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Rho GTPase-activating protein 7 (Deleted in liver cancer 1 protein homolog) (DLC-1) (Rho-type GTPase-activating protein 7) (START domain-containing protein 12) (StARD12) (StAR-related lipid transfer protein 12)

 RHG07_MOUSE             Reviewed;        1092 AA.
Q9R0Z9; Q3TRX3; Q3UH75; Q8R541;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
08-NOV-2002, sequence version 2.
22-NOV-2017, entry version 141.
RecName: Full=Rho GTPase-activating protein 7;
AltName: Full=Deleted in liver cancer 1 protein homolog;
Short=DLC-1;
AltName: Full=Rho-type GTPase-activating protein 7;
AltName: Full=START domain-containing protein 12;
Short=StARD12;
AltName: Full=StAR-related lipid transfer protein 12;
Name=Dlc1; Synonyms=Arhgap7, Stard12;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=129/Sv;
PubMed=10702663;
Yuan B.-Z., Keck-Waggoner C.L., Zimonjic D.B., Thorgeirsson S.S.,
Popescu N.C.;
"Assignment and cloning of mouse Arhgap7 to chromosome 8A4-B2, a
conserved syntenic region of human chromosome 8p22-p21.";
Cytogenet. Cell Genet. 87:189-190(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=129/Sv;
PubMed=12034501; DOI=10.1016/S0378-1119(02)00462-6;
Durkin M.E., Yuan B.-Z., Thorgeirsson S.S., Popescu N.C.;
"Gene structure, tissue expression, and linkage mapping of the mouse
DLC-1 gene (Arhgap7).";
Gene 288:119-127(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-1064 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain, and Diencephalon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with EF1A1, facilitates EF1A1 distribution to
the membrane periphery and ruffles upon growth factor stimulation
and suppresses cell migration. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction,
focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}. Note=Colocalizes with EF1A1 at
actin-rich regions in the cell periphery. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9R0Z9-1; Sequence=Displayed;
Name=2;
IsoId=Q9R0Z9-2; Sequence=VSP_026144;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with the highest levels in
heart, liver and lung.
-!- DOMAIN: The SAM domain mediates interaction with EF1A1, and
functions as an autoinhibitory regulator of RhoGAP Activity.
{ECO:0000250}.
-!- DOMAIN: The polybasic cluster is required for activation and
mediates binding to phosphatidylinositol-4,5-bisphosphate
(PI(4,5)P(2)) containing membranes. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAL87620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF178078; AAD51760.1; -; mRNA.
EMBL; AF411442; AAL87620.1; ALT_INIT; Genomic_DNA.
EMBL; AF411435; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411436; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411437; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411438; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411439; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411440; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AF411441; AAL87620.1; JOINED; Genomic_DNA.
EMBL; AK147539; BAE27982.1; -; mRNA.
EMBL; AK162413; BAE36903.1; -; mRNA.
CCDS; CCDS40322.1; -. [Q9R0Z9-1]
CCDS; CCDS57616.1; -. [Q9R0Z9-2]
RefSeq; NP_001181870.1; NM_001194941.1.
RefSeq; NP_056617.2; NM_015802.3.
UniGene; Mm.125155; -.
UniGene; Mm.210875; -.
ProteinModelPortal; Q9R0Z9; -.
SMR; Q9R0Z9; -.
BioGrid; 206100; 1.
IntAct; Q9R0Z9; 1.
STRING; 10090.ENSMUSP00000132812; -.
iPTMnet; Q9R0Z9; -.
PhosphoSitePlus; Q9R0Z9; -.
PaxDb; Q9R0Z9; -.
PRIDE; Q9R0Z9; -.
GeneID; 50768; -.
KEGG; mmu:50768; -.
CTD; 10395; -.
MGI; MGI:1354949; Dlc1.
eggNOG; KOG2200; Eukaryota.
eggNOG; ENOG410XQ10; LUCA.
HOGENOM; HOG000039960; -.
HOVERGEN; HBG055955; -.
InParanoid; Q9R0Z9; -.
KO; K20632; -.
PhylomeDB; Q9R0Z9; -.
ChiTaRS; Dlc1; mouse.
PRO; PR:Q9R0Z9; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DLC1; -.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0032587; C:ruffle membrane; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:InterPro.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
GO; GO:0021575; P:hindbrain morphogenesis; IMP:MGI.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR028854; DLC1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR023393; START-like_dom_sf.
InterPro; IPR002913; START_lipid-bd_dom.
PANTHER; PTHR12659:SF2; PTHR12659:SF2; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF07647; SAM_2; 1.
