps GABAA receptors in the endoplasmic reticulum (ER). Modulates postsynaptic GABAergic transmission, and therefore inhibitory neurotransmission, by reducing the plasma membrane expression of these receptors. Altered GABAergic signaling is one among many causes of cleft palate (By similarity). Might function as a lipid scramblase, translocating lipids in membranes from one leaflet to the other one (By similarity). Required for efficient glycosylphosphatidylinositol (GPI) inositol deacylation in the ER, which is a crucial step to switch GPI-anchored proteins (GPI-APs) from protein folding to transport states (PubMed:29255114). May play a role in T-cell development (By similarity)