RHG07_CANLF
ID RHG07_CANLF Reviewed; 1091 AA.
AC B9VTT2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Rho GTPase-activating protein 7;
DE AltName: Full=Deleted in liver cancer 1 protein homolog;
DE Short=DLC-1;
DE AltName: Full=Rho-type GTPase-activating protein 7;
DE AltName: Full=START domain-containing protein 12;
DE Short=StARD12;
DE AltName: Full=StAR-related lipid transfer protein 12;
GN Name=DLC1; Synonyms=ARHGAP7, STARD12;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=19912643; DOI=10.1186/1471-2156-10-73;
RA Bryan J.N., Jabbes M., Berent L.M., Arthur G.L., Taylor K.H.,
RA Rissetto K.C., Henry C.J., Rahmatpanah F., Rankin W.V., Villamil J.A.,
RA Lewis M.R., Caldwell C.W.;
RT "Hypermethylation of the DLC1 CpG island does not alter gene expression in
RT canine lymphoma.";
RL BMC Genet. 10:73-73(2009).
CC -!- FUNCTION: Functions as a GTPase-activating protein for the small
CC GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream
CC signaling. This induces morphological changes and detachment through
CC cytoskeletal reorganization, playing a critical role in biological
CC processes such as cell migration and proliferation. Also functions in
CC vivo as an activator of the phospholipase PLCD1. Active DLC1 increases
CC cell migration velocity but reduces directionality (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EF1A1, facilitates EF1A1 distribution to the
CC membrane periphery and ruffles upon growth factor stimulation and
CC suppresses cell migration. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal
CC adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Colocalizes with EF1A1 at actin-rich
CC regions in the cell periphery. {ECO:0000250}.
CC -!- DOMAIN: The SAM domain mediates interaction with EF1A1, and functions
CC as an autoinhibitory regulator of RhoGAP Activity. {ECO:0000250}.
CC -!- DOMAIN: The polybasic cluster is required for activation and mediates
CC binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2))
CC containing membranes. {ECO:0000250}.
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DR EMBL; FJ602870; ACM44925.1; -; mRNA.
DR RefSeq; NP_001138543.1; NM_001145071.1.
DR RefSeq; NP_001300726.1; NM_001313797.1.
DR AlphaFoldDB; B9VTT2; -.
DR SMR; B9VTT2; -.
DR STRING; 9615.ENSCAFP00000010111; -.
DR PaxDb; B9VTT2; -.
DR GeneID; 475607; -.
DR KEGG; cfa:475607; -.
DR CTD; 10395; -.
DR eggNOG; KOG2200; Eukaryota.
DR HOGENOM; CLU_004367_0_0_1; -.
DR InParanoid; B9VTT2; -.
DR OrthoDB; 218349at2759; -.
DR Reactome; R-CFA-8980692; RHOA GTPase cycle.
DR Reactome; R-CFA-9013026; RHOB GTPase cycle.
DR Reactome; R-CFA-9013106; RHOC GTPase cycle.
DR Reactome; R-CFA-9013148; CDC42 GTPase cycle.
DR Reactome; R-CFA-9013149; RAC1 GTPase cycle.
DR Proteomes; UP000002254; Chromosome 16.
DR Bgee; ENSCAFG00000006766; Expressed in mucosa of urinary bladder and 45 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR028854; DLC1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12659:SF2; PTHR12659:SF2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cytoplasm; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..1091
FT /note="Rho GTPase-activating protein 7"
FT /id="PRO_0000382028"
FT DOMAIN 11..78
FT /note="SAM"
FT DOMAIN 641..847
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 877..1084
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 273..447
FT /note="Focal adhesion-targeting (FAT)"
FT /evidence="ECO:0000250"
FT REGION 292..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..636
FT /note="Polybasic cluster (PBR)"
FT /evidence="ECO:0000250"
FT COMPBIAS 386..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QB1"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QB1"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QB1"
SQ SEQUENCE 1091 AA; 122847 MW; 809EE91A8C4CACF8 CRC64;
MCRRKPDIMI LTQIEAKEAC DWLRATGFPQ YAQLYEDLLF PIDISSVKRE HDFLDRDAIE
ALCRRLNTLN KCAVMKLEIS PHRKRSEDSD EDEPCAISGK WTFQRDSKRW SRLEEFDVFS
SKLDPAPGAP AEAPLKTAAS HESMLTELSE RQEVASVLSL SSTGSLPVHA PHAGDAATPR
TNSVISVCSS GHFVGNDDSF CSLPSPKELS SFSFSMKGQE KNAKSKTRSL LKRMESLKLR
GSPHSKHKAP SKLGLIISGP ILQEGMDEEK LKQLNCVEIS ALNGNRINVP AVRKRSVSNS
TQTSSSSSQS ETSSAVSTPS PVTRTRSLSA CNKRVGMYLE GFDPFNQSTF NNVMEQNCKN
RESYPEDTVF YIPEDHKPGT FPKALSNGSF PPSGNNSSVN WRTGSFHGPG HISLRRENSS
DSPKELKRRN SSSSMSSRLS IYDNVPGSIL YSSSGDLADL ENEDIFPELD DILYHVKGMQ
RIVNQWSEKF SDEGDSDSAL DSVSPCPSSP KQIHLDVDND RATPSDLDST GNSLNEPEEP
SDIPERRDSG VGASLTRSNR HRLRWHSFQS SHRPSLNSVS LQINCQSVAQ MNLLQKYSLL
KLTALLEKYT PSNKHGFSWA VPKFMKRIKV PDYKDRNVFG VPLTVNVQRT GQPLPQSIQQ
AMRYLRNHCL DQVGLFRKSG VKSRIQALRQ MNESAIDCVN YEGQSAYDVA DMLKQYFRDL
PEPLMTNKLS ETFLQIYQCV PKDQRLQAMK AAIMLLPDEN REVLQTLLYF LSDVTAAVKE
NQMTPTNLAV CLAPSLFHLN TLKRENSSPR VMQRKQSLGK PDQKDLNENL AATQGLAHMI
AECKKLFQVP EEMSRCRNSY TEQELKPLTL EALGRLRNDE SADYQHFLQD CVDSLFKEVK
EKFKGWVSYS TSEQAELSYK KVSEGPPLRL WRSTIEVPAM PEEILKRLLK EQHLWDVDLL
DSKVIEILDS QTEIYQYVQN SMAPHPARDY VVLRTWRTNL PKGACALLLT SVDHDRAPVV
GVRVNVLLSR YLIEPCGSGK SKLTYMCRAD LRGHMPEWYT KSFGHLCAAE VVKIRDSFSN
QNTETKDTKS R
