FARP1_MOUSE
ID FARP1_MOUSE Reviewed; 1048 AA.
AC F8VPU2; C4IXU2;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 1;
DE AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 1;
GN Name=Farp1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1048.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-427 AND SER-892, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; THR-24; SER-373;
RP SER-389; SER-403; SER-427; SER-433; SER-437; SER-512; SER-875; SER-881;
RP SER-892; SER-899 AND SER-902, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23209303; DOI=10.1083/jcb.201205041;
RA Cheadle L., Biederer T.;
RT "The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal
RT dynamics and transsynaptic organization.";
RL J. Cell Biol. 199:985-1001(2012).
CC -!- FUNCTION: Functions as guanine nucleotide exchange factor for RAC1. May
CC play a role in semaphorin signaling. Plays a role in the assembly and
CC disassembly of dendritic filopodia, the formation of dendritic spines,
CC regulation of dendrite length and ultimately the formation of synapses
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CADM1. Interacts with RAC1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303};
CC Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic
CC side {ECO:0000269|PubMed:23209303}. Synapse
CC {ECO:0000269|PubMed:23209303}. Synapse, synaptosome {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell
CC membrane via interaction with CADM1. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus, striatum,
CC olfactory bulb, cerebellum and hindbrain (at protein level).
CC {ECO:0000269|PubMed:23209303}.
CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC domains can stabilize the protein in an autoinhibited conformation.
CC {ECO:0000250}.
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DR EMBL; AC154618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141229; AAI41230.1; -; mRNA.
DR CCDS; CCDS37015.1; -.
DR RefSeq; NP_598843.3; NM_134082.3.
DR RefSeq; XP_006518977.1; XM_006518914.3.
DR AlphaFoldDB; F8VPU2; -.
DR SMR; F8VPU2; -.
DR BioGRID; 230134; 9.
DR IntAct; F8VPU2; 3.
DR MINT; F8VPU2; -.
DR STRING; 10090.ENSMUSP00000026635; -.
DR iPTMnet; F8VPU2; -.
DR PhosphoSitePlus; F8VPU2; -.
DR EPD; F8VPU2; -.
DR jPOST; F8VPU2; -.
DR MaxQB; F8VPU2; -.
DR PaxDb; F8VPU2; -.
DR PeptideAtlas; F8VPU2; -.
DR PRIDE; F8VPU2; -.
DR ProteomicsDB; 267571; -.
DR Antibodypedia; 619; 217 antibodies from 20 providers.
DR DNASU; 223254; -.
DR Ensembl; ENSMUST00000026635; ENSMUSP00000026635; ENSMUSG00000025555.
DR GeneID; 223254; -.
DR KEGG; mmu:223254; -.
DR UCSC; uc007vaa.1; mouse.
DR CTD; 10160; -.
DR MGI; MGI:2446173; Farp1.
DR VEuPathDB; HostDB:ENSMUSG00000025555; -.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000155318; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR InParanoid; F8VPU2; -.
DR OMA; LAMQPTE; -.
DR OrthoDB; 476668at2759; -.
DR PhylomeDB; F8VPU2; -.
DR TreeFam; TF351276; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 223254; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Farp1; mouse.
DR PRO; PR:F8VPU2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; F8VPU2; protein.
DR Bgee; ENSMUSG00000025555; Expressed in humerus cartilage element and 240 other tissues.
DR ExpressionAtlas; F8VPU2; baseline and differential.
DR Genevisible; F8VPU2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 3.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Developmental protein;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..1048
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 1"
FT /id="PRO_0000422336"
FT DOMAIN 40..320
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 542..733
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 762..859
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 935..1032
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 886
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 619
FT /note="V -> I (in Ref. 2; AAI41230)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="I -> V (in Ref. 2; AAI41230)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="T -> I (in Ref. 2; AAI41230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1048 AA; 118875 MW; 6F626F96959B735A CRC64;
MGEIEQKPTP ASRLGAPENS GISTLERGQK PPPTPSGKLM TVKIQMLDDT QEAFEVPQRA
PGKVLFDAVC NHLNLVEGDY FGLEFPDHRK IVVWLDLLKP IVKQIRRPKH VVVKFVVKFF
PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL
AKNKYVPQQD ALEDRIMEFH HSHVGQTPAE SDFQLLEVAR RLEMYGIRLH PAKDREGTKI
NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDVNSSYQD TLEFLMAGRD
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
FERKHSKIHS TRSLVSQPTA PNSEVPKQSP QSASLTFGEG TESPGGQSCQ QAKETKACTL
ELGPHQSPAL PKSPPGSKAA DGTTVVPPEE EEEEEGGKDG IRPSNPQPPQ PSTGSLTGSP
HLSELSINSQ GGAAPANVTL SPNLSPDNKQ ASPLISPLLN DQACPRTDDE EEGRRKRFPT
DKAYYIAKEV STTERTYLKD LEVIASWFQS TVSKEDSMPE ALKSLIFPNF EPLHKFHTNF
LKEIEQRLAL WEGRSNAHVR GDYQRIGDVM LKNIQGMKHL AAHLWKHSEA LEALETSIKG
SRRLEHFCRD FELQKVCYLP LNTFLLRPLH RLMHYKHVLE RLCKHHPPNH ADFRDCRAAL
AEITEMVAQL HGTMIKMENF QKLHELKKDL IGIDNLVTPG REFIRLGSLS KLSGKGLQQR
MFFLFNDVLL YTSRGLTASN QFKVHGQLPL YGMTIEESEE EWGVPHCLTL RGQRQSIIVA
ASSRSEMEKW MEDIQMAIDL AEKSNGPTPE LLASSPPDNK SPDEATAADQ ESEDDLSASR
TSLERQAPHR GNTMVHVCWH RSTSVSMVDF SIAVENQLSG NLLRKFKNSN GWQKLWVVFT
NFCLFFYKSH QDSHPLASLP LLGYSLTIPS ESENIHKDYV FKLHFKSHVY YFRAESEYTF
ERWMEVIRSA TSSASRAHIL SHKESHLY
