ID   B7Z6G2_HUMAN            Unreviewed;       721 AA.
AC   B7Z6G2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   13-SEP-2023, entry version 107.
DE   SubName: Full=cDNA FLJ56152, highly similar to Rho guanine nucleotide exchange factor 7 {ECO:0000313|EMBL:BAH13248.1};
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:BAH13248.1};
RN   [1] {ECO:0000313|EMBL:BAH13248.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:BAH13248.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000256|ARBA:ARBA00004510}.
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DR   EMBL; AK300272; BAH13248.1; -; mRNA.
DR   RefSeq; NP_001307782.1; NM_001320853.1.
DR   AlphaFoldDB; B7Z6G2; -.
DR   IntAct; B7Z6G2; 2.
DR   MaxQB; B7Z6G2; -.
DR   PeptideAtlas; B7Z6G2; -.
DR   ProteomicsDB; 6777; -.
DR   DNASU; 8874; -.
DR   GeneID; 8874; -.
DR   CTD; 8874; -.
DR   OrthoDB; 2879064at2759; -.
DR   BioGRID-ORCS; 8874; 230 hits in 1151 CRISPR screens.
DR   GenomeRNAi; 8874; -.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd01225; PH_Cool_Pix; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd12061; SH3_betaPIX; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 1.20.5.390; L1 transposable element, trimerization domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035789; BetaPIX_SH3.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR032409; GEF6/7_CC.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR046376; PH_Cool_Pix.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR46026:SF3; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 7; 1.
DR   PANTHER; PTHR46026; RHO-TYPE GUANINE NUCLEOTIDE EXCHANGE FACTOR, ISOFORM F; 1.
DR   Pfam; PF16523; betaPIX_CC; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF16615; RhoGEF67_u1; 1.
DR   Pfam; PF16614; RhoGEF67_u2; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          81..140
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          168..348
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          370..475
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          477..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          314..369
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          669..710
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        477..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   721 AA;  81404 MW;  4051F1413D21F0E2 CRC64;
     MKTFDANDLY QGQNFNKVLS SLVTLNKVTA DIGLGSDSVC ARPSSHRIKS FDSLGSQSLH
     TRTSKLFQGQ YRSLDMTDNS NNQLVVRAKF NFQQTNEDEL SFSKGDVIHV TRVEEGGWWE
     GTLNGRTGWF PSNYVREVKA SEKPVSPKSG TLKSPPKGFD TTAINKSYYN VVLQNILETE
     NEYSKELQTV LSTYLRPLQT SEKLSSANIS YLMGNLEEIC SFQQMLVQSL EECTKLPEAQ
     QRVGGCFLNL MPQMKTLYLT YCANHPSAVN VLTEHSEELG EFMETKGASS PGILVLTTGL
     SKPFMRLDKY PTLLKELERH MEDYHTDRQD IQKSMAAFKN LSAQCQEVRK RKELELQILT
     EAIRNWEGDD IKTLGNVTYM SQVLIQCAGS EEKNERYLLL FPNVLLMLSA SPRMSGFIYQ
     GKLPTTGMTI TKLEDSENHR NAFEISGSMI ERILVSCNNQ QDLQEWVEHL QKQTKVTSVG
     NPTIKPHSVP SHTLPSHPVT PSSKHADSKP APLTPAYHTL PHPSHHGTPH TTINWGPLEP
     PKTPKPWSLS CLRPAPPLRP SAALCYKEDL SKSPKTMKKL LPKRKPERKP SDEEFASRKS
     TAALEEDAQI LKVIEAYCTS AKTRQTLNSS SRKESAPQVL LPEEEKIIVE ETKSNGQTVI
     EEKSLVDTVY ALKDEVQELR QDNKKMKKSL EEEQRARKDL EKLVRKVLKN MNDPAWDETN
     L
//