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Database: UniProt
Entry: A0A2Y9F760_PHYMC
LinkDB: A0A2Y9F760_PHYMC
Original site: A0A2Y9F760_PHYMC 
ID   A0A2Y9F760_PHYMC        Unreviewed;       621 AA.
AC   A0A2Y9F760;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA-binding protein FXR1 {ECO:0000256|ARBA:ARBA00034847};
GN   Name=FXR1 {ECO:0000313|RefSeq:XP_007116496.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007116496.1};
RN   [1] {ECO:0000313|RefSeq:XP_007116496.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007116496.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm, Cytoplasmic
CC       ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Postsynapse
CC       {ECO:0000256|ARBA:ARBA00034110}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the FMR1 family.
CC       {ECO:0000256|ARBA:ARBA00006633}.
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DR   RefSeq; XP_007116496.1; XM_007116434.3.
DR   AlphaFoldDB; A0A2Y9F760; -.
DR   SMR; A0A2Y9F760; -.
DR   GeneID; 102988926; -.
DR   CTD; 8087; -.
DR   OrthoDB; 2995592at2759; -.
DR   Proteomes; UP000248484; Chromosome 1.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:InterPro.
DR   CDD; cd22504; KH_I_FXR1_rpt1; 1.
DR   CDD; cd22507; KH_I_FXR1_rpt2; 1.
DR   CDD; cd22510; KH_I_FXR1_rpt3; 1.
DR   CDD; cd20472; Tudor_Agenet_FXR1_rpt1; 1.
DR   CDD; cd20475; Tudor_Agenet_FXR1_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR   InterPro; IPR008395; Agenet-like_dom.
DR   InterPro; IPR040148; FMR1.
DR   InterPro; IPR022034; FMR1-like_C_core.
DR   InterPro; IPR040472; FMRP_KH0.
DR   InterPro; IPR032172; FXR1_C1.
DR   InterPro; IPR032177; FXR_C3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR047494; KH_I_FXR1_rpt1.
DR   InterPro; IPR047495; KH_I_FXR1_rpt2.
DR   InterPro; IPR047496; KH_I_FXR1_rpt3.
DR   InterPro; IPR047425; Tudor_Agenet_FXR1_rpt1.
DR   InterPro; IPR047427; Tudor_Agenet_FXR1_rpt2.
DR   InterPro; IPR041560; Tudor_FRM1.
DR   PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR   PANTHER; PTHR10603:SF6; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN 1; 1.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXMRP1_C_core; 2.
DR   Pfam; PF16096; FXR_C1; 1.
DR   Pfam; PF16097; FXR_C3; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF17904; KH_9; 1.
DR   Pfam; PF18336; Tudor_FRX1; 1.
DR   SMART; SM00322; KH; 2.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR   PROSITE; PS51641; AGENET_LIKE; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00117}.
FT   DOMAIN          4..50
FT                   /note="Agenet-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51641"
FT   DOMAIN          63..115
FT                   /note="Agenet-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51641"
FT   REGION          381..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  69749 MW;  1F9A5C4123C67298 CRC64;
     MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
     EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
     VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
     VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
     IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
     GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
     VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS
     DWSLAGEDDR ESRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL
     DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY
     ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDE ISKLQRTPGE
     EKINTLKEEN TQEAAVLNGV S
//
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