FRM4A_MOUSE
ID FRM4A_MOUSE Reviewed; 1020 AA.
AC Q8BIE6; B1AXK1; B1AXK2; Q6PDJ4; Q8CHA6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=FERM domain-containing protein 4A;
GN Name=Frmd4a; Synonyms=Frmd4, Kiaa1294;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-1020 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Spleen;
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 [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH CYTH1; CYTH2; CYTH3 AND PARD3, AND
RP FUNCTION.
RX PubMed=20080746; DOI=10.1073/pnas.0908423107;
RA Ikenouchi J., Umeda M.;
RT "FRMD4A regulates epithelial polarity by connecting Arf6 activation with
RT the PAR complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:748-753(2010).
CC -!- FUNCTION: Scaffolding protein that regulates epithelial cell polarity
CC by connecting ARF6 activation with the PAR3 complex (PubMed:20080746).
CC Plays a redundant role with FRMD4B in epithelial polarization
CC (PubMed:20080746). May regulate MAPT secretion by activating ARF6-
CC signaling (By similarity). {ECO:0000250|UniProtKB:Q9P2Q2,
CC ECO:0000269|PubMed:20080746}.
CC -!- SUBUNIT: Interacts (via coiled-coil domain) with CYTH1 (via coiled-coil
CC domain) (PubMed:20080746). Interacts with PARD3 (via coiled-coil
CC domain) (PubMed:20080746). Found in a complex with PARD3, CYTH1 and
CC FRMD4A (PubMed:20080746). Interacts with CYTH2 (PubMed:20080746).
CC Interacts with CYTH3 (PubMed:20080746). {ECO:0000269|PubMed:20080746}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell
CC junction, tight junction {ECO:0000269|PubMed:20080746}.
CC Note=Colocalized with CYTH1 at adherens junction and tight junction
CC (PubMed:20080746). Colocalized with PARD3 during the process of
CC epithelial polarization (PubMed:20080746).
CC {ECO:0000269|PubMed:20080746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BIE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BIE6-2; Sequence=VSP_035378, VSP_019592;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM46015.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM46271.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK082365; BAC38478.1; -; mRNA.
DR EMBL; AL807832; CAM46014.1; -; Genomic_DNA.
DR EMBL; AL928947; CAM46014.1; JOINED; Genomic_DNA.
DR EMBL; AL807832; CAM46015.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL928947; CAM46015.1; JOINED; Genomic_DNA.
DR EMBL; AL928947; CAM46270.1; -; Genomic_DNA.
DR EMBL; AL807832; CAM46270.1; JOINED; Genomic_DNA.
DR EMBL; AL928947; CAM46271.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL807832; CAM46271.1; JOINED; Genomic_DNA.
DR EMBL; BC058672; AAH58672.1; ALT_INIT; mRNA.
DR EMBL; AB093292; BAC41475.1; -; mRNA.
DR CCDS; CCDS15656.2; -. [Q8BIE6-2]
DR CCDS; CCDS50488.1; -. [Q8BIE6-1]
DR RefSeq; NP_001171314.1; NM_001177843.1. [Q8BIE6-1]
DR RefSeq; NP_766063.3; NM_172475.3. [Q8BIE6-2]
DR RefSeq; XP_006497503.1; XM_006497440.1.
DR RefSeq; XP_006497504.1; XM_006497441.1.
DR RefSeq; XP_006497505.1; XM_006497442.2.
DR AlphaFoldDB; Q8BIE6; -.
DR SMR; Q8BIE6; -.
DR BioGRID; 229099; 3.
DR IntAct; Q8BIE6; 1.
DR MINT; Q8BIE6; -.
DR STRING; 10090.ENSMUSP00000075172; -.
DR iPTMnet; Q8BIE6; -.
DR PhosphoSitePlus; Q8BIE6; -.
DR jPOST; Q8BIE6; -.
DR MaxQB; Q8BIE6; -.
DR PaxDb; Q8BIE6; -.
DR PRIDE; Q8BIE6; -.
DR ProteomicsDB; 271803; -. [Q8BIE6-1]
DR ProteomicsDB; 271804; -. [Q8BIE6-2]
DR Antibodypedia; 50861; 44 antibodies from 9 providers.
DR DNASU; 209630; -.
DR Ensembl; ENSMUST00000075767; ENSMUSP00000075172; ENSMUSG00000026657. [Q8BIE6-1]
DR Ensembl; ENSMUST00000091497; ENSMUSP00000089079; ENSMUSG00000026657. [Q8BIE6-2]
DR GeneID; 209630; -.
DR KEGG; mmu:209630; -.
