SH3 domain-binding protein 1
1_MMKRQ 6_ LHRMR 11_ QLAQT 16_ GSLGR 21_ TPETA 26_ EFLGE 31_ DLLQV 36_ EQRLE 41_ PAKRA 46_ AHNIH 51_ KRLQA 56_ CLQGQ 61_ SGADM 66_ DKRVK 71_ KLPLM 76_ ALSTT 81_ MAESF 86_ KELDP 91_ DSSMG 96_ KALEM 101_ SCAIQ 106_ NQLAR 111_ ILAEF 116_ EMTLE 121_ RDVLQ 126_ PLSRL 131_ SEEEL 136_ PAILK 141_ HKKSL 146_ QKLVS 151_ DWNTL 156_ KSRLS 161_ QATKN 166_ SGSSQ 171_ GLGGS 176_ PGSHS 181_ HTTMA 186_ NKVET 191_ LKEEE 196_ EELKR 201_ KVEQC 206_ RDEYL 211_ ADLYH 216_ FVTKE 221_ DSYAN 226_ YFIRL 231_ LEIQA 236_ DYHRR 241_ SLSSL 246_ DTALA 251_ ELREN 256_ HGQAD 261_ HSPSM 266_ TATHF 271_ PRVYG 276_ VSLAT 281_ HLQEL 286_ GREIA 291_ LPIEA 296_ CVMML 301_ LSEGM 306_ KEEGL 311_ FRLAA 316_ GASVL 321_ KRLKQ 326_ TMASD 331_ PHSLE 336_ EFCSD 341_ PHAVA 346_ GALKS 351_ YLREL 356_ PEPLM 361_ TFDLY 366_ DDWMR 371_ AASLK 376_ EPGAR 381_ LQALQ 386_ EVCSR 391_ LPPEN 396_ LSNLR 401_ YLMKF 406_ LARLA 411_ EEQEV 416_ NKMTP 421_ SNIAI 426_ VLGPN 431_ LLWPP 436_ EKEGD 441_ QAQLD 446_ AASVS 451_ SIQVV 456_ GVVEA 461_ LIQSA 466_ DTLFP 471_ GDINF 476_ NVSGL 481_ FSAVT 486_ LQDTV 491_ SDRLA 496_ SEELP 501_ STAVP 506_ TPATT 511_ PAPAP 516_ APAPA 521_ PAPAL 526_ ASAAT 531_ KERTE 536_ SEVPP 541_ RPASP 546_ KVTRS 551_ PPETA 556_ APVED 561_ MARRT 566_ KRPAP 571_ ARPTM 576_ PPPQV 581_ SGSRS 586_ SPPAP 591_ PLPPG 596_ SGSPG 601_ TPQAL 606_ PRRLV 611_ GSSLR 616_ APTVP 621_ PPLPP 626_ TPPQP 631_ ARRQS 636_ RRSPA 641_ SPSPA 646_ SPGPA 651_ SPSPV 656_ SLSNP 661_ AQVDL 666_ GAATA 671_ EGGAP 676_ EAISG 681_ VPTPP 686_ AIPPQ 691_ PRPRS 696_LASET
1: GTPase activating protein (GAP) which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration (PubMed:21658605). Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions (PubMed:22891260). Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment (PubMed:26465210). It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (PubMed:24841563)