LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)
1_MESSP 6_ FNRRQ 11_ WTSLS 16_ LRVTA 21_ KELSL 26_ VNKNK 31_ SSAIV 36_ EIFSK 41_ YQKAA 46_ EETNM 51_ EKKRS 56_ NTENL 61_ SQHFR 66_ KGTLT 71_ VLKKK 76_ WENPG 81_ LGAES 86_ HTDSL 91_ RNSST 96_ EIRHR 101_ ADHPP 106_ AEVTS 111_ HAASG 116_ AKADQ 121_ EEQIH 126_ PRSRL 131_ RSPPE 136_ ALVQG 141_ RYPHI 146_ KDGED 151_ LKDHS 156_ TESKK 161_ MENCL 166_ GESRH 171_ EVEKS 176_ EISEN 181_ TDASG 186_ KIEKY 191_ NVPLN 196_ RLKMM 201_ FEKGE 206_ PTQTK 211_ ILRAQ 216_ SRSAS 221_ GRKIS 226_ ENSYS 231_ LDDLE 236_ IGPGQ 241_ LSSST 246_ FDSEK 251_ NESRR 256_ NLELP 261_ RLSET 266_ SIKDR 271_ MAKYQ 276_ AAVSK 281_ QSSST 286_ NYTNE 291_ LKASG 296_ GEIKI 301_ HKMEQ 306_ KENVP 311_ PGPEV 316_ CITHQ 321_ EGEKI 326_ SANEN 331_ SLAVR 336_ STPAE 341_ DDSRD 346_ SQVKS 351_ EVQQP 356_ VHPKP 361_ LSPDS 366_ RASSL 371_ SESSP 376_ PKAMK 381_ KFQAP 386_ ARETC 391_ VECQK 396_ TVYPM 401_ ERLLA 406_ NQQVF 411_ HISCF 416_ RCSYC 421_ NNKLS 426_ LGTYA 431_ SLHGR 436_ IYCKP 441_ HFNQL 446_ FKSKG 451_ NYDEG 456_ FGHRP 461_ HKDLW 466_ ASKNE 471_ NEEIL 476_ ERPAQ 481_ LANAR 486_ ETPHS 491_ PGVED 496_ APIAK 501_ VGVLA 506_ ASMEA 511_ KASSQ 516_ QEKED 521_ KPAET 526_ KKLRI 531_ AWPPP 536_ TELGS 541_ SGSAL 546_ EEGIK 551_ MSKPK 556_ WPPED 561_ EISKP 566_ EVPED 571_ VDLDL 576_ KKLRR 581_ SSSLK 586_ ERSRP 591_ FTVAA 596_ SFQST 601_ SVKSP 606_ KTVSP 611_ PIRKG 616_ WSMSE 621_ QSEES 626_ VGGRV 631_ AERKQ 636_ VENAK 641_ ASKKN 646_ GNVGK 651_ TTWQN 656_ KESKG 661_ ETGKR 666_ SKEGH 671_ SLEME 676_ NENLV 681_ ENGAD 686_ SDEDD 691_ NSFLK 696_ QQSPQ 701_ EPKSL 706_ NWSSF 711_ VDNTF 716_ AEEFT 721_ TQNQK 726_ SQDVE 731_ LWEGE 736_ VVKEL 741_ SVEEQ 746_ IKRNR 751_YYDED
1: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity)