FRM4B_MOUSE
ID FRM4B_MOUSE Reviewed; 1035 AA.
AC Q920B0; Q3V1S1; Q920B1; Q9ESP9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=FERM domain-containing protein 4B;
DE AltName: Full=GRP1-binding protein GRSP1;
DE AltName: Full=Golgi-associated band 4.1-like protein;
DE Short=GOBLIN;
GN Name=Frmd4b;
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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM
RP 1/2), INTERACTION WITH CYTH3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Lung;
RX PubMed=11445584; DOI=10.1074/jbc.m105260200;
RA Klarlund J.K., Holik J., Chawla A., Park J.G., Buxton J., Czech M.P.;
RT "Signaling complexes of the FERM domain-containing protein GRSP1 bound to
RT ARF exchange factor GRP1.";
RL J. Biol. Chem. 276:40065-40070(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ICR; TISSUE=Brain;
RA Watanabe N.M., Kusumi A., Dan I.;
RT "Mus musculus mRNA for Golgi-associated band 4.1-like protein, Goblin,
RT complete cds.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH PARD3; CYTH3 AND CYTH1, 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: Member of GRP1 signaling complexes that are acutely recruited
CC to plasma membrane ruffles in response to insulin receptor signaling.
CC May function as a scaffolding protein that regulates epithelial cell
CC polarity by connecting ARF6 activation with the PAR3 complex
CC (PubMed:20080746). Plays a redundant role with FRMD4A in epithelial
CC polarization (PubMed:20080746). {ECO:0000269|PubMed:20080746}.
CC -!- SUBUNIT: Interacts with CYTH3 (PubMed:11445584, PubMed:20080746).
CC Interacts with PARD3 (PubMed:20080746). Interacts with CYTH1.
CC {ECO:0000269|PubMed:11445584, ECO:0000269|PubMed:20080746}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11445584}. Cell junction, tight junction
CC {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:20080746}. Note=Colocalized with PARD3 at adherens
CC junction and tight junction (PubMed:20080746).
CC {ECO:0000269|PubMed:20080746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q920B0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q920B0-2; Sequence=VSP_040896;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the brain. Isoform 2 is
CC expressed in the lung (at protein level).
CC {ECO:0000269|PubMed:11445584}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL26916.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF327856; AAL26916.1; ALT_INIT; mRNA.
DR EMBL; AF327857; AAL26917.1; -; mRNA.
DR EMBL; AB042027; BAB17031.1; -; mRNA.
DR EMBL; AK132280; BAE21079.1; -; mRNA.
DR EMBL; BC052390; AAH52390.1; -; mRNA.
DR CCDS; CCDS39577.1; -. [Q920B0-2]
DR CCDS; CCDS85102.1; -. [Q920B0-1]
DR RefSeq; NP_001333566.1; NM_001346637.1. [Q920B0-1]
DR RefSeq; NP_001333568.1; NM_001346639.1.
DR RefSeq; NP_660130.2; NM_145148.2. [Q920B0-2]
DR RefSeq; XP_017177026.1; XM_017321537.1. [Q920B0-2]
DR AlphaFoldDB; Q920B0; -.
DR SMR; Q920B0; -.
DR BioGRID; 231236; 2.
DR STRING; 10090.ENSMUSP00000108982; -.
DR iPTMnet; Q920B0; -.
DR PhosphoSitePlus; Q920B0; -.
DR EPD; Q920B0; -.
DR MaxQB; Q920B0; -.
DR PaxDb; Q920B0; -.
DR PRIDE; Q920B0; -.
DR ProteomicsDB; 267627; -. [Q920B0-1]
DR ProteomicsDB; 267628; -. [Q920B0-2]
DR Antibodypedia; 2768; 44 antibodies from 9 providers.
DR DNASU; 232288; -.
DR Ensembl; ENSMUST00000032146; ENSMUSP00000032146; ENSMUSG00000030064. [Q920B0-1]
DR Ensembl; ENSMUST00000113355; ENSMUSP00000108982; ENSMUSG00000030064. [Q920B0-2]
DR GeneID; 232288; -.
DR KEGG; mmu:232288; -.
DR UCSC; uc009dat.1; mouse. [Q920B0-1]
DR CTD; 23150; -.
DR MGI; MGI:2141794; Frmd4b.
DR VEuPathDB; HostDB:ENSMUSG00000030064; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01020000230354; -.
