FRMD5_MOUSE
ID FRMD5_MOUSE Reviewed; 517 AA.
AC Q6P5H6; B0R0I9; Q6PFH6; Q8C0K0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=FERM domain-containing protein 5;
GN Name=Frmd5;
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] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in regulation of cell migration. May regulate
CC cell-matrix interactions via its interaction with ITGB5 and modifying
CC ITGB5 cytoplasmic tail interactions such as with FERMT2 and TLN1. May
CC regulate ROCK1 kinase activity possibly involved in regulation of actin
CC stress fiber formation. {ECO:0000250|UniProtKB:Q7Z6J6}.
CC -!- SUBUNIT: Interacts with CTNND1, ITGB5 (via cytoplasmic domain) and
CC ROCK1. {ECO:0000250|UniProtKB:Q7Z6J6}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q7Z6J6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P5H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5H6-2; Sequence=VSP_019983, VSP_019984;
CC Name=3;
CC IsoId=Q6P5H6-3; Sequence=VSP_019983, VSP_019985;
CC Name=4;
CC IsoId=Q6P5H6-4; Sequence=VSP_019983, VSP_019986;
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DR EMBL; AK030883; BAC27170.1; -; mRNA.
DR EMBL; AL928678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057549; AAH57549.1; -; mRNA.
DR EMBL; BC062889; AAH62889.1; -; mRNA.
DR CCDS; CCDS16649.1; -. [Q6P5H6-1]
DR RefSeq; NP_766261.2; NM_172673.3. [Q6P5H6-1]
DR AlphaFoldDB; Q6P5H6; -.
DR SMR; Q6P5H6; -.
DR BioGRID; 230742; 5.
DR STRING; 10090.ENSMUSP00000115136; -.
DR iPTMnet; Q6P5H6; -.
DR PhosphoSitePlus; Q6P5H6; -.
DR MaxQB; Q6P5H6; -.
DR PaxDb; Q6P5H6; -.
DR PeptideAtlas; Q6P5H6; -.
DR PRIDE; Q6P5H6; -.
DR ProteomicsDB; 267521; -. [Q6P5H6-1]
DR ProteomicsDB; 267522; -. [Q6P5H6-2]
DR ProteomicsDB; 267523; -. [Q6P5H6-3]
DR ProteomicsDB; 267524; -. [Q6P5H6-4]
DR Antibodypedia; 2633; 98 antibodies from 16 providers.
DR DNASU; 228564; -.
DR Ensembl; ENSMUST00000121219; ENSMUSP00000113568; ENSMUSG00000027238. [Q6P5H6-2]
DR Ensembl; ENSMUST00000138157; ENSMUSP00000115136; ENSMUSG00000027238. [Q6P5H6-1]
DR GeneID; 228564; -.
DR KEGG; mmu:228564; -.
DR UCSC; uc008lzk.1; mouse. [Q6P5H6-1]
DR UCSC; uc008lzm.1; mouse. [Q6P5H6-2]
DR CTD; 84978; -.
DR MGI; MGI:2442557; Frmd5.
DR VEuPathDB; HostDB:ENSMUSG00000027238; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000156346; -.
DR InParanoid; Q6P5H6; -.
DR OMA; EXLEKSS; -.
DR OrthoDB; 484046at2759; -.
DR PhylomeDB; Q6P5H6; -.
DR TreeFam; TF343477; -.
DR BioGRID-ORCS; 228564; 2 hits in 61 CRISPR screens.
DR ChiTaRS; Frmd5; mouse.
DR PRO; PR:Q6P5H6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6P5H6; protein.
DR Bgee; ENSMUSG00000027238; Expressed in cardiac muscle of left ventricle and 185 other tissues.
DR ExpressionAtlas; Q6P5H6; baseline and differential.
DR Genevisible; Q6P5H6; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
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; 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 PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Phosphoprotein; Reference proteome.
FT CHAIN 1..517
FT /note="FERM domain-containing protein 5"
FT /id="PRO_0000247447"
FT DOMAIN 17..298
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 308..353
FT /note="Interaction with ROCK1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J6"
FT REGION 344..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019983"
FT VAR_SEQ 494..517
FT /note="RVHLKGPQLQQQQWKGWGKSVPLD -> VNKFVLSVLRLLLVTMGLLFVLLL
FT LLIILTESDLDVAFFRDIRQTPEFEQFHYQYFCPLRRWFACKIRSVVSLLIDT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019984"
FT VAR_SEQ 494..517
FT /note="RVHLKGPQLQQQQWKGWGKSVPLD -> MQERDRSEEGIEKEQRPWKGPGST
FT KQDL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019985"
FT VAR_SEQ 494..517
FT /note="RVHLKGPQLQQQQWKGWGKSVPLD -> AMVCLQNPLSGEPAN (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019986"
SQ SEQUENCE 517 AA; 58583 MW; 064722C4016B4BD5 CRC64;
MLSRLMSGSS RSLEREYSCT VRLLDDSEYT CTIQRDAKGQ YLFDLLCHHL NLLEKDYFGI
RFVDPDKQRH WLEFTKSVVK QLRSQPPFTM CFRVKFYPAD PAALKEEITR YLVFLQIKRD
LYHGRLLCKT SDAALLAAYI LQAEIGDYDP GKHPEGYSSK FQFFPKHSEK LEKKIAEIHK
TELSGQTPAT SELNFLRKAQ TLETYGVDPH PCKDVSGNAA FLAFTPFGFV VLQGNKRVHF
IKWNEVTKLK FEGKTFYLYV SQKEEKKIIL TYFAPTPEAC KHLWKCGIEN QAFYKLEKSS
QVRTVSSSNL FFKGSRFRYS GRVAKEVMES SAKIKREPPE IHRAGMVPSR SCPSITHGPR
LSSVPRTRRR AVHISIMEGL ESLRDSAHST PVRSSSHGDT FLPHVRSSRA DSNERVAVIA
DEAYSPADSV LPTPVAEHSL ELMLLSRQIN GATCSIEEEK ESEASTPTAT EAEALGGELR
ALCQGHGGSE QEQRVHLKGP QLQQQQWKGW GKSVPLD
