C42S2_PONAB
ID C42S2_PONAB Reviewed; 84 AA.
AC Q5R4F8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=CDC42 small effector protein 2;
GN Name=CDC42SE2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton by acting downstream of CDC42, inducing actin filament
CC assembly. Alters CDC42-induced cell shape changes. In activated T-
CC cells, may play a role in CDC42-mediated F-actin accumulation at the
CC immunological synapse. May play a role in early contractile events in
CC phagocytosis in macrophages (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts weakly
CC with RAC1 and not at all with RHOA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection,
CC phagocytic cup {ECO:0000250}. Note=Recruited to the activated TCR prior
CC actin polymerization. Localizes at the phagocytic cup of macrophages.
CC {ECO:0000250}.
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC42SE/SPEC family. {ECO:0000305}.
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DR EMBL; CR861291; CAH93358.1; -; mRNA.
DR RefSeq; NP_001126978.1; NM_001133506.1.
DR AlphaFoldDB; Q5R4F8; -.
DR STRING; 9601.ENSPPYP00000017611; -.
DR GeneID; 100173997; -.
DR KEGG; pon:100173997; -.
DR CTD; 56990; -.
DR eggNOG; ENOG502S22R; Eukaryota.
DR InParanoid; Q5R4F8; -.
DR OrthoDB; 1646014at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR039056; SPEC.
DR PANTHER; PTHR13502; PTHR13502; 1.
DR Pfam; PF00786; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Cell shape; Cytoplasm; Cytoskeleton;
KW Lipoprotein; Membrane; Palmitate; Phagocytosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..84
FT /note="CDC42 small effector protein 2"
FT /id="PRO_0000334641"
FT DOMAIN 29..42
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGH7"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGH7"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 9168 MW; BBC85EF915F38339 CRC64;
MSEFWLCFSC CIAEQPQPKR RRRIDRSMIG EPTNFAHTAH VGSGDLFSGM NSVSSIQNQM
QSKGGYGGGM PANVQMQLVD TKAG