Pfam; PF01852; START; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00234; START; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50848; START; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Complete proteome; Cytoplasm;
GTPase activation; Membrane; Phosphoprotein; Reference proteome;
Tumor suppressor.
CHAIN 1 1092 Rho GTPase-activating protein 7.
/FTId=PRO_0000056708.
DOMAIN 11 78 SAM.
DOMAIN 642 848 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 878 1085 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
REGION 275 448 Focal adhesion-targeting (FAT).
{ECO:0000250}.
REGION 615 637 Polybasic cluster (PBR). {ECO:0000250}.
COMPBIAS 306 312 Poly-Ser.
COMPBIAS 432 438 Poly-Ser.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000250|UniProtKB:Q63744}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QB1}.
VAR_SEQ 1 13 MCRDEPDTMILTQ -> MGDPEGHVMARPLRGPLRRSFSDH
IRDSTARALDAIWKNTRERRLAE (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_026144.
CONFLICT 42 42 V -> I (in Ref. 3; BAE36903/BAE27982).
{ECO:0000305}.
CONFLICT 120 120 F -> S (in Ref. 3; BAE36903/BAE27982).
{ECO:0000305}.
CONFLICT 192 192 G -> R (in Ref. 1; AAD51760).
{ECO:0000305}.
CONFLICT 421 422 HD -> SH (in Ref. 1; AAD51760).
{ECO:0000305}.
CONFLICT 715 717 KQY -> NRN (in Ref. 1; AAD51760).
{ECO:0000305}.
CONFLICT 730 735 LSETFL -> FSEPSM (in Ref. 1; AAD51760).
{ECO:0000305}.
CONFLICT 917 917 D -> E (in Ref. 3; BAE36903/BAE27982).
{ECO:0000305}.
SEQUENCE 1092 AA; 123367 MW; 9B5DC3103986A751 CRC64;
MCRDEPDTMI LTQIEAKEAC DWLRVTGFPQ YAQLYEDLLF PVDIALVKRE HDFLDRDAIE
ALCRRLNTLN KCAVMKLEIS PHRKRSEDSD EDEPCAISGK WTFQRDSKRW SRLEEFDVFF
PKQDPIPGSP DNSRLQSATS HESMLTDLSE HQEVASVRSL SSTSSSVPTH AAHSGDATTP
RTNSVISVCS SGHFVGNDDS FSSLPSPKEL SSFSFSMKGH HEKNTKSKTR SLLKRMESLK
LKGSHHSKHK APSKLGLIIS APILQEGMDE AKLKQLNCVE ISALNGNHIN VPMVRKRSVS
NSTQTSSSSS QSETSSAVST PSPVTRTRSL STCNKRVGMY LEGFDPFSQS TLNNVTEQNY
KNRESYPEDT VFYIPEDHKP GTFPKALSHG SFCPSGNSSV NWRTGSFHGP GHLSLRRENS
HDSPKELKRR NSSSSLSSRL SIYDNVPGSI LYSSSGELAD LENEDIFPEL DDILYHVKGM
QRIVNQWSEK FSDEGDSDSA LDSVSPCPSS PKQIHLDVDH DRRTPSDLDS TGNSLNEPEE
PTDIPERRDS GVGASLTRCN RHRLRWHSFQ SSHRPSLNSV SLQINCQSVA QMNLLQKYSL
LKLTALLEKY TPSNKHGFSW AVPKFMKRIK VPDYKDRSVF GVPLTVNVQR SGQPLPQSIQ
QAMRYLRNHC LDQVGLFRKS GVKSRIQALR QMNESAEDNV NYEGQSAYDV ADMLKQYFRD
LPEPLMTNKL SETFLQIYQY VPKDQRLQAI KAAIMLLPDE NREVLQTLLY FLSDVTAAVK
ENQMTPTNLA VCLAPSLFHL NTLKRENSSP RVMQRKQSLG KPDQKDLNEN LAATQGLAHM
IAECKKLFQV PEEMSRCRNS YTEQELKPLT LEALGHLNSD QPADYRHFLQ DCVDGLFKEV
KEKFKGWVSY PTSEQADLSY KKVSEGPPLR LWRSTIEVPA APEEILKRLL KEQHLWDVDL
LDSKVIEILD SQTEIYQYVQ NSMAPHPARD YVVLRTWRTN LPRGACALLL TSVDHDRAPV
AGVRVNVLLS RYLIEPCGSG KSKLTYMCRA DLRGHMPEWY SKSFGHLCAA EVVKIRDSFS
NQNTESKDTR SR


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