CYRIB_HUMAN
ID CYRIB_HUMAN Reviewed; 324 AA.
AC Q9NUQ9; Q96AZ5; Q9NW21; Q9NZE7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=CYFIP-related Rac1 interactor B {ECO:0000305};
DE AltName: Full=L1;
GN Name=CYRIB {ECO:0000303|PubMed:30250061, ECO:0000312|HGNC:HGNC:25216};
GN Synonyms=CYRI {ECO:0000303|PubMed:31285585}, FAM49B; ORFNames=BM-009;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-169.
RA Petroziello J., Carter P.;
RT "Expression profiling in NSCLC.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-169.
RC TISSUE=Brain, Kidney, and 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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [8]
RP MYRISTOYLATION AT GLY-2, FUNCTION, INTERACTION WITH RAC1, AND MUTAGENESIS
RP OF 160-ARG-ARG-161.
RX PubMed=30250061; DOI=10.1038/s41556-018-0198-9;
RA Fort L., Batista J.M., Thomason P.A., Spence H.J., Whitelaw J.A.,
RA Tweedy L., Greaves J., Martin K.J., Anderson K.I., Brown P., Lilla S.,
RA Neilson M.P., Tafelmeyer P., Zanivan S., Ismail S., Bryant D.M.,
RA Tomkinson N.C.O., Chamberlain L.H., Mastick G.S., Insall R.H.,
RA Machesky L.M.;
RT "Fam49/CYRI interacts with Rac1 and locally suppresses protrusions.";
RL Nat. Cell Biol. 20:1159-1171(2018).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29059164; DOI=10.1038/onc.2017.358;
RA Chattaragada M.S., Riganti C., Sassoe M., Principe M., Santamorena M.M.,
RA Roux C., Curcio C., Evangelista A., Allavena P., Salvia R., Rusev B.,
RA Scarpa A., Cappello P., Novelli F.;
RT "FAM49B, a novel regulator of mitochondrial function and integrity that
RT suppresses tumor metastasis.";
RL Oncogene 37:697-709(2018).
RN [10]
RP FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF PRO-150 AND ARG-161,
RP INDUCTION BY SALMONELLA (MICROBIAL INFECTION), AND UBIQUITINATION AT
RP LYS-74.
RX PubMed=31285585; DOI=10.1038/s41564-019-0484-8;
RA Yuki K.E., Marei H., Fiskin E., Eva M.M., Gopal A.A.,
RA Schwartzentruber J.A., Majewski J., Cellier M., Mandl J.N., Vidal S.M.,
RA Malo D., Dikic I.;
RT "CYRI/FAM49B negatively regulates RAC1-driven cytoskeletal remodelling and
RT protects against bacterial infection.";
RL Nat. Microbiol. 4:1516-1531(2019).
CC -!- FUNCTION: Negatively regulates RAC1 signaling and RAC1-driven
CC cytoskeletal remodeling (PubMed:31285585, PubMed:30250061). Regulates
CC chemotaxis, cell migration and epithelial polarization by controlling
CC the polarity, plasticity, duration and extent of protrusions. Limits
CC Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion
CC signals and regulates pseudopod complexity by inhibiting Scar/WAVE-
CC induced actin polymerization (PubMed:30250061). Protects against
CC Salmonella bacterial infection. Attenuates processes such as
CC macropinocytosis, phagocytosis and cell migration and restrict sopE-
CC mediated bacterial entry (PubMed:31285585). Restricts also infection
CC mediated by Mycobacterium tuberculosis and Listeria monocytogenes (By
CC similarity). Involved in the regulation of mitochondrial dynamics and
CC oxidative stress (PubMed:29059164). {ECO:0000250|UniProtKB:Q921M7,
CC ECO:0000269|PubMed:29059164, ECO:0000269|PubMed:30250061,
CC ECO:0000269|PubMed:31285585}.
CC -!- SUBUNIT: Interacts with RAC1 (GTP-bound form preferentially).
CC {ECO:0000269|PubMed:30250061, ECO:0000269|PubMed:31285585}.
CC -!- INTERACTION:
CC Q9NUQ9; P46379-2: BAG6; NbExp=3; IntAct=EBI-1055930, EBI-10988864;
CC Q9NUQ9; O00291: HIP1; NbExp=3; IntAct=EBI-1055930, EBI-473886;
CC Q9NUQ9; O14901: KLF11; NbExp=3; IntAct=EBI-1055930, EBI-948266;
CC Q9NUQ9; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-1055930, EBI-740897;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:29059164}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUQ9-2; Sequence=VSP_056503;
CC -!- INDUCTION: Protein levels are negatively regulated by Salmonella.
