ID   A0A2D0RHV0_ICTPU        Unreviewed;      1195 AA.
AC   A0A2D0RHV0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Rho guanine nucleotide exchange factor 9 {ECO:0000256|ARBA:ARBA00017486};
DE   AltName: Full=Collybistin {ECO:0000256|ARBA:ARBA00031572};
DE   AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 9 {ECO:0000256|ARBA:ARBA00032237};
GN   Name=arhgef9b {ECO:0000313|RefSeq:XP_017330112.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017330112.1};
RN   [1] {ECO:0000313|RefSeq:XP_017330112.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017330112.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for CDC42.
CC       Promotes formation of GPHN clusters. {ECO:0000256|ARBA:ARBA00043844}.
CC   -!- SUBUNIT: Interacts with GPHN. {ECO:0000256|ARBA:ARBA00011232}.
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DR   RefSeq; XP_017330112.1; XM_017474623.3.
DR   AlphaFoldDB; A0A2D0RHV0; -.
DR   GeneID; 108269078; -.
DR   CTD; 560923; -.
DR   OrthoDB; 24739at2759; -.
DR   Proteomes; UP000221080; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd01224; PH_Collybistin_ASEF; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11975; SH3_ARHGEF9; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) 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; IPR035728; ARHGEF9_SH3.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR47544; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4; 1.
DR   PANTHER; PTHR47544:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 9; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
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; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          676..735
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          804..988
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1019..1126
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          329..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  136303 MW;  651F3ABD20108072 CRC64;
     MENVESRVSN CNVSNGYVNK VFSVSLDMES ETGILQIRKS KDLKESLDLA SFPNPVREKQ
     ELNRASKSAG IWRILNHRRI ASDYERRPHS MILPGEASAS KLSFADKVRG FKKLKSPSVF
     RGKSGKLASA KFQSALKADT NEDSRNSPAL LHSQRNLLRN KGKRHSYAGY TTEFDCSFED
     IDFTTTIEND HQLPKNTVRQ QNCYKAHTCP KKVHSSCNNS CATGHEEDYV KDSPGIPLAG
     RRSKGGDVWN YLKRISFIGK GSSTLLEKSF DSMYTLDKTI DSDYGSVDIE CIKDSIPVPK
     QTGPEVKNSH FRGLFRFFNS MAETARKWRS SSRPFSSPEG ECPNIGPART QQIPEFLPTG
     ANTLRSEDEA YTKPAFTPDI CEVISPAEVL NRSPHVVPKS WKAWPDSSST NGFSEGTESQ
     HTSTHTSLAT IENHQRSDGP EGSSLSEPEL QFDLHEQSES ESSGISEKTK EQTNCKKSGI
     CSDIIPDCPE EIFKVSTGGC CVSEGSPGSF RTSRTMRLSL MKKLWHWPAS DYAIRPSFQC
     PIIKEGVIPS GLEEHWTPVL RPPVPRIPKR LRRPCSVIKG YEPIQLDSIP TQRTLSRPPG
     MSPQDPPFKV VLHRCHSLPL PQNAMSGSMV ASLLLEQSES LRQSATVQNG NGSTGQRKLL
     RPRSGPLQVN MLISGGSIVS AEAVWDHVAM ADRELAFKAG DVIKVLDASN KDWWWGQIDD
     EEGWFPASFV RVEPHPPQPQ TKQVFYINPI ATRRFQITTA KLWVNQDDRS IEAAEGSSEV
     QNGHLDAGSD CLCLGQPLQN RDQMRANVIN EIMSTERHYI KHLKDICEGY LRQCRKRIDM
     FNDDQVKVIF GNIEDIYRFQ MGFVRDLEKQ YNTEEPHLSE IGPCFLEHQD GFWIYSEYCN
     NHLDACMELS KLMKDGRYQH FFEACRLLQQ MIDIAIDGFL LTPVQKICKY PLQLAELLKY
     TAQEHSDYRY VAAALAVMRN VTQQINERKR RLENIDKIAQ WQASVLDWEG NDILDTSSEL
     IYTGELSWIY QPYGRSQHRV FFLFDHQLVL CKKDLIRRDI LYYKGRINMD RYEVKDAIDG
     RDDDFNVSIK NAFKLHNKDT EEIHIFLAKK LEEKIRWLRA FHEERKMVLE DEKIGFEISE
     YQKRQAAMTV RKVTKQKGEA PKRYQYFLEF ADSFIDIILR KRAILYGHGM KMIKL
//