GenomeNet

Database: UniProt
Entry: F7FZ90_MONDO
LinkDB: F7FZ90_MONDO
Original site: F7FZ90_MONDO 
ID   F7FZ90_MONDO            Unreviewed;      1503 AA.
AC   F7FZ90;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Rho GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00014465};
DE   AltName: Full=Rho-type GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00030675};
DE   AltName: Full=START domain-containing protein 12 {ECO:0000256|ARBA:ARBA00032733};
DE   AltName: Full=StAR-related lipid transfer protein 12 {ECO:0000256|ARBA:ARBA00030542};
GN   Name=DLC1 {ECO:0000313|Ensembl:ENSMODP00000023804.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000023804.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000023804.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000023804.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
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DR   RefSeq; XP_007495695.1; XM_007495633.2.
DR   RefSeq; XP_007495696.1; XM_007495634.2.
DR   STRING; 13616.ENSMODP00000023804; -.
DR   Ensembl; ENSMODT00000024228.4; ENSMODP00000023804.3; ENSMODG00000019070.4.
DR   GeneID; 100022416; -.
DR   KEGG; mdo:100022416; -.
DR   CTD; 10395; -.
DR   eggNOG; KOG2200; Eukaryota.
DR   GeneTree; ENSGT00950000183061; -.
DR   InParanoid; F7FZ90; -.
DR   OMA; AMSHESM; -.
DR   OrthoDB; 2883046at2759; -.
DR   TreeFam; TF314044; -.
DR   Proteomes; UP000002280; Chromosome 5.
DR   Bgee; ENSMODG00000019070; Expressed in cerebellum and 17 other cell types or tissues.
DR   ExpressionAtlas; F7FZ90; baseline.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04375; RhoGAP_DLC1; 1.
DR   CDD; cd09591; SAM_DLC1; 1.
DR   Gene3D; 1.10.287.2070; -; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
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; RHO GTPASE-ACTIVATING PROTEIN 7; 1.
DR   PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 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; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50848; START; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280}.
FT   DOMAIN          1053..1259
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          1289..1471
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          146..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..986
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1503 AA;  165213 MW;  F223542F99A95384 CRC64;
     MSVAVRKRSW EEHVTQRMGF LLHPPDAPTP TCHHGLVADS LHASLEKGGA LAGGHHQRWA
     SLPDCCQALE PASCPEQLLG NVSRELDGND PCDVAEGLLS LVASTETLVH VSDEETDAEA
     NLGAANHWRD GDRESADEWR LNGMGTFAKM PPSPEGDQES PVSLEASETA SEPEQEEFIL
     MEESRKKEDW DPNGDNQELG SSNLSVSRVR EAPKADCSNT LSANEILPEK QLLHSAVIAQ
     QRRKCADTIK DRNERRAGEA LQDGFSASPC TGRTQLRSEN PESCLEEPSC CPYTLDKSSI
     THSHSSAPQN KHLAEAGSRG GVTSEHGTAP MAAGYPYGTQ VALREKKEMR EDGGRRRIDS
     MALLIMKLDQ LDRDIENALS TSPSPASLQE HQPQQKPSLE QEPRDESGEN AGPIHQDQVD
     LPSNPEEAVL VAGPASLPPT ASSATKPKAV PSASEKGKAE IEAKEACDWL RAAGFPQYAQ
     LYEDLLFPID IALVKREHDF LDRDSIEALY RRLNTLNKCA VMKLEISPHR KRSEDSDEDE
     PCAISGKWTF QRDSKRWSRM DEFDAFPPGL GLSARAPGNP ALASTASRES LLTNLSESQE
     LASLRSLGSA SSLPTEPSTP RASSALSVCS SGPQEEAPPP APAESPSPDT KGQGQPAKAK
     PRSLLKRMES LKLRRSHTGR PKAAPAKLGL VISGPVLQEG AEQEKLQHLH CVELSALGAG
     GPFRGPGVRK RSVSNSTLTS SGSSSQSESS SAVSTPSPVT RTRSLSACKK RGGMYLEGFD
     PFDSVLEQNL RNRESCPQDA VFYIPEDHKP GTFPKALSNG RLPAPGGPAA GWRAGSFHGH
     AWEGAKEPPR RNSCSVSSRL SVYDNVPGPG LYPDLEQDDV FPELDDILFH VKGMQRIVNQ
     WSEKFSDEGD SDSALDSVSP CPSSPKQIHL EGEHGRASPS DLDSVGNSVH EAEEPSGGPE
     RRDSGVGASL TRTNRPRQSW QSSQQSALSS AGSQISCQSV AQMNLLQKYS LLKLTALLER
     YTPSNKHGFS WAVPKFMKRL KVPDYKDRSV FGVPLPVNVQ RTGQPLPPSI QQAMGYLHGQ
     CLDQVGLFRK SGVKSRIQAL RQMNEGSAAY VSYEGQSAYD VADMLKQYFR DLPEPLMTHK
     LSETFLQIYQ YVPKDQRLQA IQAAVMLLPD ENREVLQTLL YFLSEVTAAV KENQMTATNL
     AVCLAPSLFH LNTLKRENSS PRVMQRKQSL GKPDQKDLSE NLAATQGLAH MITECHQLFQ
     VPEEMSRCRN SYSEQELRPL SLEALSRLNG QDPSDYRHFL QDSMDSLFKE VKDKFRGWVN
     HPTSEPAELA YKKLSEGPPL RLWKSAIEVL AKPEEVLNRL LKEQHVWDSD LLDAKVIEVL
     DSQTEIYQFV RSSMAPHPAR DHVVLRTWRT NLPKGACVLL LTSVDHSQVP VLGVRVNVLL
     ARYLVEPCGA GRSKLTYMCR SDLRGHIPEW YTKVFGHMCV AEVVKIRDSF CRPSMDSKDG
     KSR
//
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