CYH2_CHLAE
ID CYH2_CHLAE Reviewed; 399 AA.
AC Q76MY7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cytohesin-2;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 2;
GN Name=CYTH2; Synonyms=PSCD2;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim H.-S.;
RT "Identification and characterization of cytohesin-2 gene in the African
RT green monkey (Cercopithecus aethiops): sequence, evolution, and
RT phylogeny.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes
CC guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the
CC activation of ARF factors through replacement of GDP with GTP. The cell
CC membrane form, in association with ARL4 proteins, recruits ARF6 to the
CC plasma membrane (By similarity). Involved in neurite growth (By
CC similarity). {ECO:0000250|UniProtKB:P63034,
CC ECO:0000250|UniProtKB:Q99418}.
CC -!- SUBUNIT: Heteromer. Composed of GRASP, CYTH2 and at least one GRM1.
CC Interacts with ARRB1. Interacts with ARL4D; the interaction is direct
CC (By similarity). Directly interacts with CCDC120 through the coiled
CC coil domain; this interaction stabilizes CCDC120, possibly by
CC preventing its ubiquitination, and is required for neurite growth in
CC neuroblastoma cells. Interacts (via N-terminal domain) with INAVA (via
CC N-terminal domain) (By similarity). {ECO:0000250|UniProtKB:P63034,
CC ECO:0000250|UniProtKB:Q99418}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99418};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63034}. Cell projection
CC {ECO:0000250|UniProtKB:P63034}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P63034}. Note=Recruited to the cell membrane
CC through its association with ARL4A, ARL4C and ARL4D. Requires also
CC interaction with phosphoinositides for targeting to plasma membrane. In
CC differentiating neuroblastoma cells, colocalizes with CCDC120 in both
CC neurite shaft and growth cone areas. {ECO:0000250|UniProtKB:P63034,
CC ECO:0000250|UniProtKB:Q99418}.
CC -!- DOMAIN: Binds via its PH domain to the inositol head group of
CC phosphatidylinositol 3,4,5-trisphosphate. The PH domain is necessary
CC and sufficient for plasma membrane relocalization (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain is involved in interaction with CCDC120.
CC {ECO:0000250|UniProtKB:P63034}.
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DR EMBL; AB023376; BAA87927.1; -; mRNA.
DR AlphaFoldDB; Q76MY7; -.
DR BMRB; Q76MY7; -.
DR SMR; Q76MY7; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane.
FT CHAIN 1..399
FT /note="Cytohesin-2"
FT /id="PRO_0000270822"
FT DOMAIN 54..241
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 259..375
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 386..394
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 13..56
FT /evidence="ECO:0000255"
FT BINDING 268..275
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 46489 MW; 436A1C1651C8894C CRC64;
MEDGVYEPPD LTPEERMELE NIRRRKQELL VEIQRLREEL SEAMSEVEGL EANEGSKTLQ
RNRKMAMGRK KFNMDPKKGI QFLVENELLQ NTPEEIARFL YKGEGLNKTA IGDYLGEREE
LNLAVLHAFV DLHEFTDLNL VQALRQFLWS FRLPGEAQKI DRMMEAFAQR YCLCNPGVFQ
STDTCYVLSF AVIMLNTSLH NPNVRDKPGL ERFVAMNRGI NEGGDLPEEL LRNLYDSIRN
EPFKIPEDDG NDLTHTFFNP DREGWLLKLG GRVKTWKRRW FILTDNCLYY FEYTTDKEPR
GIIPLENLSI REVDDPRKPN CFELYIPNNK GQLIKACKTE ADGRVVEGNH MVYRISAPTQ
EEKDEWIKSI QAAVSVDPFY EMLAARKKRI SVKKKQEQP
