Rho GTPase-activating protein 7 (Deleted in liver cancer 1 protein) (DLC-1) (HP protein) (Rho-type GTPase-activating protein 7) (START domain-containing protein 12) (StARD12) (StAR-related lipid transfer protein 12)
1_MSVAI 6_ RKRSW 11_ EEHVT 16_ HWMGQ 21_ PFNSD 26_ DRNTA 31_ CHHGL 36_ VADSL 41_ QASME 46_ KDATL 51_ NVDRK 56_ EKCVS 61_ LPDCC 66_ HGSEL 71_ RDFPG 76_ RPMGH 81_ LSKDV 86_ DENDS 91_ HEGED 96_ QFLSL 101_ EASTE 106_ TLVHV 111_ SDEDN 116_ NADLC 121_ LTDDK 126_ QVLNT 131_ QGQKT 136_ SGQHM 141_ IQGAG 146_ SLEKA 151_ LPIIQ 156_ SNQVS 161_ SNSWG 166_ IAGET 171_ ELALV 176_ KESGE 181_ RKVTD 186_ SISKS 191_ LELCN 196_ EISLS 201_ EIKDA 206_ PKVNA 211_ VDTLN 216_ VKDIA 221_ PEKQL 226_ LNSAV 231_ IAQQR 236_ RKPDP 241_ PKDEN 246_ ERSTC 251_ NVVQN 256_ EFLDT 261_ PCTNR 266_ GLPLL 271_ KTDFG 276_ SCLLQ 281_ PPSCP 286_ NGMSA 291_ ENGLE 296_ KSGFS 301_ QHQNK 306_ SPPKV 311_ KAEDG 316_ MQCLQ 321_ LKETL 326_ ATQEP 331_ TDNQV 336_ RLRKR 341_ KEIRE 346_ DRDRA 351_ RLDSM 356_ VLLIM 361_ KLDQL 366_ DQDIE 371_ NALST 376_ SSSPS 381_ GTPTN 386_ LRRHV 391_ PDLES 396_ GSESG 401_ ADTIS 406_ VNQTR 411_ VNLSS 416_ DTEST 421_ DLPSS 426_ TPVAN 431_ SGTKP 436_ KTTAI 441_ QGISE 446_ KEKAE 451_ IEAKE 456_ ACDWL 461_ RATGF 466_ PQYAQ 471_ LYEDF 476_ LFPID 481_ ISLVK 486_ REHDF 491_ LDRDA 496_ IEALC 501_ RRLNT 506_ LNKCA 511_ VMKLE 516_ ISPHR 521_ KRSDD 526_ SDEDE 531_ PCAIS 536_ GKWTF 541_ QRDSK 546_ RWSRL 551_ EEFDV 556_ FSPKQ 561_ DLVPG 566_ SPDDS 571_ HPKDG 576_ PSPGG 581_ TLMDL 586_ SERQE 591_ VSSVR 596_ SLSST 601_ GSLPS 606_ HAPPS 611_ EDAAT 616_ PRTNS 621_ VISVC 626_ SSSNL 631_ AGNDD 636_ SFGSL 641_ PSPKE 646_ LSSFS 651_ FSMKG 656_ HEKTA 661_ KSKTR 666_ SLLKR 671_ MESLK 676_ LKSSH 681_ HSKHK 686_ APSKL 691_ GLIIS 696_ GPILQ 701_ EGMDE 706_ EKLKQ 711_ LNCVE 716_ ISALN 721_ GNRIN 726_ VPMVR 731_ KRSVS 736_ NSTQT 741_ SSSSS 746_ QSETS 751_ SAVST 756_ PSPVT 761_ RTRSL 766_ SACNK 771_ RVGMY 776_ LEGFD 781_ PFNQS 786_ TFNNV 791_ VEQNF 796_ KNRES 801_ YPEDT 806_ VFYIP 811_ EDHKP 816_ GTFPK 821_ ALTNG 826_ SFSPS 831_ GNNGS 836_ VNWRT 841_ GSFHG 846_ PGHIS 851_ LRREN 856_ SSDSP 861_ KELKR 866_ RNSSS 871_ SMSSR 876_ LSIYD 