Full text data of CDC42SE2
CDC42SE2
(SPEC2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
CDC42 small effector protein 2 (Small effector of CDC42 protein 2)
CDC42 small effector protein 2 (Small effector of CDC42 protein 2)
UniProt
Q9NRR3
ID C42S2_HUMAN Reviewed; 84 AA.
AC Q9NRR3; B2R622; Q4KMT9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=CDC42 small effector protein 2;
DE AltName: Full=Small effector of CDC42 protein 2;
GN Name=CDC42SE2; Synonyms=SPEC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CDC42.
RX PubMed=10816584; DOI=10.1074/jbc.M002832200;
RA Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.;
RT "SPECs, small binding proteins for Cdc42.";
RL J. Biol. Chem. 275:22650-22656(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PALMITOYLATION
RP AT CYS-10 AND CYS-11.
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
RT accumulation at the immunological synapse.";
RL J. Biol. Chem. 280:23660-23667(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17045588; DOI=10.1016/j.yexcr.2006.09.011;
RA Ching K.H., Kisailus A.E., Burbelo P.D.;
RT "Biochemical characterization of distinct regions of SPEC molecules
RT and their role in phagocytosis.";
RL Exp. Cell Res. 313:10-21(2007).
RN [7]
RP POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX PubMed=17030554; DOI=10.1093/hmg/ddl409;
RA Chen X., Wang X., Hossain S., O'Neill F.A., Walsh D., Pless L.,
RA Chowdari K.V., Nimgaonkar V.L., Schwab S.G., Wildenauer D.B.,
RA Sullivan P.F., van den Oord E., Kendler K.S.;
RT "Haplotypes spanning SPEC2, PDZ-GEF2 and ACSL6 genes are associated
RT with schizophrenia.";
RL Hum. Mol. Genet. 15:3329-3342(2006).
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton by acting downstream of CDC42, inducing actin
CC filament assembly. Alters CDC42-induced cell shape changes. In
CC activated T-cells, may play a role in CDC42-mediated F-actin
CC accumulation at the immunological synapse. May play a role in
CC early contractile events in phagocytosis in macrophages.
CC -!- SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts
CC weakly with RAC1 and not at all with RHOA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Lipid-anchor. Cell projection, phagocytic cup. Note=Recruited to
CC the activated TCR prior actin polymerization. Localizes at the
CC phagocytic cup of macrophages.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC T-lymphocytes. Highly expressed in CCRF-CEM T-lymphocytes, Jurkat
CC T-lymphocytes, and Raji B-lymphocytes compared (at protein level).
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC -!- MISCELLANEOUS: CDC42SE2 is mapped in the genomic region associated
CC with schizophrenia.
CC -!- SIMILARITY: Belongs to the CDC42SE/SPEC family.
CC -!- SIMILARITY: Contains 1 CRIB domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF189692; AAF87598.1; -; mRNA.
DR EMBL; AK312406; BAG35319.1; -; mRNA.
DR EMBL; CH471062; EAW62373.1; -; Genomic_DNA.
DR EMBL; BC096703; AAH96703.1; -; mRNA.
DR EMBL; BC096738; AAH96738.1; -; mRNA.
DR EMBL; BC098349; AAH98349.1; -; mRNA.
DR RefSeq; NP_001033791.1; NM_001038702.1.
DR RefSeq; NP_064625.1; NM_020240.2.
DR UniGene; Hs.508829; -.
DR UniGene; Hs.713870; -.
DR ProteinModelPortal; Q9NRR3; -.
DR STRING; 9606.ENSP00000353706; -.
DR PhosphoSite; Q9NRR3; -.
DR DMDM; 74719133; -.
DR PaxDb; Q9NRR3; -.
DR PRIDE; Q9NRR3; -.
DR Ensembl; ENST00000360515; ENSP00000353706; ENSG00000158985.
DR Ensembl; ENST00000395246; ENSP00000378667; ENSG00000158985.
DR Ensembl; ENST00000505065; ENSP00000427421; ENSG00000158985.
DR GeneID; 56990; -.
DR KEGG; hsa:56990; -.
DR UCSC; uc003kvh.3; human.
DR CTD; 56990; -.
DR GeneCards; GC05P130581; -.
DR H-InvDB; HIX0005148; -.
DR HGNC; HGNC:18547; CDC42SE2.
DR HPA; HPA038624; -.
DR neXtProt; NX_Q9NRR3; -.
DR PharmGKB; PA133787056; -.
DR eggNOG; NOG78697; -.
DR HOGENOM; HOG000006512; -.
DR HOVERGEN; HBG107546; -.
DR InParanoid; Q9NRR3; -.
DR OMA; ISANVQM; -.
DR PhylomeDB; Q9NRR3; -.
DR SignaLink; Q9NRR3; -.
DR GenomeRNAi; 56990; -.
DR NextBio; 62683; -.
DR PRO; PR:Q9NRR3; -.
DR ArrayExpress; Q9NRR3; -.
DR Bgee; Q9NRR3; -.
DR CleanEx; HS_CDC42SE2; -.
DR Genevestigator; Q9NRR3; -.
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:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IDA:UniProtKB.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF00786; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cell shape; Complete proteome;
KW Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Palmitate;
KW Phagocytosis; Reference proteome.
FT CHAIN 1 84 CDC42 small effector protein 2.
FT /FTId=PRO_0000334639.
FT DOMAIN 29 42 CRIB.
FT COMPBIAS 20 23 Poly-Arg.
FT LIPID 10 10 S-palmitoyl cysteine.
FT LIPID 11 11 S-palmitoyl cysteine.
