FARP1_CHICK
ID FARP1_CHICK Reviewed; 1046 AA.
AC F1P065;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 63.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-57.
RC TISSUE=Chondrocyte;
RA Boardman P.E., Bonfield J.K., Brown W.R.A., Carder C., Chalk S.E.,
RA Croning M.D.R., Davies R.M., Francis M.D., Grafham D.V., Hubbard S.J.,
RA Humphray S.J., Hunt P.J., Maddison M., McLaren S.R., Niblett D.,
RA Overton I.M., Rogers J., Scott C.E., Taylor R.G., Tickle C., Wilson S.A.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH PLXNA4, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=19217374; DOI=10.1016/j.neuron.2008.12.022;
RA Zhuang B., Su Y.S., Sockanathan S.;
RT "FARP1 promotes the dendritic growth of spinal motor neuron subtypes
RT through transmembrane Semaphorin6A and PlexinA4 signaling.";
RL Neuron 61:359-372(2009).
CC -!- FUNCTION: Functions as guanine nucleotide exchange factor for RAC1 (By
CC similarity). Plays a role in semaphorin signaling via its interaction
CC with PLXNA4. Plays a role in the assembly and disassembly of dendritic
CC filopodia, the formation of dendritic spines, regulation of dendrite
CC length and ultimately the formation of synapses. {ECO:0000250,
CC ECO:0000269|PubMed:19217374}.
CC -!- SUBUNIT: Interacts with PLXNA4. {ECO:0000269|PubMed:19217374}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Synapse
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19217374}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:19217374}.
CC Cell projection, dendritic spine {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in lateral motor column motor neurons and
CC in preganglionic autonomic motor neurons of the column of Terni in the
CC embryonic spinal cord (at protein level).
CC {ECO:0000269|PubMed:19217374}.
CC -!- INDUCTION: Up-regulated by retinol. {ECO:0000269|PubMed:19217374}.
CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC domains can stabilize the protein in an autoinhibited conformation.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AADN02029275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02029276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02029277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02029278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02029279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR353349; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; F1P065; -.
DR SMR; F1P065; -.
DR STRING; 9031.ENSGALP00000027234; -.
DR PaxDb; F1P065; -.
DR VEuPathDB; HostDB:geneid_418781; -.
DR eggNOG; KOG3531; Eukaryota.
DR InParanoid; F1P065; -.
DR OrthoDB; 476668at2759; -.
DR TreeFam; TF351276; -.
DR Proteomes; UP000000539; Unplaced.
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:0030175; C:filopodium; IEA:UniProtKB-SubCell.
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:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
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; Reference proteome; Repeat;
KW Synapse; Synaptosome.
FT CHAIN 1..1046
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 1"
FT /id="PRO_0000422338"
FT DOMAIN 40..320
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 541..732
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 761..858
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 933..1030
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 374..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1046 AA; 119705 MW; 1F6B075309DE9D4E CRC64;
MGETEQRPTA GSRLGAQENA GISTLEHGQK PPLTPPGKLI SIKIQMLDDT QETFEVPQRA
PGKVLHDAVC NHLNLVEGDY FGLEFPDHKK MMVWLDLLKP VMKQIRRPKH VVVKFVVKFF
PPDHAQLQEE LTRYLFALQV KQDLAQGRLT CNDTSTALLI SHIVQSEIGD FDETIDREHL
AKNKYIPQQE ALEDKIMEFH RKHTGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI
NLAVANTGIL VFQGHTKINA FNWAKVRKLS FKRKRFLIKL RPDVNSSFQD TLEFLMASRD
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
FERKHSKIRS IRSLTAQPSE QHAEVPKQSF QSSSFAYGDD SDAAAVQSCQ QGKELKASTE
DTGQHKSPSL KKSPKEGRKV DGAVVSAVEE EEEAATDRMQ QNRPQSQQPS TAGSLTGSPH
LSELSINSQG GPSVANMSLS PNLSPDAKQS SPLISPLLND PSCIRTEEEE EVKKKRFPTE
KAYFIAKEVA TTERTYLKDL EVITSWFQSA VSKEDCMPET LKNLIFSNFE PLHKFHTGFL
KEIEQRLALW EGRSNAHIKG GHQRIGDVML KNIQGMKQLT IHLWKHNEIL TELENGIKNS
RKLETFCRDF ELQKVCYLPL NTFLLRPLHR LMHYKQIMER LCKHYPPNHV DFRDSRAALA
EITEMMAQLH GNMIKMENFQ KLHELKKDLI GIDNLVIPGR EFIRLGSLSK LSGKGLQQRM
FFLFNDILLY TSRGLTASNQ FKVHGHLPLY GMTIEDSEEE WGVPHCLTLR GQQQSIIVAA
STRAEIDKWI EDIQMAIDLA EKSSDPVPEL LASSPPDNKS PDETTVDQES EDDLSASRTS
LERQSPHRGN TTVHVCWHRN TSVSMIDFSI AVENQLSGNL LRKFKNSNGW QKLWVVFTNF
CMFFYKSHQD NHPLASLPLL GYSLTIPSES ENIHKDYVFK LHFKSHVYYF RAESEYTFER
WMEVIRSATS SALRTRALSH REPHTY