CC {ECO:0000269|PubMed:31285585}.
CC -!- PTM: Ubiquitinated at Lys-74 upon Salmonella bacterial infection.
CC {ECO:0000269|PubMed:31285585}.
CC -!- SIMILARITY: Belongs to the CYRI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64265.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF208851; AAF64265.1; ALT_FRAME; mRNA.
DR EMBL; AY598320; AAT06731.1; -; mRNA.
DR EMBL; AK001226; BAA91566.1; -; mRNA.
DR EMBL; AK002059; BAA92062.1; -; mRNA.
DR EMBL; AC022973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003599; AAH03599.1; -; mRNA.
DR EMBL; BC016345; AAH16345.1; -; mRNA.
DR EMBL; BC017297; AAH17297.1; -; mRNA.
DR CCDS; CCDS6361.1; -. [Q9NUQ9-1]
DR CCDS; CCDS83327.1; -. [Q9NUQ9-2]
DR RefSeq; NP_001243692.1; NM_001256763.1. [Q9NUQ9-1]
DR RefSeq; NP_001317541.1; NM_001330612.1. [Q9NUQ9-2]
DR RefSeq; NP_057707.3; NM_016623.4. [Q9NUQ9-1]
DR RefSeq; XP_011515410.1; XM_011517108.2.
DR RefSeq; XP_011515411.1; XM_011517109.2.
DR RefSeq; XP_011515412.1; XM_011517110.2.
DR RefSeq; XP_011515413.1; XM_011517111.2.
DR RefSeq; XP_011515414.1; XM_011517112.2. [Q9NUQ9-1]
DR RefSeq; XP_011515415.1; XM_011517113.2.
DR RefSeq; XP_011515416.1; XM_011517114.2.
DR RefSeq; XP_011515417.1; XM_011517115.2.
DR RefSeq; XP_011515423.1; XM_011517121.2. [Q9NUQ9-1]
DR RefSeq; XP_011515424.1; XM_011517122.2.
DR RefSeq; XP_011515425.1; XM_011517123.2.
DR RefSeq; XP_011515426.1; XM_011517124.2.
DR RefSeq; XP_011515427.1; XM_011517125.2.
DR RefSeq; XP_016869028.1; XM_017013539.1.
DR RefSeq; XP_016869029.1; XM_017013540.1.
DR RefSeq; XP_016869030.1; XM_017013541.1.
DR RefSeq; XP_016869031.1; XM_017013542.1.
DR RefSeq; XP_016869032.1; XM_017013543.1.
DR RefSeq; XP_016869033.1; XM_017013544.1.
DR RefSeq; XP_016869034.1; XM_017013545.1. [Q9NUQ9-1]
DR RefSeq; XP_016869035.1; XM_017013546.1.
DR RefSeq; XP_016869036.1; XM_017013547.1.
DR RefSeq; XP_016869037.1; XM_017013548.1. [Q9NUQ9-1]
DR RefSeq; XP_016869038.1; XM_017013549.1.
DR RefSeq; XP_016869039.1; XM_017013550.1.
DR RefSeq; XP_016869040.1; XM_017013551.1. [Q9NUQ9-1]
DR RefSeq; XP_016869047.1; XM_017013558.1.
DR RefSeq; XP_016869048.1; XM_017013559.1.
DR RefSeq; XP_016869049.1; XM_017013560.1.
DR RefSeq; XP_016869050.1; XM_017013561.1.
DR RefSeq; XP_016869051.1; XM_017013562.1.
DR PDB; 7AJK; X-ray; 3.10 A; CCC=1-324.
DR PDBsum; 7AJK; -.
DR AlphaFoldDB; Q9NUQ9; -.
DR SMR; Q9NUQ9; -.
DR BioGRID; 119617; 95.
DR IntAct; Q9NUQ9; 16.
DR MINT; Q9NUQ9; -.
DR STRING; 9606.ENSP00000429150; -.
DR iPTMnet; Q9NUQ9; -.
DR MetOSite; Q9NUQ9; -.
DR PhosphoSitePlus; Q9NUQ9; -.
DR SwissPalm; Q9NUQ9; -.
DR BioMuta; FAM49B; -.
DR DMDM; 52782794; -.
DR EPD; Q9NUQ9; -.
DR jPOST; Q9NUQ9; -.
DR MassIVE; Q9NUQ9; -.
DR MaxQB; Q9NUQ9; -.
DR PaxDb; Q9NUQ9; -.
DR PeptideAtlas; Q9NUQ9; -.
DR PRIDE; Q9NUQ9; -.
