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Database: UniProt
Entry: L5L4D5_PTEAL
LinkDB: L5L4D5_PTEAL
Original site: L5L4D5_PTEAL 
ID   L5L4D5_PTEAL            Unreviewed;      1456 AA.
AC   L5L4D5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=SH3 and multiple ankyrin repeat domains protein 1 {ECO:0000313|EMBL:ELK18492.1};
GN   ORFNames=PAL_GLEAN10004497 {ECO:0000313|EMBL:ELK18492.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK18492.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC       transposable elements and preventing their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements during
CC       meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC       governs the methylation and subsequent repression of transposons. Its
CC       association with pi-bodies suggests a participation in the primary
CC       piRNAs metabolic process. Required prior to the pachytene stage to
CC       facilitate the production of multiple types of piRNAs, including those
CC       associated with repeats involved in the regulation of retrotransposons.
CC       May act by mediating protein-protein interactions during germ cell
CC       maturation. {ECO:0000256|ARBA:ARBA00025297}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
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DR   EMBL; KB030309; ELK18492.1; -; Genomic_DNA.
DR   STRING; 9402.L5L4D5; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4375; Eukaryota.
DR   InParanoid; L5L4D5; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   CDD; cd17175; FERM_F0_SHANK1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd09506; SAM_Shank1_2_3; 1.
DR   CDD; cd11982; SH3_Shank1; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035735; Shank1_SH3.
DR   PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24135:SF3; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   REPEAT          246..278
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          313..345
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          460..519
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          608..664
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1393..1456
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1187..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1135..1151
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1206..1236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1252
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1456 AA;  153286 MW;  6B44D30487AEEC01 CRC64;
     MTRRPASSED EERHSASECP EGGSESDSSP DGPGRGLRGT RGRGSGAPGS LASVRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKV
     AVIAGNFELG ELIRNHREQD TVPFQESPKY AARRRGPPSA GLTVPPALLR ANSDTSMALP
     DWMVSRGTPR EGPTGGTGGS AGPGGSLGSR GRRRKLYSAV PGRSFMAVKS YQAQAEGEIS
     LSKGEKIKVL SIGEGGFWEG QVKGRVGWFP SDCLEEVANR SQEGKQESRS DKAKRLFRHY
     TVGSYDSFDA PRVPVPQLRQ GLRDLGLSPV PCSASPPPPL RPRRLLPSAA QTPIEEFTPT
     PAFPALQYLE SVDEGGVAWR AGLRMGDFLI EVNGQNVVKV GHRQVVNMIR QGGNTLMVKV
     VMVTRHPDMD EAVHKKAPQQ AKRLPPPAIS LRSKSMTSEL EEMEYEQPPA PVPSMEKKRT
     VYQMALNKLD EILAAAQQTI SASESPVAGG LASLGKHRPK GFFATELPAH RPQLWSSLVG
     LVPPGPGCNG HFLRGASLPC SSLAPEACPW ASPKPTLSCQ GSLSLPTSHP DLSHLESAEA
     TRGPLLDISV DGRLACGPDL LCLHRSSLSA SVPSLFSCSN PSAPRPEGAS RRCGAQCGPK
     AWSDLLGSEG EQSIAGHTTA QKLKARGISA LPDTYASALH PGGVGGPVQA SGGGAESPLI
     HCRSGRLLDP EVDSRSSSDH PLETISSAST LSSLSAEGGG SAGGGGGAGG ASVASGPELL
     DTYVAYLDGQ AFGGSGAPGP PYPPQLMTPS KLRGRALGAS GGLRPSPSGG LRDPVTPTSP
     TVSVTGAGTD GLLALSGCSG PSAAGVTGGP VAVEPEGPPV PLPSATSLPR KLLPWEEGPG
     PPPPPLPGPL AQPQASALAT VKASIISELS SKLQQFGGSS AAGGALPWAR GGSGGSGDSH
     HGGASYVPER TSSLQRQRLS DDSQSSLLSK PVSSLFQNWP KPPLPPLPTG TGVPPSAAAA
     PGATSPSASS SSTSTRHLQG VEFEMRPPLL RRAPSPSLLP ASEHKVSPAP RPSSLPILPS
     GPLYPGLFDM RSSPTGGAGG SADPFAPVFV PPHPGMSGGL GGALSGASRS LSPTRLLSLP
     ADKPFGAKPL GFWTKFDVAD WLEWLGLAEH RARFLDHEID GSHLPALTKE DYVDLGVTRV
     GHRMNIDRAL RFFLER
//
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