DR UCSC; uc008ieo.2; mouse. [Q8BIE6-2]
DR UCSC; uc008ies.2; mouse. [Q8BIE6-1]
DR CTD; 55691; -.
DR MGI; MGI:1919850; Frmd4a.
DR VEuPathDB; HostDB:ENSMUSG00000026657; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01020000230354; -.
DR HOGENOM; CLU_003623_2_0_1; -.
DR InParanoid; Q8BIE6; -.
DR OMA; XSQESDS; -.
DR OrthoDB; 125121at2759; -.
DR PhylomeDB; Q8BIE6; -.
DR TreeFam; TF328984; -.
DR BioGRID-ORCS; 209630; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Frmd4a; mouse.
DR PRO; PR:Q8BIE6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BIE6; protein.
DR Bgee; ENSMUSG00000026657; Expressed in manus and 229 other tissues.
DR ExpressionAtlas; Q8BIE6; baseline and differential.
DR Genevisible; Q8BIE6; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:MGI.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IGI:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13191; FERM_C_FRMD4A_FRMD4B; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021774; DUF3338.
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; IPR041785; FRMD4A/B_FERM_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11819; CUPID; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR SMART; SM00295; B41; 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; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..1020
FT /note="FERM domain-containing protein 4A"
FT /id="PRO_0000219445"
FT DOMAIN 5..307
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 343..405
FT /note="Necessary for interaction with CYTH1"
FT /evidence="ECO:0000269|PubMed:20080746"
FT REGION 351..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..920
FT /note="Necessary for tight junction and adherens junction
FT localization; Requires for interaction with PARD3"
FT /evidence="ECO:0000269|PubMed:20080746"
FT REGION 698..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 367..401
FT /evidence="ECO:0000255"
FT COMPBIAS 538..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Q2"
FT VAR_SEQ 1
FT /note="M -> MEGLLSPMRTKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035378"
FT VAR_SEQ 999..1020
FT /note="EATENSPIMDGSESPTHQSTDE -> SYSDSCFLDSSLYPELADVQWYGQEK
FT AKPGTLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019592"
FT CONFLICT 758
FT /note="E -> G (in Ref. 1; BAC38478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 113879 MW; 68E4E578FB91BF45 CRC64;
MTEGRRCQVH LLDDRKLELL VQPKLLAKEL LDLVASHFNL KEKEYFGIAF TDETGHLNWL
QLDRRVLEHD FPKKSGPVVL YFCVRFYIES ISYLKDNATI ELFFLNAKSC IYKELIDVDS
EVVFELASYI LQEAKGDFSS NEVVRSDLKK LPALPTQALK EHPSLAYCED RVIEYYKKLN
GQTRGQAIVN YMSIVESLPT YGVHYYAVKD KQGIPWWLGL SYKGIFQYDY HDKVKPRKIF
QWRQLENLYF REKKFSVEVH DPRRASVTRR TFGHSGIAVH TWYACPALIK SIWAMAISQH
QFYLDRKQSK SKIHAARSLS EIAIDLTETG TLKTSKLANM GSKGKIISGS SGSLLSSGSQ
ESDSSQSAKK DMLAALKSRQ EALEETLRQR LEELKRLCLR EAELTGKLPV EYPLDPGEEP
PIVRRRIGTA FKLDEQKILP KGEEAELERL EREFAIQSQI TEAARRLASD PNVSKKLKKQ
RKTSYLNALK KLQEIENAIN ENRIKSGKKP TQRASLVIDD GNIASEDSSL SDALVLEDED
SQVTSTISPL QSPHKGLPPR PPSSHNRPPP PQSLEGLRQL HYHRTDYDKS PLKPKMWSES
SLDEPYEKVK KRSSHGHSSS HKRFPSTGSC TEAGVSSSLQ NSPIRSLPHW NSQSSMPSTP
DLRVRSPHYV HSTRSVDISP TRLHSLALHF RHRSSSLESQ GKLLGSENDT GSPDFYTPRT
RSSNGSDPMD DCSSCTSHSS SEHYYPAQMN ANYSTLAEDS PSKARQRQRQ RQRAAGALGS
ASSGSMPNLA ARSGAASTGG GVYLHSQSQP SSQYRIKEYP LYIEGSATPV VVRSLESDQE
GHYSVKAQFK TSNSYTAGGL FKESWRGGGD EGDAGRLTPS RSQILRTPSL GRDGAHDKGS
GRAAVSDELR QWYQRSTASH KEHSRLSHTS STSSDSGSQY STSSQSTFVA HSRVTRMPQM
CKATSAALPQ SQRSSTPSSE IGATPPSSPH HILTWQTGEA TENSPIMDGS ESPTHQSTDE
