C42S2_MOUSE
ID C42S2_MOUSE Reviewed; 84 AA.
AC Q8BGH7; Q3UKN9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CDC42 small effector protein 2;
GN Name=Cdc42se2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Cerebellum, Egg, Lung, Placenta, Spinal cord, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15840583; DOI=10.1074/jbc.m500128200;
RA Ching K.H., Kisailus A.E., Burbelo P.D.;
RT "The role of SPECs, small Cdc42-binding proteins, in F-actin accumulation
RT at the immunological synapse.";
RL J. Biol. Chem. 280:23660-23667(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-52, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Detected in spleen, thymus and lung (at protein
CC level). {ECO:0000269|PubMed:15840583}.
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; AK039301; BAC30311.1; -; mRNA.
DR EMBL; AK080473; BAC37927.1; -; mRNA.
DR EMBL; AK088090; BAC40139.1; -; mRNA.
DR EMBL; AK090381; BAC41193.1; -; mRNA.
DR EMBL; AK135775; BAE22655.1; -; mRNA.
DR EMBL; AK145931; BAE26762.1; -; mRNA.
DR EMBL; AK146313; BAE27068.1; -; mRNA.
DR EMBL; AK160934; BAE36099.1; -; mRNA.
DR EMBL; AL607091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048935; AAH48935.1; -; mRNA.
DR CCDS; CCDS36153.1; -.
DR RefSeq; NP_848741.1; NM_178626.3.
DR RefSeq; XP_006534383.1; XM_006534320.2.
DR AlphaFoldDB; Q8BGH7; -.
DR STRING; 10090.ENSMUSP00000070725; -.
DR iPTMnet; Q8BGH7; -.
DR PhosphoSitePlus; Q8BGH7; -.
DR SwissPalm; Q8BGH7; -.
DR EPD; Q8BGH7; -.
DR MaxQB; Q8BGH7; -.
DR PaxDb; Q8BGH7; -.
DR PeptideAtlas; Q8BGH7; -.
DR PRIDE; Q8BGH7; -.
DR ProteomicsDB; 281717; -.
DR Antibodypedia; 25863; 97 antibodies from 14 providers.
DR DNASU; 72729; -.
DR Ensembl; ENSMUST00000064104; ENSMUSP00000070725; ENSMUSG00000052298.
DR GeneID; 72729; -.
DR KEGG; mmu:72729; -.
DR UCSC; uc007iyf.2; mouse.
DR CTD; 56990; -.
DR MGI; MGI:1919979; Cdc42se2.
DR VEuPathDB; HostDB:ENSMUSG00000052298; -.
DR eggNOG; ENOG502S22R; Eukaryota.
DR GeneTree; ENSGT00940000158245; -.
DR HOGENOM; CLU_173417_1_0_1; -.
DR InParanoid; Q8BGH7; -.
DR OMA; IGVPTNF; -.
DR OrthoDB; 1646014at2759; -.
DR PhylomeDB; Q8BGH7; -.
DR TreeFam; TF323815; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 72729; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cdc42se2; mouse.
DR PRO; PR:Q8BGH7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BGH7; protein.
DR Bgee; ENSMUSG00000052298; Expressed in animal zygote and 269 other tissues.
DR ExpressionAtlas; Q8BGH7; baseline and differential.
DR Genevisible; Q8BGH7; MM.
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:MGI.
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 1: Evidence at protein level;
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_0000334640"
FT DOMAIN 29..42
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 76
FT /note="M -> T (in Ref. 1; BAE26762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9223 MW; 98C5E82176DA990A CRC64;
MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
QSKGGYGGGM PANVQMQLVD TKAG
