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Database: UniProt
Entry: Q6ZN13_HUMAN
LinkDB: Q6ZN13_HUMAN
Original site: Q6ZN13_HUMAN 
ID   Q6ZN13_HUMAN            Unreviewed;       803 AA.
AC   Q6ZN13;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 119.
DE   SubName: Full=cDNA FLJ16525 fis, clone OCBBF2005433, weakly similar to N-CHIMAERIN {ECO:0000313|EMBL:BAD18562.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD18562.1};
RN   [1] {ECO:0000313|EMBL:BAD18562.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD18562.1};
RA   Oshima A., Takahashi-Fujii A., Tanase T., Imose N., Takeuchi K., Arita M.,
RA   Musashino K., Yuuki H., Hara H., Sugiyama T., Irie R., Otsuki T., Sato H.,
RA   Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y.,
RA   Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., Nakamura Y.,
RA   Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K.,
RA   Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y.,
RA   Nagai K., Isogai T.;
RT   "NEDO human cDNA sequencing project.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK131415; BAD18562.1; -; mRNA.
DR   AlphaFoldDB; Q6ZN13; -.
DR   PeptideAtlas; Q6ZN13; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13233; PH_ARHGAP9-like; 1.
DR   CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1.
DR   CDD; cd12143; SH3_ARHGAP9; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 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; IPR035465; ARHGAP9_SH3.
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:SF103; RHO GTPASE-ACTIVATING PROTEIN 9; 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; SM00456; WW; 1.
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; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          101..167
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          292..326
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          401..514
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          602..802
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          42..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  88374 MW;  2E22A3812A7AF083 CRC64;
     MISAQCNLCL PGSGDSCASG SQLAGTTVAG PAHPESLTLC SGEAERRGKE EWPDSHHYPG
     PTPAPESSDG PHKVTVLATM LSSRWWPSSW GILGLGPRSP PRGSQLCALY AFTYTGADGQ
     QVSLAEGDRF LLLRKTNSDW WLARRLEAPS TSRPIFVPAA YMIEESIPSQ SPTTVIPGQL
     LWTPGPKLFH GSLEELSQAL PSRAQASSEQ PPPLPRKMCR SVSTDNLSPS LLKPFQEGPS
     GRSLSQENLP PEASASTAGP QPLMSEPPVY CNLVDLRRCP RSPPPGPACP LLQRPDAWEQ
     HLDPNSGRCF YINSLTGCKS WKPPRRSRSE TNPGSMEGTQ TLKRNNDVLQ PQAKGFRSDT
     GTPEPLDPQG SLSLSQRTSQ LDPPALQAPR PLPQLLDDPH EVEKSGLLNM TKIAQGGRKL
     RKNWGPSWVV LTGNSLVFYR EPPPTAPSAG WGPAGSRPES SVDLRGAALA HGRHLSSRRN
     VLHIRTIPGH EFLLQSDHET ELRAWHRALR TVIERLDREN PLELRLSGSG PAELSAGEDE
     EEESELVSKP LLRLSSRRSS IRGPEGTEQN RVRNKLKRLI AKRPPLQSLQ ERGLLRDQVF
     GCQLESLCQR EGDTVPSFLR LCIAAVDKRG LDVDGIYRVS GNLAVVQKLR FLVDRERAVT
     SDGRYVFPEQ PGQEGRLDLD STEWDDIHVV TGALKLFLRE LPQPLVPPLL LPHFRAALAL
     SQIQELIGSM PKPNHDTLRY LLEHLCRVIA HSDKNRMTPH NLGIVFGPTL FRPEQETSDP
     AAHALYPGQL VQLMLTNFTS LFP
//
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