ID   C42S2_RAT               Reviewed;          83 AA.
AC   A1L1K4; B5DFF3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=CDC42 small effector protein 2;
GN   Name=Cdc42se2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway/Mcwi; TISSUE=Embryonic lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC169039; AAI69039.1; -; mRNA.
DR   AlphaFoldDB; A1L1K4; -.
DR   SMR; A1L1K4; -.
DR   STRING; 10116.ENSRNOP00000061001; -.
DR   SwissPalm; A1L1K4; -.
DR   PaxDb; A1L1K4; -.
DR   PeptideAtlas; A1L1K4; -.
DR   Ensembl; ENSRNOT00000063891; ENSRNOP00000061001; ENSRNOG00000042449.
DR   UCSC; RGD:1563924; rat.
DR   RGD; 1563924; Cdc42se2.
DR   eggNOG; ENOG502S22R; Eukaryota.
DR   InParanoid; A1L1K4; -.
DR   PhylomeDB; A1L1K4; -.
DR   TreeFam; TF323815; -.
DR   Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR   PRO; PR:A1L1K4; -.
DR   Proteomes; UP000002494; Chromosome 10.
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:0035591; F:signaling adaptor activity; ISO:RGD.
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..83
FT                   /note="CDC42 small effector protein 2"
FT                   /id="PRO_0000334642"
FT   DOMAIN          28..41
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGH7"
FT   MOD_RES         51
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   83 AA;  9095 MW;  62E606333D90EEEA CRC64;
     MSEFWLCFNC CIAEQPQPRR RRIDRSMIGE PTNFVHTAHV GSGDLFSGMN SVSSIQNQMQ
     SKGGYGGGMP ANVQMQLVDT KAG