DR HOGENOM; CLU_003623_2_0_1; -.
DR InParanoid; Q920B0; -.
DR OrthoDB; 125121at2759; -.
DR PhylomeDB; Q920B0; -.
DR TreeFam; TF328984; -.
DR BioGRID-ORCS; 232288; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Frmd4b; mouse.
DR PRO; PR:Q920B0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q920B0; protein.
DR Bgee; ENSMUSG00000030064; Expressed in indifferent gonad and 245 other tissues.
DR ExpressionAtlas; Q920B0; baseline and differential.
DR Genevisible; Q920B0; MM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IPI:MGI.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IGI: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; 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 Isopeptide bond; Phosphoprotein; Reference proteome; Tight junction;
KW Ubl conjugation.
FT CHAIN 1..1035
FT /note="FERM domain-containing protein 4B"
FT /id="PRO_0000219447"
FT DOMAIN 59..361
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 542..972
FT /note="Necessary for adherens junction and tight junction
FT localization"
FT /evidence="ECO:0000269|PubMed:20080746"
FT REGION 563..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..451
FT /evidence="ECO:0000255"
FT COILED 535..559
FT /evidence="ECO:0000255"
FT COMPBIAS 577..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L6"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L6"
FT CROSSLNK 883
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L6"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2L6"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_040896"
FT CONFLICT 62
FT /note="Q -> R (in Ref. 2; BAB17031)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="D -> G (in Ref. 3; BAE21079)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="P -> S (in Ref. 2; BAB17031)"
FT /evidence="ECO:0000305"
FT CONFLICT 917..918
FT /note="PQ -> TK (in Ref. 2; BAB17031)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="S -> N (in Ref. 2; BAB17031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1035 AA; 118007 MW; 5CA90A96E3F3368A CRC64;
MASVFMCGVE DLLFSGSRFV WNLTVSTLRR WYTERLRACH QVLRTWCGLR DVYQMTEGRH
CQVHLLDDRR LELLVQPKLL SRELLDLVAS HFNLKEKEYF GITFIDDTGQ ENWLQLDHRV
LEHDLPKKPG PTLLHFAVRF YIESISFLKD KNTVELFFLN AKACVHKGQI EVDSETIFKL
AALVLQESKG DYTSDENARK DLKTLPVFPT KTLQEHPSLA YCEDRVIEHY LKIKGLTRGQ
AVVQYMKIVE ALPTYGVHYY AVKDKQGLPW WLGISYKGIG QYDLQDKVKP RKLFQWKQLE
NLYFREKKFA VEVHDPRRIS VSRRTFGQSG LFVQTWYANS SLIKSIWVMA ISQHQFYLDR
KQSKAKIPSA RSLDDIAMDL TETGTQRGSK LVTLEAKSQF IMASNGSLIS SGSQDSEGME
EQKREKILEL KKKEKLLQEK LLQKVEELKK ICLREAELTG RMPKEYPLNI GEKPPQVRRR
VGTTFKLDDN LLPTEEDPAL QELESNFLIQ QKLVEAAKKL ASEPDLCKTV KKKRKQDYTD
AVKRLQEIEN SINEYRIRCG KKPSQKAAVV PPEDIIPSES SSLSDTTTYD DPNDSFTLAG
QRPSSVPHSP RILPPKSLGI ERIHFRKSSI NEQFMDTRHS REMLSTHSSP YKTLERRPQG
GRSMPTTPVL TRNAYSSSHL EPDSSSQHCR QRSGSLESQS HLLSEMDSDK PFFTLSKSQR
SSSTEILDDG SSYTSQSSSE YYCVTPAASP YYTTQTLDTR ARGRRRSKKH SVSTSNSGSM
PNLAQKDPLR NGVYSKGQDP PPSGYYIAGY PPYAECDLYY SGGYVYENDT EGQYSVNPSY
RSSAHYGYDR QRDYSRSFHE DEVDRVPHNP YATLRLPRKA AVKSEHITKN IHKALVAEHL
RGWYQRASGQ KDQGHSPQTS FDSDRGSQRC LGFAGLQVPC SPSSRASSYS SVSSTNASGN
WRTQLTIGLS EYENPVHSPY TSYYGSIYNP LSSPSRQYAE TTPLDGTDGS QLEDNLEGSE
QRLFWHEDSK PGTLV
