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Database: UniProt
Entry: A0A1S3HF49_LINUN
LinkDB: A0A1S3HF49_LINUN
Original site: A0A1S3HF49_LINUN 
ID   A0A1S3HF49_LINUN        Unreviewed;       875 AA.
AC   A0A1S3HF49;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Rho GTPase-activating protein 27 isoform X6 {ECO:0000313|RefSeq:XP_013384121.1};
GN   Name=LOC106154344 {ECO:0000313|RefSeq:XP_013384121.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013384121.1};
RN   [1] {ECO:0000313|RefSeq:XP_013384121.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013384121.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013384121.1; XM_013528667.1.
DR   AlphaFoldDB; A0A1S3HF49; -.
DR   EnsemblMetazoa; XM_013528667.1; XP_013384121.1; LOC106154344.
DR   GeneID; 106154344; -.
DR   OrthoDB; 5395569at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 6.10.140.2130; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          6..73
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          250..284
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          363..396
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          452..563
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          679..874
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          109..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  99571 MW;  C2B221DF82E60CB8 CRC64;
     MATGRGSHTY VLVLYDYDYV ADDGSPVSIK KDEEYVLLKK ANKDWWHVAN LHAKANGEKP
     FYVPAAYVEE IYKNVISVGP GEIRETNEDV QMDATVTVNE DQVTTIKVGY DQEPEPDYPG
     DPPDLHPKTP KPNEDLDNNN MKDFSFQEDS DSVRVKQSPQ IVRQKSAPPE VPQKPQRRYE
     DPTYANLEEV RVAAGMDRPL SQVSQSSDLS QDSPDSDRDY ANYRPGSLSP FSTFAISPPS
     PSLVPNNPKK NLDYGWEEHL DETTGRTYYY NVHTRQTSWN PPRVRARIRS HSDAVFTARQ
     RLQLNTSRDS AFSSDFSPAS PVSPHSPSIS PLRPSTLSSK SASLPRGWKQ EVNDGGEVTF
     VNDGLGEKWL CSQDDQGRTY YYKEDGSESA WELPEMPKLD YERQFSNDSQ PDEREFSADL
     DPTDQHGGSG GARRPSAPVG PGEVSQSPRQ RPPEKRGYLK VTKIMDGNKK LKKNWSQIFI
     VLTGPKLFFY KDTKSAVGQQ GKPDQEFEVG KMDVEWAGKE VSSKKNTIQL SCTVDLELQQ
     YLLQQDDQGV MQEWHSDISK AIKRFRPRPA ESLQHSTSFK KSATLPATLQ SNESYDSVQM
     RPISARGRFQ SSSKSRKSEL VRMASSKYIV TPDQETVDQM NFSDKKSKIR DRLLKFLKKR
     PTMESLQEQG ILQESVFGSH LDRLCERERT TVPIFVKRCI QAIENKGLSI DGIYRVSGNL
     AQVQKLRCAV DQGIMSLLDQ EGEYNFFESE WDIHVLTGSL KLFFRELQEP VFPFAVFDRL
     IAAIKGDPSK RIPMLRDIVK TLPRPNYDTL KVLFEHLNRV IGRSNENRMQ VQNIAIVFGP
     TLMWPEKESH NMAISMMFQS NIVEVMLTEY QNIFR
//
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