SQ SEQUENCE 84 AA; 9223 MW; 98C5E82176DA990A CRC64;
MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
QSKGGYGGGM PANVQMQLVD TKAG
//
ID C42S2_HUMAN Reviewed; 84 AA.
AC Q9NRR3; B2R622; Q4KMT9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=CDC42 small effector protein 2;
DE AltName: Full=Small effector of CDC42 protein 2;
GN Name=CDC42SE2; Synonyms=SPEC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CDC42.
RX PubMed=10816584; DOI=10.1074/jbc.M002832200;
RA Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.;
RT "SPECs, small binding proteins for Cdc42.";
RL J. Biol. Chem. 275:22650-22656(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PALMITOYLATION
RP AT CYS-10 AND CYS-11.
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
RT accumulation at the immunological synapse.";
RL J. Biol. Chem. 280:23660-23667(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17045588; DOI=10.1016/j.yexcr.2006.09.011;
RA Ching K.H., Kisailus A.E., Burbelo P.D.;
RT "Biochemical characterization of distinct regions of SPEC molecules
RT and their role in phagocytosis.";
RL Exp. Cell Res. 313:10-21(2007).
RN [7]
RP POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX PubMed=17030554; DOI=10.1093/hmg/ddl409;
RA Chen X., Wang X., Hossain S., O'Neill F.A., Walsh D., Pless L.,
RA Chowdari K.V., Nimgaonkar V.L., Schwab S.G., Wildenauer D.B.,
RA Sullivan P.F., van den Oord E., Kendler K.S.;
RT "Haplotypes spanning SPEC2, PDZ-GEF2 and ACSL6 genes are associated
RT with schizophrenia.";
RL Hum. Mol. Genet. 15:3329-3342(2006).
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton by acting downstream of CDC42, inducing actin
CC filament assembly. Alters CDC42-induced cell shape changes. In
CC activated T-cells, may play a role in CDC42-mediated F-actin
CC accumulation at the immunological synapse. May play a role in
CC early contractile events in phagocytosis in macrophages.
CC -!- SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts
CC weakly with RAC1 and not at all with RHOA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Lipid-anchor. Cell projection, phagocytic cup. Note=Recruited to
CC the activated TCR prior actin polymerization. Localizes at the
CC phagocytic cup of macrophages.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC T-lymphocytes. Highly expressed in CCRF-CEM T-lymphocytes, Jurkat
CC T-lymphocytes, and Raji B-lymphocytes compared (at protein level).
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC -!- MISCELLANEOUS: CDC42SE2 is mapped in the genomic region associated
CC with schizophrenia.
CC -!- SIMILARITY: Belongs to the CDC42SE/SPEC family.
CC -!- SIMILARITY: Contains 1 CRIB domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF189692; AAF87598.1; -; mRNA.
DR EMBL; AK312406; BAG35319.1; -; mRNA.
DR EMBL; CH471062; EAW62373.1; -; Genomic_DNA.
DR EMBL; BC096703; AAH96703.1; -; mRNA.
DR EMBL; BC096738; AAH96738.1; -; mRNA.
DR EMBL; BC098349; AAH98349.1; -; mRNA.
DR RefSeq; NP_001033791.1; NM_001038702.1.
DR RefSeq; NP_064625.1; NM_020240.2.
DR UniGene; Hs.508829; -.
DR UniGene; Hs.713870; -.
DR ProteinModelPortal; Q9NRR3; -.
DR STRING; 9606.ENSP00000353706; -.
DR PhosphoSite; Q9NRR3; -.
DR DMDM; 74719133; -.
DR PaxDb; Q9NRR3; -.
DR PRIDE; Q9NRR3; -.
DR Ensembl; ENST00000360515; ENSP00000353706; ENSG00000158985.
DR Ensembl; ENST00000395246; ENSP00000378667; ENSG00000158985.
DR Ensembl; ENST00000505065; ENSP00000427421; ENSG00000158985.
DR GeneID; 56990; -.
DR KEGG; hsa:56990; -.
DR UCSC; uc003kvh.3; human.
DR CTD; 56990; -.
DR GeneCards; GC05P130581; -.
DR H-InvDB; HIX0005148; -.
DR HGNC; HGNC:18547; CDC42SE2.
DR HPA; HPA038624; -.
DR neXtProt; NX_Q9NRR3; -.
DR PharmGKB; PA133787056; -.
DR eggNOG; NOG78697; -.
DR HOGENOM; HOG000006512; -.
DR HOVERGEN; HBG107546; -.
DR InParanoid; Q9NRR3; -.
DR OMA; ISANVQM; -.
DR PhylomeDB; Q9NRR3; -.
DR SignaLink; Q9NRR3; -.
DR GenomeRNAi; 56990; -.
DR NextBio; 62683; -.
DR PRO; PR:Q9NRR3; -.
DR ArrayExpress; Q9NRR3; -.
DR Bgee; Q9NRR3; -.
DR CleanEx; HS_CDC42SE2; -.
DR Genevestigator; Q9NRR3; -.
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:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IDA:UniProtKB.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF00786; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cell shape; Complete proteome;
KW Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Palmitate;
KW Phagocytosis; Reference proteome.
FT CHAIN 1 84 CDC42 small effector protein 2.
FT /FTId=PRO_0000334639.
FT DOMAIN 29 42 CRIB.
FT COMPBIAS 20 23 Poly-Arg.
FT LIPID 10 10 S-palmitoyl cysteine.
FT LIPID 11 11 S-palmitoyl cysteine.
SQ SEQUENCE 84 AA; 9223 MW; 98C5E82176DA990A CRC64;
MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
QSKGGYGGGM PANVQMQLVD TKAG
//