FARP1_RAT
ID FARP1_RAT Reviewed; 1049 AA.
AC F1LYQ8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 79.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CADM1 AND RAC1,
RP DEVELOPMENTAL STAGE, 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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-24; SER-876 AND
RP SER-893, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in semaphorin signaling (By similarity).
CC Functions as guanine nucleotide exchange factor for RAC1. Plays a role
CC in the assembly and disassembly of dendritic filopodia, the formation
CC of dendritic spines, regulation of dendrite length and ultimately the
CC formation of synapses. {ECO:0000250, ECO:0000269|PubMed:23209303}.
CC -!- SUBUNIT: Interacts with CADM1. Interacts with RAC1.
CC {ECO:0000269|PubMed:23209303}.
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 {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000269|PubMed:23209303}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23209303}. Cell projection, filopodium
CC {ECO:0000269|PubMed:23209303}. Cell projection, dendrite
CC {ECO:0000269|PubMed:23209303}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:23209303}. Note=Recruited to the cell membrane via
CC interaction with CADM1.
CC -!- TISSUE SPECIFICITY: Detected in forbrain (at protein level).
CC {ECO:0000269|PubMed:23209303}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in forebrain during the first 15
CC days after birth, a period of intense synaptogenesis.
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; AABR06085873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06085880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473951; EDM02559.1; -; Genomic_DNA.
DR RefSeq; NP_001100757.1; NM_001107287.1.
DR RefSeq; XP_006252534.1; XM_006252472.3.
DR RefSeq; XP_006252535.1; XM_006252473.3.
DR RefSeq; XP_017455209.1; XM_017599720.1.
DR AlphaFoldDB; F1LYQ8; -.
DR SMR; F1LYQ8; -.
DR STRING; 10116.ENSRNOP00000015271; -.
DR CarbonylDB; F1LYQ8; -.
DR iPTMnet; F1LYQ8; -.
DR PhosphoSitePlus; F1LYQ8; -.
DR jPOST; F1LYQ8; -.
DR PaxDb; F1LYQ8; -.
DR PeptideAtlas; F1LYQ8; -.
DR PRIDE; F1LYQ8; -.
DR Ensembl; ENSRNOT00000015271; ENSRNOP00000015271; ENSRNOG00000011203.
DR GeneID; 306183; -.
DR KEGG; rno:306183; -.
DR CTD; 10160; -.
DR RGD; 1305346; Farp1.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000155318; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR InParanoid; F1LYQ8; -.
DR OMA; LAMQPTE; -.
DR OrthoDB; 476668at2759; -.
DR TreeFam; TF351276; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:F1LYQ8; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000011203; Expressed in lung and 19 other tissues.
DR Genevisible; F1LYQ8; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IDA:SynGO.
DR GO; GO:0007416; P:synapse assembly; IMP: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..1049
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 1"
FT /id="PRO_0000422337"
FT DOMAIN 40..320
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 543..734
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 763..860
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 936..1033
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..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..908
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 472..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F1"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
SQ SEQUENCE 1049 AA; 118842 MW; C6B916C7739E71CC CRC64;
MGEIEQKPTP ASRLGAPENS GISTLERGQK PPPTPSGKLM TVKIQMLDDT QEAFEVPQRA
PGKVLFDAVC NHLNLVEGDY FGLEFPDHRK IVVWLDLLKP IVKQIRRPKH VLVKFVVKFF
PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL
AKNKYVPQQD ALEDKIVEFH HSHIGQTPAE SDFQLLEVAR RLEMYGIRLH PAKDREGTKI
NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDVNSSYQD TLEFLMAGRD
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
FERKHSKIHS TRSLVSQPTA PNSEVPKQSP QSASLTFGEG TESPSAQSCQ QAKETKVCTL
EPGPRQSPAL SKSPSGSKAA DGTAAAAPPE EEDEEEGGKD GIRPSNPQPP QPSTGSLTGS
PHLSELSINS QGGAAPANVT LSPNLSPDNK QASPLISPLL NDQACPRTDD EEEGRRKRFP
TDKAYYIAKE VSTTERTYLK DLEVIASWFQ STVSKEDSMP EALKSLIFPN FEPLHKFHTN
FLKEIEQRLA LWEGRSNAHI RGDYQRIGDV MLKNIQGMKH LAAHLWKHSE ALEALETSIK
GSRRLEHFCR DFELQKVCYL PLNTFLLRPL HRLMHYKQVL ERLCKHHPPN HADFRDCRAA
LAEITEMVAQ LHGTMIKMEN FQKLHELKKD LIGIDNLVIP GREFIRLGSL SKLSGKGLQQ
RMFFLFNDVL LYTSRGLTAS NQFKVHGQLP LYGMTIEESE EEWGVPHCLT LRGQRQSIIV
AASSRSEMEK WLEDIQMAID LAEKSNGPTP ELLASSPPDN KSPDEATAAD QESEDDLSAS
RTSLERQAPH RGNTMVHVCW HRSTSVSMVD FSIAVENQLS GNLLRKFKNS NGWQKLWVVF
TNFCLFFYKS HQDSHPLASL PLLGYSLTIP SESENIHKDY VFKLHFKSHV YYFRAESEYT
FERWMEVIRS ATSSASRAHS LSHKESHLY
