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Database: UniProt
Entry: Q6NRF8_XENLA
LinkDB: Q6NRF8_XENLA
Original site: Q6NRF8_XENLA 
ID   Q6NRF8_XENLA            Unreviewed;      1049 AA.
AC   Q6NRF8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=DLC1 Rho GTPase activating protein S homeolog {ECO:0000313|RefSeq:NP_001084765.1};
DE   SubName: Full=MGC83845 protein {ECO:0000313|EMBL:AAH70794.1};
GN   Name=dlc1.S {ECO:0000313|RefSeq:NP_001084765.1,
GN   ECO:0000313|Xenbase:XB-GENE-6251782};
GN   Synonyms=dlc1 {ECO:0000313|RefSeq:NP_001084765.1,
GN   ECO:0000313|Xenbase:XB-GENE-6251782}, MGC83845
GN   {ECO:0000313|EMBL:AAH70794.1}, rhogap7
GN   {ECO:0000313|RefSeq:NP_001084765.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH70794.1};
RN   [1] {ECO:0000313|RefSeq:NP_001084765.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH70794.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocytes {ECO:0000313|EMBL:AAH70794.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001084765.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; BC070794; AAH70794.1; -; mRNA.
DR   RefSeq; NP_001084765.1; NM_001091296.1.
DR   DNASU; 431800; -.
DR   GeneID; 431800; -.
DR   KEGG; xla:431800; -.
DR   AGR; Xenbase:XB-GENE-6251782; -.
DR   CTD; 431800; -.
DR   Xenbase; XB-GENE-6251782; dlc1.S.
DR   OrthoDB; 2883046at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 431800; Expressed in lung and 18 other cell types or tissues.
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; cd08869; START_RhoGAP; 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:SF4; RHO-GAP DOMAIN-CONTAINING PROTEIN; 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   2: Evidence at transcript level;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          603..810
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          854..1024
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          146..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1049 AA;  118854 MW;  7C2ACF3CD2331304 CRC64;
     MLVTQIEAKE ACDWLRAAGF PQYAQLYEDL QFPINIEIVK NDHEFLDRDA MESLYRRLNT
     LNKCGAMKIE INRHRKRSDE SEEDEPCAIS NKWSYQRQSQ RWSRLENLEC PLPDEASSLS
     LPIIPVLNIP KEDAAFSVLI DKNDASSLHS SSSGESDGSP KPYEELETSR SSSRCSSIKF
     VSLDSTFSPS PCEMLNIISE EKLTDKPPNK KGKSLIRKME KLRIRSSTVK RNSYLKGKPT
     ISGPVLLDGI DEDKLRNLNC VNISDLADAH SKAGFSCSSQ TCSSSSPSET SSTVSTPSPV
     IRVRSHGKRG GIYAEDFDPN KLSLWNDISE RNFRNERHLH EQQIFQIPQG HKPGTFPKAL
     TNSILSPMDN TSVNWRTGSF HGCNRNRMRS SSSKDTEMPS SPLSLVDNRL SIYDNVPNIP
     FHFSKLESPG DDDDVFSELD NVMEHVNGLR KLVSEWSEKF SDDGDSDFAN DSVSPCPSSP
     KTIHLEVNEH LDSKSKTDVR DAERCTPRTD SDSPILPYIT VSEIDSTFTD CSRQSPEPVN
     LSMQVDSQSA AHLNRIQRLA LLKLTALMDK YSPSSKQGWN WNVPKFIRKI RAPDYKDKNV
     FGVPFLLNVQ RTGHPIPKSI LQAMEYLRIH FLDQVGLFRK SGVKSRIQSL REMNEQDCKY
     VNYEGQSAFD VADMVKQYFR DLPEPIFTSK LCESFLHIFQ YLPKDQQFRA VQAAILLLPD
     ENRDALKILL YFLRDVVACV KENQMTPTNI AVCLAPSLFH LNTLRRESSS SSRSSQRKYS
     LGKPDQKDLS ENLAATQGLA HMIAECNRLF QLPDYWCDLC PSICEVQPIH AETSVNTSTN
     SLAAHCGTLV SLENSMQNLL RDAKDKYRSW VACSGFEHVE LAFKKVESDE FPIRVWKAST
     EIEAKPHAVL QHILREQHTW DPNLQQSKII ETLDEDTEIY HYITESMPPL PCREYVVLRT
     WRTDPQSGTC ILAATSVECE DVPISGILGH VILCQHLIEN IGTQKCKVTH SCRTDTRGRS
     TEWYNKVCGH MCAAEILRIK DSFNKKKTP
//
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