ID A0A3Q7SZV5_VULVU Unreviewed; 1901 AA.
AC A0A3Q7SZV5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=SH3 and multiple ankyrin repeat domains protein 1 {ECO:0000313|RefSeq:XP_025870009.1};
GN Name=SHANK1 {ECO:0000313|RefSeq:XP_025870009.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025870009.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025870009.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025870009.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025870009.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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: Postsynaptic density
CC {ECO:0000256|ARBA:ARBA00034105}.
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DR RefSeq; XP_025870009.1; XM_026014224.1.
DR STRING; 9627.ENSVVUP00000017445; -.
DR KEGG; vvp:112931508; -.
DR OrthoDB; 2247290at2759; -.
DR Proteomes; UP000286640; Unplaced.
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 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 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; 6.
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; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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:UP000286640};
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 REPEAT 346..378
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 554..613
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 664..758
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1838..1901
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1795
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 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1901 AA; 198817 MW; CF1F378E7370B28E CRC64;
MTHSPASSED EERHSASECP EGGSESDSSP DGPSRGPRGT RGQGSGAPGS LASTRGLQGR
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 LHICALYNKE
TCARILLYRG ANKDVKNHNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
RGPPGAGLTV PPALLRANSD TSMALPDWMV FAAPGTSSSG APGPTSGTQG QSQPSAPSTK
LSSGTLRSAS SPRGARARSP SRGRHPEEAK RQPRGRPSSS GTPREGPAGG TGGSGGPGGS
LGSRGRRRKL YSAVPGRSFM AVKSYQAQAE GEISLSKGEK IKVLSIGEGG FWEGQVKGRI
GWFPSDCLEE VANRSQEGKQ ESRSDKAKRL FRHYTVGSYD SFDAPRSLMD GIGPGSDYII
KEKTVLLQKK DSEGFGFVLR GAKAQTPIEE FTPTPAFPAL QYLESVDEGG VAWRAGLRMG
DFLIEVNGQN VVKVGHRQVV NMIRQGGNTL MVKVVMVTRH PDMDEVHKKA PQQAKRLPPP
AISLRSKSMT SELEEMEYEQ QPAPVPSMEK KRTVYQMALN KLDEILAAAQ QTISASESPG
PGGLASLGKH RPKGFFATES SFDPHHRSQP SYERPSYLPP GPGLMLRQKS IGAAEDDRPY
LAPPAMKFSR SLSVPGSEDI PPPPTTSPPE PPYSTPPAPS SAPSPAPAMS PVPPSPSPVP
TPTSPSGPAT LDFTSQFGAA LVGAARREGG WQNEARRRST LFLSTDAGDE DGGDSGLGPG
APPGPRLRHS KSIDEGMFSA EPYLRLESAG AGSGAGYGAY GAGSRAYGGS GGSSAFTSFL
PPRPLVHPLT GKALDPASPL GLALAARERA LKESSEGGGP PQPPPRPPSP RYEAPPPTSL
SIPRLKGSLX PDPARRELGY RAGLGSQEKS LPASPPAARR SLLHRLPPTA PGVGPLLLQL
GPEPPPPHPG VSKAWRSGAP EEPERLPLHV RFLENCQPRA SGPGGRGPPS EDGPGVPPPS
PRRSVPPSPT SPRGGEENGL PLLVLPPPAP SVDVEDGEFL FVEPLPPPLE FSNSFEKPES
PLTPGPPHPL PDPPTPTTPL TPVPPPAVAA APPTLDSTAS SLTSYDSEVA TLTQGAPVAP
GDPPPPGPPA PAAPAPPAPQ PGPDPPPGTD SGIEEVDSRS SSDHPLETIS SASTLSSLSA
EGGGSAGGGG GGGGSVASVA SGPELLDTYV AYLDGQAFGG SGTPGPPYPP QLMTPSKLRG
RALGTSGGLR PGPSGGLRDP VTPTSPTVSV TGAGTDGLLA LSGCTGPSVA SMAGGSVAIE
PEGPTVPLPS ASSLPRKLLP WEEGPGPPPP PLPGPLAQPQ ASALATVKAS IISELSSKLQ
QFGGSSAAGG ALPWARGGSG GSGDSHHGGA SYVPERTSSL QRQRLSEDSQ SSLLSKPVSS
LFQNWPKPPL PPLPTGSGVP PSAAAAPGAT SPSASSSTST RHLQGVEFEM RPPLLRRAPS
PSLLPASEHK VSPAPRPSSL PILPSGPLYP GLFDIRGSPT GGAGGSADPF APVFVPPHPG
ISGGLGGALS GASRSLSPTR LLSLPPDKPF GAKPLGFWTK FDVADWLEWL GLAEHRAQFL
DHEIDGSHLP ALTKEDYVDL GVTRVGHRMN IDRALKFFLE R
//
