ID M7AY24_CHEMY Unreviewed; 1167 AA.
AC M7AY24;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Far upstream element-binding protein 2 {ECO:0000313|EMBL:EMP29649.1};
GN ORFNames=UY3_13248 {ECO:0000313|EMBL:EMP29649.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP29649.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
CC {ECO:0000256|ARBA:ARBA00006840}.
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DR EMBL; KB554793; EMP29649.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AY24; -.
DR STRING; 8469.M7AY24; -.
DR eggNOG; KOG3882; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd22479; KH-I_FUBP2_rpt1; 1.
DR CDD; cd22485; KH-I_FUBP2_rpt3; 1.
DR CDD; cd03156; uroplakin_I_like_LEL; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 4.
DR Gene3D; 1.10.1450.10; Tetraspanin; 2.
DR InterPro; IPR015096; FUBP_C.
DR InterPro; IPR047372; KH-I_FUBP2_rpt1.
DR InterPro; IPR047370; KH-I_FUBP2_rpt3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; TETRASPANIN; 1.
DR PANTHER; PTHR19282:SF216; TETRASPANIN-1; 1.
DR Pfam; PF09005; DUF1897; 1.
DR Pfam; PF00013; KH_1; 4.
DR Pfam; PF00335; Tetraspanin; 2.
DR PRINTS; PR00259; TMFOUR.
DR SMART; SM00322; KH; 4.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 4.
DR SUPFAM; SSF48652; Tetraspanin; 2.
DR PROSITE; PS50084; KH_TYPE_1; 4.
DR PROSITE; PS00421; TM4_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 559..629
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 647..719
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 808..878
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 883..936
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 511..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1056
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 125447 MW; CDA043CF68373A3F CRC64;
MGCFSFLKMM MFVFNGIIFL GGLAVLGIGI WMKVDGGSFV QILGAAAPQL MQLINILGAA
APQLMQLINV GYLCIAVGTF LLLMGFLGCC GAMKESKCML LLFFVIILIL FIAEVTGAVV
VLAFSSMADI FIEHLKTWAV KTLREDYGRQ DDLTAIWDTT MKELKCCGFN NYKDFNSSYF
YQTHSQTYPA GCCLPPKREC LESELDSTKK GCLQEFQTFL SRNGRIVGGV ALGIGVLEKP
FCEQPHWPVF TMAPSRSYYA TLKTVMICFN TIIFVVGCTM VALGLWIKLG STSFVRVLGS
TSVNFVHIGY FCIVVGIMVA MLGFIGCWGA VKESRCLLRM YFLIMLVIFI AEITAAVVVF
AFTQFARSVI LDKSLTALKK KYSGYKHDDI VSYGWNAFML KLNCCGVHNY TDFSGSAFQI
RTNLTYPKSC CKDPMSSACN GHNVSSVVIN QEGCFHKLVS LVKEKSLLLG GAATGAALLE
VPVVVSAPVE QNPKLELQQI AAKIGGDAAT TVNNNTPDFG FGGQKRQLED GDQPESKKLA
AQGDSMSAQL GPIHPPPRST VTEEYRVPDG MVGLIIGRGG EQINKIQQDS GCKVQISPDS
GGLPERSVSL TGSPESVQKA KMMLDDIVSR GRGGPPGQFH DNANGQNGTV QEIMIPAGKA
GLVIGKGGET IKQLQERAGV KMILIQDGSQ NTNVDKPLRI IGDPYKVQKT VAGAGHPATE
TPPPPPQCCC REAVVGRIIT TEKQQRFSAA FQRQGVLRLH KNALAGSMVP VGTVLGIAVL
QACEMVMDIL RERDQGGFGD RNEYGSRIGG GIDVPVPRHS VGVVIGRSGE MIKKIQNDAG
VRIQFKQDDG TGPEKIAHIM GPPDRCEHAA RIINDLLQSL RVGGENVKAI NQQTGAFVEI
SRQLPPNGDP NFKLFIIRGS PQQIDHAKQL IEEKIEGPLC PVGPGPGPGG PPGPAGPMGP
FNPGPFNPGP PGAPPHPGAP PPHPYPPQGW GNTYPQWQPP APHDPSKAAA AADPNAAWAA
YYSHYYQQPP GPVPGQPPAP TAPPVQGEPP QPPPAGQSDY TKAWEEYYKK LGQQPQQPGA
PPQQDYTKAW EEYYKKQAAQ VATGGGPGAP PGPQPDYSAA WAEYYRQQAA YYGQTPGAGG
PVPPPTQQGQ QVSDRPCAPL PAFNPQL
//
