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Database: UniProt
Entry: A0A2K6CZ59_MACNE
LinkDB: A0A2K6CZ59_MACNE
Original site: A0A2K6CZ59_MACNE 
ID   A0A2K6CZ59_MACNE        Unreviewed;      1086 AA.
AC   A0A2K6CZ59;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:ENSMNEP00000028952.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000028952.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000028952.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6CZ59; -.
DR   Ensembl; ENSMNET00000053321.1; ENSMNEP00000028952.1; ENSMNEG00000037830.1.
DR   GeneTree; ENSGT00950000183061; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000037830; Expressed in heart and 12 other cell types or tissues.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04375; RhoGAP_DLC1; 1.
DR   CDD; cd09591; SAM_DLC1; 1.
DR   CDD; cd08908; START_STARD12-like; 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; SM00454; SAM; 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:UP000233120}.
FT   DOMAIN          636..842
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          872..1057
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          114..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1086 AA;  122051 MW;  97BF3B31C8702E50 CRC64;
     LLKEKPKQIE AKEACDWLRA TGFPQYAQLY EDFLFPIDIS LVKREHDFLD RDAIEALCRR
     LNTLNKCAVM KLEISPHRKR SDDSDEDEPC AISGKWTFQR DSKRWSRLEE FDVFSPKQDP
     VPGSPDDSHP KDGASPGGTL MDRGERQEVS SVRSLSSTGS LASHAPPSED AATPRTNSVI
     SVCSSSNLAG NDDSFGSLPS PKELSSFSFS MKGHEKTAKS KTRSLLKRME SLKLKGSHHS
     KHKAPSKLGL IISGPILQEG VDEEKLKQLN CVEISALNGN GVNVPMVRKR SVSNSTQTSS
     SSSQSETSSA VSTPSPVTRT RSLSACNKRV GMYLEGFDPF NQSTFNNVME QNFKNRESYP
     EDTVFYIPED HKPGTFPKAL TNGSFSPSGN NGSVNWRTGS FHGPGHISLR RENSSDNPKE
     LKRRNSSSSM SSRLSIYDNV PGSILYSSSG DLADLENEDI FPELDDILYH VKGMQRIVNQ
     WSEKFSDEGD SDSALDSVSP CPSSPKQIHL DVDNDRTTPS DLDSTGNSLN EPEEPSDIPE
     RRDSGVGASL TRSNRHRLRW HSFQSSHRPS LNSVSLQINC QSVAQMNLLQ KYSLLKLTAL
     LEKYTPSNKH GFSWAVPKFM KRIKVPDYKD RSVFGVPLTV NVQRTGQPLP QSIQQAMRYL
     RNHCLDQVGL FRKSGVKSRI QALRQMNEGA VDCVNYEGQS AYDVADMLKQ YFRDLPEPLM
     TNKLSETFLQ IYQYVPKDQR LQAIKAAIML LPDENREVLQ TLLYFLSDVT AAVKENQMTP
     TNLAMCLAPS LFHLNTLKRE NSSPRVMQRK QSLGKPDQKD LNENLAATQG LAHMIAECKK
     LFQVPEEMSR CRNSYTEQEL KPLTLEALGH LGNDDSADYQ HFLQDCVDGL FKEVKEKFKG
     WVSYSTSKQA ELSYKKVSEG PPLRLWRSTI EVPAVPEEIL KRLLKEQHLW DVDLLDSKVI
     EILDSQTEIY QYVQNSMAPH PARDYVVLRT WRTNLPKGAC ALLLTSVDHD RAPVVGVRVN
     VLLSRYLIEP CGPGKSKLTY MCRADLRGHM PEWYTKSFGH LCAAEVVKIR DSFSNQNTET
     KDTKSR
//
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