ID   CYRIB_BOVIN             Reviewed;         324 AA.
AC   Q2KJI3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=CYFIP-related Rac1 interactor B;
DE   AltName: Full=Protein FAM49B;
GN   Name=CYRIB; Synonyms=FAM49B;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negatively regulates RAC1 signaling and RAC1-driven
CC       cytoskeletal remodeling. Regulates chemotaxis, cell migration and
CC       epithelial polarization by controlling the polarity, plasticity,
CC       duration and extent of protrusions. Limits Rac1 mediated activation of
CC       the Scar/WAVE complex, focuses protrusion signals and regulates
CC       pseudopod complexity by inhibiting Scar/WAVE-induced actin
CC       polymerization. Protects against Salmonella bacterial infection.
CC       Attenuates processes such as macropinocytosis, phagocytosis and cell
CC       migration and restrict sopE-mediated bacterial entry (By similarity).
CC       Restricts also infection mediated by Mycobacterium tuberculosis and
CC       Listeria monocytogenes (By similarity). Involved in the regulation of
CC       mitochondrial dynamics and oxidative stress (By similarity).
CC       {ECO:0000250|UniProtKB:Q921M7, ECO:0000250|UniProtKB:Q9NUQ9}.
CC   -!- SUBUNIT: Interacts with RAC1 (GTP-bound form preferentially).
CC       {ECO:0000250|UniProtKB:Q9NUQ9}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NUQ9}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q9NUQ9}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9NUQ9}.
CC   -!- PTM: Ubiquitinated at Lys-74 upon Salmonella bacterial infection.
CC       {ECO:0000250|UniProtKB:Q9NUQ9}.
CC   -!- SIMILARITY: Belongs to the CYRI family. {ECO:0000305}.
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DR   EMBL; BC105327; AAI05328.1; -; mRNA.
DR   RefSeq; NP_001039512.1; NM_001046047.1.
DR   AlphaFoldDB; Q2KJI3; -.
DR   SMR; Q2KJI3; -.
DR   STRING; 9913.ENSBTAP00000040143; -.
DR   PaxDb; Q2KJI3; -.
DR   PeptideAtlas; Q2KJI3; -.
DR   PRIDE; Q2KJI3; -.
DR   Ensembl; ENSBTAT00000040368; ENSBTAP00000040143; ENSBTAG00000020801.
DR   Ensembl; ENSBTAT00000080408; ENSBTAP00000061575; ENSBTAG00000020801.
DR   GeneID; 510019; -.
DR   KEGG; bta:510019; -.
DR   CTD; 51571; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020801; -.
DR   VGNC; VGNC:28819; CYRIB.
DR   eggNOG; KOG3951; Eukaryota.
DR   GeneTree; ENSGT00390000015159; -.
DR   HOGENOM; CLU_056470_0_0_1; -.
DR   InParanoid; Q2KJI3; -.
DR   OrthoDB; 1129868at2759; -.
DR   TreeFam; TF314541; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000020801; Expressed in neutrophil and 104 other tissues.
DR   ExpressionAtlas; Q2KJI3; baseline and differential.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0023030; F:MHC class Ib protein binding, via antigen binding groove; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:UniProtKB.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS: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; ISS:UniProtKB.
DR   GO; GO:0050920; P:regulation of chemotaxis; ISS:UniProtKB.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0090140; P:regulation of mitochondrial fission; ISS:UniProtKB.
DR   InterPro; IPR039789; CYRI.
DR   InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR   PANTHER; PTHR12422; PTHR12422; 1.
DR   Pfam; PF07159; DUF1394; 1.
PE   2: Evidence at transcript level;
KW   Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Myristate;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUQ9"
FT   CHAIN           2..324
FT                   /note="CYFIP-related Rac1 interactor B"
FT                   /id="PRO_0000290016"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUQ9"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUQ9"
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