ID A0A2U3WLZ7_ODORO Unreviewed; 2166 AA.
AC A0A2U3WLZ7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=SH3 and multiple ankyrin repeat domains protein 1 {ECO:0000313|RefSeq:XP_004409995.1};
GN Name=SHANK1 {ECO:0000313|RefSeq:XP_004409995.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004409995.1};
RN [1] {ECO:0000313|RefSeq:XP_004409995.1}
RP IDENTIFICATION.
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_004409995.1; XM_004409938.1.
DR STRING; 9708.A0A2U3WLZ7; -.
DR GeneID; 101374247; -.
DR KEGG; oro:101374247; -.
DR CTD; 50944; -.
DR InParanoid; A0A2U3WLZ7; -.
DR OrthoDB; 2247290at2759; -.
DR Proteomes; UP000245340; 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; 1.
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:UP000245340};
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 663..757
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 2103..2166
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1825..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1950..2028
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..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1017
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1862
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2166 AA; 225218 MW; 64DF2D890C7729B1 CRC64;
MTHSPASSED EEHHSASECP 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 ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
RGPPGAGLTV PPALLRANSD TSMALPDWMV FAAPGTSSSG APGPTSGPQG QSQPSAPSTK
LSSGTLRSAS SPRGARARSP SRGRHPEEAK RQPRGRPSSS GTPREGPAGG TGGSGGPGGS
LGSRGRRRKL YSAVPGRSFM AVKSYQAQAE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
GWFPSDCLEE VANRSQEGKQ EGRSDKAKRL FRHYTVGSYD SFDAPSLMDG IGPGSDYIIK
EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA PQQAKRLPPP
AISLRSKSMT SELEEMEYEQ QPAPVPSMEK KRTVYQMALN KLDEILAAAQ QTISASESPG
PGGLASLGKH RPKGFFATES SFDPHHRSQP SYERPSYLPP GPGLMLRQKS IGAAEDDRPY
LAPPAMKFSR SLSVPGSEDI PPPPTTSPPE PPYSTPPAPS SSGRLTPSPR GGPFNPSSGG
PLPSSSPASF DGPSPPDTRV GGREKSLYHS GALPPAHHHP PHHHHHHAPP PPPHHHHAHP
PHPPEMETGG SPDDPPPRLA LGPQPSLRGW RGGGPSPTPG APSPSHHGSG GGGISSSQAP
ALRYFQLPPR AASAAMYVPA RSGRGRKGPL VKQTKVEGEP QKGGGLPPAP SPTSPASPQP
PPAAPSEKNS IPIPTIIIKA PSTSSSGRSS QGSSTEAEPP TQPEAAGGGG GGGGSSAPSP
APAMSPVPPS PSPVPTPTSP SGPATLDFTS QFGAALVGAA RREGGWQNEA RRRSTLFLST
DAGDEDGGDS GLGPGAPPGP RLRHSKSIDE GMFSAEPYLR LESAGAGSSG GGYGAYAAGS
RAYAGSGSSS AFTSFLPPRP LVHPLTGKAL DPASPLGLAL AARERALKES SEGGGPPQPP
PRPPSPRYEA PPPTPHHHSP HAHHEPVLRL WGASPPDPAR RELGYRAGLG SQEKSLPASP
PAARRSLLHR LPPTAPGVGP LLLQLGPEPP PPHPGVSKAW RSGAPEEPER LPLHVRFLEN
CQPRASGAGG RGPPSEDGPG VPPPSPRRSV PPSPTSPRGS EENGLPLLVL PPPAPSVDVE
DGEFLFVEPL PPPLEFSNSF EKPESPLTPG PPHPLPDPPT PTTPLPPAPP PAIAAAPPTL
DSTASSLTSY DSEVATLTQG APVAPGDPPP PGPAAPAAPA PPAPQPGPDP PPGTDSGIEE
VDSRSSSDHP LETISSASTL SSLSAEGGGS AGGGGGGGAG GAGVASGPEL LDTYVAYLDG
QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGGLRPGPSG GLRDPVTPTS PTVSVTGAGT
DGLLALSGCT GPSTAAMAGG PVAIEPEGPP VPLPSASSLP RKLLPWEEGP GPPPPPLPGP
LAQPQASALA TVKASIISEL SSKLQQFGGS SAAGGALPWA RGGSGGSGDS HHGGASYVPE
RTASLQRQRL SEDSQSSLLS KPVSSLFQNW PKPPLPPLPT GSGVPPSAAA APGATSPSAS
SSTSTRHLQG VEFEMRPPLL RRAPSPSLLP ASEHKVSPAP RPSSLPILPS GPLYPGLFDI
RSSPTGGAGG SADPFAPVFV PPHPGMSGGL GGALSGASRS LSPTRLLSLP PDKPFGAKPL
GFWTKFDVAD WLEWLGLAEH RAQFLDHEID GSHLPALTKE DYVDLGVTRV GHRMNIDRAL
KFFLER
//
