C42S1_MOUSE
ID C42S1_MOUSE Reviewed; 80 AA.
AC Q8BHL7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=CDC42 small effector protein 1;
GN Name=Cdc42se1;
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; TISSUE=Liver, Skin, and Stomach;
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 MRNA].
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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}.
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; AK004859; BAC25099.1; -; mRNA.
DR EMBL; AK019052; BAC25576.1; -; mRNA.
DR EMBL; AK028573; BAC26014.1; -; mRNA.
DR EMBL; BC060964; AAH60964.1; -; mRNA.
DR CCDS; CCDS38545.1; -.
DR RefSeq; NP_001033797.1; NM_001038708.3.
DR RefSeq; NP_765983.1; NM_172395.3.
DR AlphaFoldDB; Q8BHL7; -.
DR STRING; 10090.ENSMUSP00000052986; -.
DR iPTMnet; Q8BHL7; -.
DR PhosphoSitePlus; Q8BHL7; -.
DR SwissPalm; Q8BHL7; -.
DR MaxQB; Q8BHL7; -.
DR PaxDb; Q8BHL7; -.
DR PeptideAtlas; Q8BHL7; -.
DR PRIDE; Q8BHL7; -.
DR ProteomicsDB; 281716; -.
DR Antibodypedia; 34046; 10 antibodies from 9 providers.
DR DNASU; 57912; -.
DR Ensembl; ENSMUST00000053872; ENSMUSP00000052986; ENSMUSG00000046722.
DR Ensembl; ENSMUST00000107201; ENSMUSP00000102819; ENSMUSG00000046722.
DR GeneID; 57912; -.
DR KEGG; mmu:57912; -.
DR UCSC; uc008qiu.2; mouse.
DR CTD; 56882; -.
DR MGI; MGI:1889510; Cdc42se1.
DR VEuPathDB; HostDB:ENSMUSG00000046722; -.
DR eggNOG; ENOG502S499; Eukaryota.
DR GeneTree; ENSGT00940000160112; -.
DR HOGENOM; CLU_173417_1_0_1; -.
DR InParanoid; Q8BHL7; -.
DR OMA; DRPWNNS; -.
DR OrthoDB; 1646014at2759; -.
DR PhylomeDB; Q8BHL7; -.
DR TreeFam; TF323815; -.
DR BioGRID-ORCS; 57912; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cdc42se1; mouse.
DR PRO; PR:Q8BHL7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BHL7; protein.
DR Bgee; ENSMUSG00000046722; Expressed in granulocyte and 261 other tissues.
DR ExpressionAtlas; Q8BHL7; baseline and differential.
DR Genevisible; Q8BHL7; MM.
DR GO; GO:0005938; C:cell cortex; ISS:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:MGI.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; ISS:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:MGI.
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 PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane;
KW Palmitate; Phagocytosis; Reference proteome.
FT CHAIN 1..80
FT /note="CDC42 small effector protein 1"
FT /id="PRO_0000334630"
FT DOMAIN 30..43
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 48..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 80 AA; 9076 MW; 0652F07FB832CF2B CRC64;
MSEFWHKLGC CVVEKPQPKK KRRRIDRTMI GEPMNFVHLT HIGSGEMGAG DGLAMTGAVQ
EQMRSKGNHR DRPWSNSRAL