DR ProteomicsDB; 82714; -. [Q9NUQ9-1]
DR ProteomicsDB; 82891; -.
DR Antibodypedia; 2198; 85 antibodies from 21 providers.
DR DNASU; 51571; -.
DR Ensembl; ENST00000401979.6; ENSP00000384880.2; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000517654.5; ENSP00000430674.1; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000519110.5; ENSP00000429078.1; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000519540.5; ENSP00000429499.1; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000519824.6; ENSP00000429150.1; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000522250.5; ENSP00000429978.1; ENSG00000153310.20. [Q9NUQ9-2]
DR Ensembl; ENST00000522746.5; ENSP00000428117.1; ENSG00000153310.20. [Q9NUQ9-1]
DR Ensembl; ENST00000522941.5; ENSP00000430433.1; ENSG00000153310.20. [Q9NUQ9-2]
DR Ensembl; ENST00000523509.5; ENSP00000429802.1; ENSG00000153310.20. [Q9NUQ9-1]
DR GeneID; 51571; -.
DR KEGG; hsa:51571; -.
DR UCSC; uc003yss.5; human. [Q9NUQ9-1]
DR CTD; 51571; -.
DR DisGeNET; 51571; -.
DR GeneCards; CYRIB; -.
DR HGNC; HGNC:25216; CYRIB.
DR HPA; ENSG00000153310; Tissue enhanced (bone).
DR MIM; 617978; gene.
DR neXtProt; NX_Q9NUQ9; -.
DR OpenTargets; ENSG00000153310; -.
DR VEuPathDB; HostDB:ENSG00000153310; -.
DR eggNOG; KOG3951; Eukaryota.
DR GeneTree; ENSGT00390000015159; -.
DR HOGENOM; CLU_056470_0_0_1; -.
DR InParanoid; Q9NUQ9; -.
DR OMA; EYRSRFN; -.
DR OrthoDB; 1129868at2759; -.
DR PhylomeDB; Q9NUQ9; -.
DR TreeFam; TF314541; -.
DR PathwayCommons; Q9NUQ9; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9NUQ9; -.
DR BioGRID-ORCS; 51571; 46 hits in 1092 CRISPR screens.
DR ChiTaRS; FAM49B; human.
DR GenomeRNAi; 51571; -.
DR Pharos; Q9NUQ9; Tbio.
DR PRO; PR:Q9NUQ9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NUQ9; protein.
DR Bgee; ENSG00000153310; Expressed in monocyte and 204 other tissues.
DR ExpressionAtlas; Q9NUQ9; baseline and differential.
DR Genevisible; Q9NUQ9; HS.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0023030; F:MHC class Ib protein binding, via antigen binding groove; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:2000568; P:positive regulation of memory T cell activation; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP:UniProtKB.
DR InterPro; IPR039789; CYRI.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR PANTHER; PTHR12422; PTHR12422; 1.
DR Pfam; PF07159; DUF1394; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Lipoprotein; Membrane;
KW Mitochondrion; Myristate; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:30250061"
FT CHAIN 2..324
FT /note="CYFIP-related Rac1 interactor B"
FT /id="PRO_0000187060"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:30250061"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:31285585"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056503"
FT VARIANT 169
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_019704"
FT MUTAGEN 150
FT /note="P->D: No effect on interaction with RAC1. Almost
FT abolishes interaction with RAC1; when associated with D-
FT 161."
FT /evidence="ECO:0000269|PubMed:31285585"
FT MUTAGEN 160..161
FT /note="RR->DD: Abolishes interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:30250061"
FT MUTAGEN 161
FT /note="R->D: Strongly decreases interaction with RAC1.
FT Almost abolishes interaction with RAC1; when associated
FT with D-150."
FT /evidence="ECO:0000269|PubMed:31285585"
SQ SEQUENCE 324 AA; 36748 MW; EE370E3D170A6E38 CRC64;
MGNLLKVLTC TDLEQGPNFF LDFENAQPTE SEKEIYNQVN VVLKDAEGIL EDLQSYRGAG
HEIREAIQHP ADEKLQEKAW GAVVPLVGKL KKFYEFSQRL EAALRGLLGA LTSTPYSPTQ
HLEREQALAK QFAEILHFTL RFDELKMTNP AIQNDFSYYR RTLSRMRINN VPAEGENEVN
NELANRMSLF YAEATPMLKT LSDATTKFVS ENKNLPIENT TDCLSTMASV CRVMLETPEY
RSRFTNEETV SFCLRVMVGV IILYDHVHPV GAFAKTSKID MKGCIKVLKD QPPNSVEGLL
NALRYTTKHL NDETTSKQIK SMLQ
