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FRMD7_MOUSE
ID   FRMD7_MOUSE             Reviewed;         703 AA.
AC   A2AD83; Q8CCP8;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=FERM domain-containing protein 7;
GN   Name=Frmd7 {ECO:0000312|MGI:MGI:2686379};
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] {ECO:0000312|EMBL:CAM15767.1}
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   [2] {ECO:0000305, ECO:0000312|EMBL:BAC27826.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-703.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC27826.1};
RC   TISSUE=Olfactory bulb {ECO:0000312|EMBL:BAC27826.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:AAI47258.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-703.
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI47258.1};
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] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19892780; DOI=10.1093/hmg/ddp500;
RA   Betts-Henderson J., Bartesaghi S., Crosier M., Lindsay S., Chen H.L.,
RA   Salomoni P., Gottlob I., Nicotera P.;
RT   "The nystagmus-associated FRMD7 gene regulates neuronal outgrowth and
RT   development.";
RL   Hum. Mol. Genet. 19:342-351(2010).
CC   -!- FUNCTION: Plays a role in neurite development, may be through the
CC       activation of the GTPase RAC1. Plays a role in the control of eye
CC       movement and gaze stability. {ECO:0000250|UniProtKB:Q6ZUT3,
CC       ECO:0000269|PubMed:19892780}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, neuron projection
CC       {ECO:0000269|PubMed:19892780}. Cell projection, growth cone
CC       {ECO:0000269|PubMed:19892780}. Note=In undifferentiated neurons,
CC       located in the actin-rich regions of the cell body. In differentiated
CC       neurons, located in the actin-rich regions of the cell body and primary
CC       neurite processes but is almost absent from secondary extensions
CC       arising from the primary neurite. Also found at the actin-rich distal
CC       end of growth cones. {ECO:0000269|PubMed:19892780}.
CC   -!- TISSUE SPECIFICITY: In the developing cerebral cortex, strong
CC       expression is observed in the ventricular and intermediate zones at 13
CC       and 17 dpc. At 17 dpc and P0, expression appears to be restricted to
CC       the cortical plate. In neonates, highly expressed in cortex,
CC       hippocampus, cerebellum, olfactory bulb and eye with little or no
CC       expression in liver, kidney, skeletal muscle or heart muscle (at
CC       protein level). {ECO:0000269|PubMed:19892780}.
CC   -!- INDUCTION: Up-regulated during retinoic acid-induced differentiation of
CC       neuroblastoma cells. {ECO:0000269|PubMed:19892780}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI47258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI47259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC27826.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL670230; CAM15767.1; -; Genomic_DNA.
DR   EMBL; AK032347; BAC27826.1; ALT_INIT; mRNA.
DR   EMBL; BC147257; AAI47258.1; ALT_INIT; mRNA.
DR   EMBL; BC147258; AAI47259.1; ALT_INIT; mRNA.
DR   CCDS; CCDS53067.1; -.
DR   RefSeq; NP_001177261.1; NM_001190332.1.
DR   RefSeq; XP_006541568.1; XM_006541505.3.
DR   RefSeq; XP_006541569.1; XM_006541506.3.
DR   AlphaFoldDB; A2AD83; -.
DR   SMR; A2AD83; -.
DR   STRING; 10090.ENSMUSP00000057103; -.
DR   iPTMnet; A2AD83; -.
DR   PhosphoSitePlus; A2AD83; -.
DR   PaxDb; A2AD83; -.
DR   PRIDE; A2AD83; -.
DR   ProteomicsDB; 271808; -.
DR   Antibodypedia; 430; 107 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000060650; ENSMUSP00000057103; ENSMUSG00000036131.
DR   GeneID; 385354; -.
DR   KEGG; mmu:385354; -.
DR   UCSC; uc012hgz.1; mouse.
DR   CTD; 90167; -.
DR   MGI; MGI:2686379; Frmd7.
DR   VEuPathDB; HostDB:ENSMUSG00000036131; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   eggNOG; KOG3531; Eukaryota.
DR   GeneTree; ENSGT00940000158972; -.
DR   HOGENOM; CLU_030239_0_0_1; -.
DR   InParanoid; A2AD83; -.
DR   OMA; ERPDSCL; -.
DR   OrthoDB; 476668at2759; -.
DR   PhylomeDB; A2AD83; -.
DR   TreeFam; TF317513; -.
DR   BioGRID-ORCS; 385354; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Frmd7; mouse.
DR   PRO; PR:A2AD83; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2AD83; protein.
DR   Bgee; ENSMUSG00000036131; Expressed in olfactory bulb and 25 other tissues.
DR   ExpressionAtlas; A2AD83; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:MGI.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IGI:MGI.
DR   GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13193; FERM_C_FARP1-like; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
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; 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   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   Cell projection; Coiled coil; Neurogenesis; Reference proteome.
FT   CHAIN           1..703
FT                   /note="FERM domain-containing protein 7"
FT                   /id="PRO_0000391462"
FT   DOMAIN          2..282
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   COILED          525..552
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   703 AA;  80330 MW;  4D964A61B041F0C0 CRC64;
     MLHLKVQFLD DSQKIFVVDQ KSSGKALFNL SCGHLNLAEK EYFGLEFCSH SGNNVWLELL
     KPITKQVKNP KEVVFKFMVK FFPVDPGHLR EELTRYLFTL QIKKDLALGR LPCSDNCTAL
     MVSHILQSEL GDFHEETVRK HLVQTQYLPS QASLESKIMQ FHQQHIGRSP AESDILLLDI
     ARKLDMYGIR PQPASDGEGM QIHLAVAHMG VLVLRGNTKI NTFNWAKIRK LSFKRKHFLI
     KLHANILVLC KDTLEFTMAS RDACKAFWKT CVEYHAFFRL SEEPKSKPKT LLCSKGSSFR
     YSGRTQRQLL EYGKKGRLKS LPFERKQYPS QYHERQCRSS PDILSDVSKQ VEDLRLTYGS
     SYYRNVNGVH ASESMLDSRR RNSAVEVTFA AELEHSKPEA EATSLHPSQS SSSFTFIYAD
     PVFNTDPEPI EFFEERSPLS SFQTTSKFAD SHTSKASPAR QLTYTDVPYI PCTSQKVDIM
     PPQVFFYVDK PPQVPRRSLI MAEENMRPDS YVDHSAIKPA KRSPRNMRIK SLQQDLQELQ
     EAMARTSGRS NINVEPEEED PHLDDAFAYN LQEQTPKRSQ SQSDMKTIRF PFGSEFRPLG
     PCPALTRKTD LFACTFAEQE FPTVLIDQSS AERYVASESS DSESEIIKPD YYFLYGKGTK
     SPRARIRLSS GSLQLEEEDE TISFATPGAE DRTLLKPCNY FLA
 
 
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