881_ NVPGS 886_ ILYSS 891_ SGDLA 896_ DLENE 901_ DIFPE 906_ LDDIL 911_ YHVKG 916_ MQRIV 921_ NQWSE 926_ KFSDE 931_ GDSDS 936_ ALDSV 941_ SPCPS 946_ SPKQI 951_ HLDVD 956_ NDRTT 961_ PSDLD 966_ STGNS 971_ LNEPE 976_ EPSEI 981_ PERRD 986_ SGVGA 991_ SLTRS 996_ NRHRL 1001_ RWHSF 1006_ QSSHR 1011_ PSLNS 1016_ VSLQI 1021_ NCQSV 1026_ AQMNL 1031_ LQKYS 1036_ LLKLT 1041_ ALLEK 1046_ YTPSN 1051_ KHGFS 1056_ WAVPK 1061_ FMKRI 1066_ KVPDY 1071_ KDRSV 1076_ FGVPL 1081_ TVNVQ 1086_ RTGQP 1091_ LPQSI 1096_ QQAMR 1101_ YLRNH 1106_ CLDQV 1111_ GLFRK 1116_ SGVKS 1121_ RIQAL 1126_ RQMNE 1131_ GAIDC 1136_ VNYEG 1141_ QSAYD 1146_ VADML 1151_ KQYFR 1156_ DLPEP 1161_ LMTNK 1166_ LSETF 1171_ LQIYQ 1176_ YVPKD 1181_ QRLQA 1186_ IKAAI 1191_ MLLPD 1196_ ENREV 1201_ LQTLL 1206_ YFLSD 1211_ VTAAV 1216_ KENQM 1221_ TPTNL 1226_ AVCLA 1231_ PSLFH 1236_ LNTLK 1241_ RENSS 1246_ PRVMQ 1251_ RKQSL 1256_ GKPDQ 1261_ KDLNE 1266_ NLAAT 1271_ QGLAH 1276_ MIAEC 1281_ KKLFQ 1286_ VPEEM 1291_ SRCRN 1296_ SYTEQ 1301_ ELKPL 1306_ TLEAL 1311_ GHLGN 1316_ DDSAD 1321_ YQHFL 1326_ QDCVD 1331_ GLFKE 1336_ VKEKF 1341_ KGWVS 1346_ YSTSE 1351_ QAELS 1356_ YKKVS 1361_ EGPPL 1366_ RLWRS 1371_ VIEVP 1376_ AVPEE 1381_ ILKRL 1386_ LKEQH 1391_ LWDVD 1396_ LLDSK 1401_ VIEIL 1406_ DSQTE 1411_ IYQYV 1416_ QNSMA 1421_ PHPAR 1426_ DYVVL 1431_ RTWRT 1436_ NLPKG 1441_ ACALL 1446_ LTSVD 1451_ HDRAP 1456_ VVGVR 1461_ VNVLL 1466_ SRYLI 1471_ EPCGP 1476_ GKSKL 1481_ TYMCR 1486_ VDLRG 1491_ HMPEW 1496_ YTKSF 1501_ GHLCA 1506_ AEVVK 1511_ IRDSF 1516_ SNQNT 1521_ETKDT
1: Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality. Required for growth factor-induced epithelial cell migration; in resting cells, interacts with TNS3 while PTEN interacts with the p85 regulatory subunit of the PI3K kinase complex but growth factor stimulation induces phosphorylation of TNS3 and PTEN, causing them to change their binding preference so that PTEN interacts with DLC1 and TNS3 interacts with p85 (PubMed:26166433). The PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA while the TNS3-p85 complex translocates to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433)