ID   C42S2_BOVIN             Reviewed;          84 AA.
AC   A6QLJ4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=CDC42 small effector protein 2;
GN   Name=CDC42SE2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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; BC147986; AAI47987.1; -; mRNA.
DR   RefSeq; NP_001096007.1; NM_001102537.1.
DR   RefSeq; XP_005209117.1; XM_005209060.3.
DR   RefSeq; XP_005209119.1; XM_005209062.3.
DR   RefSeq; XP_010805364.1; XM_010807062.1.
DR   AlphaFoldDB; A6QLJ4; -.
DR   STRING; 9913.ENSBTAP00000047577; -.
DR   PaxDb; A6QLJ4; -.
DR   Ensembl; ENSBTAT00000052263; ENSBTAP00000047577; ENSBTAG00000005961.
DR   GeneID; 789618; -.
DR   KEGG; bta:789618; -.
DR   CTD; 56990; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005961; -.
DR   VGNC; VGNC:27078; CDC42SE2.
DR   eggNOG; ENOG502S22R; Eukaryota.
DR   GeneTree; ENSGT00940000158245; -.
DR   HOGENOM; CLU_173417_1_0_1; -.
DR   InParanoid; A6QLJ4; -.
DR   OMA; IGVPTNF; -.
DR   TreeFam; TF323815; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000005961; Expressed in occipital lobe and 105 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
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   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_0000334638"
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;  9197 MW;  98C5E82176CF8C0A CRC64;
     MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
     QSKGGYGGGM AANVQMQLVD TKAG