ID   CYRIB_MOUSE             Reviewed;         324 AA.
AC   Q921M7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=CYFIP-related Rac1 interactor B;
DE   AltName: Full=Protein FAM49B;
GN   Name=Cyrib; Synonyms=Cyri {ECO:0000303|PubMed:31285585}, Fam49b;
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=Cerebellum, and Spleen;
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   STRAIN=Czech II; TISSUE=Mammary tumor;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
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   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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). Regulates chemotaxis, cell
CC       migration and epithelial polarization by controlling the polarity,
CC       plasticity, duration and extent of protrusions. Limits Rac1 mediated
CC       activation of the Scar/WAVE complex, focuses protrusion signals and
CC       regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin
CC       polymerization (By similarity). Protects against Salmonella bacterial
CC       infection. Attenuates processes such as macropinocytosis, phagocytosis
CC       and cell migration and restrict sopE-mediated bacterial entry
CC       (PubMed:31285585). Restricts also infection mediated by Mycobacterium
CC       tuberculosis and Listeria monocytogenes (PubMed:31285585). Involved in
CC       the regulation of mitochondrial dynamics and oxidative stress
CC       (PubMed:29059164). {ECO:0000250|UniProtKB:Q9NUQ9,
CC       ECO:0000269|PubMed:29059164, ECO:0000269|PubMed:31285585}.
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   -!- TISSUE SPECIFICITY: Expressed in pancreatic ducts (at protein level).
CC       {ECO:0000269|PubMed:29059164}.
CC   -!- PTM: Ubiquitinated at Lys-74 upon Salmonella bacterial infection.
CC       {ECO:0000250|UniProtKB:Q9NUQ9}.
CC   -!- DISRUPTION PHENOTYPE: Myeloid-specific conditional knockout mice have a
CC       reduced survival following Salmonella systemic infection. Upon
CC       infection, they show increased levels of several serum pro-inflammatory
CC       cytokines and chemokines produced by activated neutrophils and
CC       monocytes. {ECO:0000269|PubMed:31285585}.
CC   -!- SIMILARITY: Belongs to the CYRI family. {ECO:0000305}.
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DR   EMBL; AK028062; BAC25731.1; -; mRNA.
DR   EMBL; AK075613; BAC35858.1; -; mRNA.
DR   EMBL; BC011343; AAH11343.1; -; mRNA.
DR   CCDS; CCDS27505.1; -.
DR   RefSeq; NP_659095.1; NM_144846.5.
DR   RefSeq; XP_006520824.1; XM_006520761.2.
DR   RefSeq; XP_006520826.1; XM_006520763.2.
DR   RefSeq; XP_006520827.1; XM_006520764.3.
DR   RefSeq; XP_011243865.1; XM_011245563.1.
DR   RefSeq; XP_011243867.1; XM_011245565.2.
DR   PDB; 7AJL; X-ray; 2.37 A; AAA/BBB=26-324.
DR   PDBsum; 7AJL; -.
DR   AlphaFoldDB; Q921M7; -.
DR   SMR; Q921M7; -.
DR   BioGRID; 230158; 4.
DR   IntAct; Q921M7; 4.
DR   MINT; Q921M7; -.
DR   STRING; 10090.ENSMUSP00000066359; -.
DR   GlyConnect; 2631; 1 N-Linked glycan (1 site).
DR   GlyGen; Q921M7; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q921M7; -.
DR   PhosphoSitePlus; Q921M7; -.
DR   SwissPalm; Q921M7; -.
DR   EPD; Q921M7; -.
DR   MaxQB; Q921M7; -.
DR   PaxDb; Q921M7; -.
DR   PeptideAtlas; Q921M7; -.
DR   PRIDE; Q921M7; -.
DR   ProteomicsDB; 277027; -.
DR   Antibodypedia; 2198; 85 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000063838; ENSMUSP00000066359; ENSMUSG00000022378.
DR   Ensembl; ENSMUST00000164532; ENSMUSP00000132486; ENSMUSG00000022378.
DR   Ensembl; ENSMUST00000228226; ENSMUSP00000154320; ENSMUSG00000022378.
DR   GeneID; 223601; -.
DR   KEGG; mmu:223601; -.
DR   UCSC; uc007vze.2; mouse.
DR   CTD; 51571; -.
DR   MGI; MGI:1923520; Cyrib.
DR   VEuPathDB; HostDB:ENSMUSG00000022378; -.
DR   eggNOG; KOG3951; Eukaryota.
DR   GeneTree; ENSGT00390000015159; -.
DR   HOGENOM; CLU_056470_0_0_1; -.
DR   InParanoid; Q921M7; -.
DR   OMA; EYRSRFN; -.
DR   OrthoDB; 1129868at2759; -.
DR   PhylomeDB; Q921M7; -.
DR   TreeFam; TF314541; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   BioGRID-ORCS; 223601; 8 hits in 71 CRISPR screens.
DR   ChiTaRS; Fam49b; mouse.
DR   PRO; PR:Q921M7; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q921M7; protein.
DR   Bgee; ENSMUSG00000022378; Expressed in granulocyte and 246 other tissues.
DR   ExpressionAtlas; Q921M7; baseline and differential.
DR   Genevisible; Q921M7; MM.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
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; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
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; ISS: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; IDA:UniProtKB.
DR   GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProtKB.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA: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; 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; Isopeptide bond; Lipoprotein; Membrane; Mitochondrion;
KW   Myristate; 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_0000187061"
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;  36776 MW;  EE370E3D003A6E38 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 NDETTSKQIR SMLQ