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Database: UniProt
Entry: H0V1Q0_CAVPO
LinkDB: H0V1Q0_CAVPO
Original site: H0V1Q0_CAVPO 
ID   H0V1Q0_CAVPO            Unreviewed;       665 AA.
AC   H0V1Q0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Rho GTPase activating protein 18 {ECO:0000313|Ensembl:ENSCPOP00000003428.3};
GN   Name=ARHGAP18 {ECO:0000313|Ensembl:ENSCPOP00000003428.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003428.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000003428.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003428.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAKN02038160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02038161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013006494.1; XM_013151040.1.
DR   AlphaFoldDB; H0V1Q0; -.
DR   STRING; 10141.ENSCPOP00000003428; -.
DR   Ensembl; ENSCPOT00000003842.3; ENSCPOP00000003428.3; ENSCPOG00000003798.4.
DR   GeneID; 100729447; -.
DR   KEGG; cpoc:100729447; -.
DR   CTD; 93663; -.
DR   VEuPathDB; HostDB:ENSCPOG00000003798; -.
DR   eggNOG; KOG2200; Eukaryota.
DR   GeneTree; ENSGT00940000157142; -.
DR   HOGENOM; CLU_023268_2_1_1; -.
DR   InParanoid; H0V1Q0; -.
DR   OMA; QHNMESQ; -.
DR   OrthoDB; 11483at2759; -.
DR   TreeFam; TF314044; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000003798; Expressed in thyroid gland and 13 other cell types or tissues.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:2000145; P:regulation of cell motility; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR   CDD; cd04391; RhoGAP_ARHGAP18; 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   PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR   PANTHER; PTHR14963:SF6; RHO GTPASE-ACTIVATING PROTEIN 18; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   DOMAIN          326..525
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          14..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  74917 MW;  1FF28836455CE921 CRC64;
     MSWLSSSQGV VLTAYHPSSK DQAVGDSHAK QGEESISSSS CRYGQYTMSQ GSTTKATEKP
     PFDRSSSQDS LDEMSMEDYW TELENIKKSS ENRQAQEVVV VKIPDEGELE EEWLKEAGLS
     NLFGESAEDP QESMVFLSTL TRTQAAAVQK RVETVSQTLR KKNKQYHIPD VRDIFAQQTE
     LKEKAPDGPE LQSVGTNENK YQEKDGQASC LAGDKQLILP VPEDTPTSIT DINLEVSFAE
     QAFNQKQNSK DKIQKTKGSD ASLPSFRLPK DKTGTTKMGD LAPQDMKKVC YLAFIELTAL
     YDVLGLELKQ QKAVKIKTRD SGLFGVSLTM LLEKDQRTVP GTRIPLIFQK LISRIEEGGL
     DTEGLLRIPG AAVRIKNLCQ ELEAKFYEGT FNWENVKQHD AASLLKLFIR ELPQPLLSVE
     YLKAFQAVQN LPTKKHQLQA LNLLIILLPD ANRDTLKALL EFLQRVIDNK EKNKMTVMNV
     AMVMAPNLFM CHALGLKSSE QREFVMAAET ASIMHLLIKY QKLLWTIPKF IVTQVRKQNT
     ESQKKDKKPM KKLLKKMAYD REKYEKQDKS TNDADVPQGV IRVQAPHLSK VSMAIQLTEE
     LKASDVLARF LSQESGVAQT LKKGEVFLYE IGGNIGERCL DDDTYMQDLY QLNPNAEWVI
     KSKPS
//
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