ID A0A2I3S289_PANTR Unreviewed; 1080 AA.
AC A0A2I3S289;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSPTRP00000071053.1,
GN ECO:0000313|VGNC:VGNC:13167};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000071053.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000071053.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000071053.1}
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 EMBL; AACZ04024028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04024029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04024030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04024031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04024032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3S289; -.
DR Ensembl; ENSPTRT00000100151.1; ENSPTRP00000071053.1; ENSPTRG00000020009.7.
DR VGNC; VGNC:13167; DLC1.
DR GeneTree; ENSGT00950000183061; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000020009; Expressed in lung and 21 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; 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:UP000002277}.
FT DOMAIN 630..836
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 866..1051
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 110..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 121544 MW; 78BE63B0BB0DA731 CRC64;
LEIEAKEACD WLRATGFPQY AQLYEDFLFP IDISLVKREH DFLDRDAIEA LCRRLNTLNK
CAVMKLEISP HRKRSDDSDE DEPCAISGKW TFQRDSKRWS RLEEFDVFSP KQDLVPGSPD
DSHSKDSPSP GGTLMDLSER QEVSSVRSLS STGSLPSHAP PSEDAATPRT NSVISVCSSS
NLAGNDDSFG SLPSPKELSS FSFSMKGHEK TAKSKTRSLL KRMESLKLKG SHHSKHKAPS
KLGLIISGPI LQEGMDEEKL KQLNCVEISA LNGNRINVPM VRKRSVSNST QTSSSSSQSE
TSSAVSTPSP VTRTRSLSAC NKRVGMYLEG FDPFNQSTFN NVMEQNFKNR ESYPEDTVFY
IPEDHKPGTF PKALTNGSFS PSGNNGSVNW RTGSFHGPGH ISLRRENSSD SPKELQRRNS
SSSMSSRLSI YDNVPGSILY SSSGDLADLE NEDIFPELDD ILYHVKGMQR IVNQWSEKFS
DEGDSDSALD SVSPCPSSPK QIHLDVDNDR TTPSDLDSTG NSLNEPEEPS DIPERRDSGV
GASLTRSNRH RLRWHSFQSS HRPSLNSVSL QINCQSVAQM NLLQKYSLLK LTALLEKYTP
SNKHGFSWAV PKFMKRIKVP DYKDRSVFGV PLTVNVQRTG QPLPQSIQQA MRYLRNHCLD
QVGLFRKSGV KSRIQALRQM NEGAIDCVNY EGQSAYDVAD MLKQYFRDLP EPLMTNKLSE
TFLQIYQYVP KDQRLQAIKA AIMLLPDENR EVLQTLLYFL SDVTAAVKEN QMTPTNLAVC
LAPSLFHLNT LKRENSSPRV MQRKQSLGKP DQKDLNENLA ATQGLAHMIA ECKKLFQVPE
EMSRCRNSYT EQELKPLTLE ALGHLGNDDS ADYQHFLQDC VDGLFKEVKE KFKGWVSYST
SEQAELSYKK VSEGPPLRLW RSIIEVPAVP EEILKRLLKE QHLWDVDLLD SKVIEILDSQ
TEIYQYVQNS MAPHPARDYV VLRTWRTNLP KGACALLLTS VDHDRAPVVG VRVNVLLSRY
LIEPCGPGKS KLTYMCRVDL RGHMPEWYTK SFGHLCAAEV VKIRDSFSNQ NTETKDTKSR
//
