ID D3ZFK8_RAT Unreviewed; 1060 AA.
AC D3ZFK8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=FERM, ARH/RhoGEF and pleckstrin domain protein 2 {ECO:0000313|Ensembl:ENSRNOP00000024440.5};
GN Name=Farp2 {ECO:0000313|Ensembl:ENSRNOP00000024440.5,
GN ECO:0000313|RGD:1308003};
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 {ECO:0000313|Ensembl:ENSRNOP00000024440.5, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000024440.5, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024440.5,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
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] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
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).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000024440.5}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024440.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_001101703.1; NM_001108233.1.
DR RefSeq; XP_006245594.1; XM_006245532.3.
DR AlphaFoldDB; D3ZFK8; -.
DR SMR; D3ZFK8; -.
DR STRING; 10116.ENSRNOP00000024440; -.
DR PhosphoSitePlus; D3ZFK8; -.
DR PaxDb; 10116-ENSRNOP00000024440; -.
DR Ensembl; ENSRNOT00000024440.6; ENSRNOP00000024440.5; ENSRNOG00000018051.6.
DR GeneID; 316639; -.
DR KEGG; rno:316639; -.
DR UCSC; RGD:1308003; rat.
DR AGR; RGD:1308003; -.
DR CTD; 9855; -.
DR RGD; 1308003; Farp2.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000158642; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR OMA; HKHMPED; -.
DR OrthoDB; 2876516at2759; -.
DR TreeFam; TF351276; -.
DR Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018051; Expressed in liver and 20 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0022405; P:hair cycle process; ISO:RGD.
DR GO; GO:0016322; P:neuron remodeling; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0071800; P:podosome assembly; ISO:RGD.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:RGD.
DR GO; GO:0033623; P:regulation of integrin activation; ISO:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISO:RGD.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd17190; FERM_F1_FARP2; 1.
DR CDD; cd01220; PH1_FARP1-like; 1.
DR CDD; cd13235; PH2_FARP1-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR014847; FA.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
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 PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45858:SF4; FERM, ARHGEF AND PLECKSTRIN DOMAIN-CONTAINING PROTEIN 2; 1.
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; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 3.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ SEQUENCE 1060 AA; 120801 MW; 1E757C3D7C4DB75C CRC64;
MGEIEGTYRT LPTSGTRLGG QTAIGVSTLE PEQALSPKMQ EKHMHIRVKL LDSTVEIFDI
EPKCDGQVLL TQVWKHLNLI ECDYFGLEFK NVQSYWIWLE PMKPIIRQVR KPKNAVLRLA
VKFFPPDPGQ LQEEYTRYLF ALQLRRDLLE ERLTCTATTS ALLISHLLQS EIGDYDETLD
REHLKANDYL PNQEQSLDKI LDFHQRHTGQ TPADSDFQVL EIARKLEMYG IRFHMASDRE
GTKINLAVSH MGVLVFQGTT KINTFNWSKV RKLSFKRKRF LIKLHPEVHG PYQDTLEFLL
GSRDECKNFW KICVEHHTFF RLSDQPKPKA KAVFFSRGSS FRYSGRTQKQ LVDYIRDGGT
KRIPYERRHS KTRTSLHTLT GDLPKQSISF TDGLRTSASL SSANASFYPP PTSLSSPGLP
SVKDSSSSPV DPQAPHIKST AAERSSRPSS SEGPSTQSAH LPGPPVLQPG PGFSVDSPQP
SPSSLKSRLS LSPERQASLS TAEQGSSPVL SPVLSGTGTA RMDNQEEQKH KHTSEDEAYF
IAKEIVATER TYLKDLEVIT VWFRSVVIKE EAMPAALMTL LFSNIDPIYE FHRGFLHEVE
QRLALWEGPS SGDHQRIGDI LLRNMRQLKE FTSYFQRHDE VLTELEKATK HCKRLEAVYK
EFELQKVCYL PLNTFLLKPV QRLVHYRLLL NRLCTHYSPE HEDYTDCHEA LKAITEVTTE
LQQSLTRLEN LQKLTELQRD LVGVENLIAP GREFIREGCL HKLTKKGLQQ RMFFLFSDML
LYTSKSVTGA SQFRIRGFLP LRGMLVEDSE NEWSVPHCFT IYAAQKTIVV AASTRLEKEK
WMQDLNAAIQ AAKSAGDTPA VLLGGPVYTR SPRSSDEVSL EDSEDGRGTR GSLEGNSQHR
ANTTMHVCWY RNTSVSRADH SAAVENQLSG YLLRKFKNSN GWQKLWVVFT NFCLFFYKTH
QDDYPLASLP LLGYSVSLPR EADSIHKDYV FKLQFKSHVY FFRAESKYTF ERWMEVIKRA
SSSPGRPPSF TQDCSHLSPG LEAEVREKEA CPSLCLDKNL
//
