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Database: UniProt
Entry: A0A3Q2EIZ5_CYPVA
LinkDB: A0A3Q2EIZ5_CYPVA
Original site: A0A3Q2EIZ5_CYPVA 
ID   A0A3Q2EIZ5_CYPVA        Unreviewed;      1695 AA.
AC   A0A3Q2EIZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=SH3 and multiple ankyrin repeat domains protein 1-like {ECO:0000313|Ensembl:ENSCVAP00000032588.1};
GN   Name=SHANK1 {ECO:0000313|Ensembl:ENSCVAP00000032588.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000032588.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000032588.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic density
CC       {ECO:0000256|ARBA:ARBA00034105}.
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DR   STRING; 28743.ENSCVAP00000032588; -.
DR   Ensembl; ENSCVAT00000033113.1; ENSCVAP00000032588.1; ENSCVAG00000022791.1.
DR   GeneTree; ENSGT00940000153561; -.
DR   OMA; EEIHKAC; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
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; 2.
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:UP000265020};
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          165..198
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          199..231
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          299..331
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          474..533
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          573..667
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1632..1695
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          380..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1544..1578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..856
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..959
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1179..1193
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1303
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1695 AA;  186466 MW;  7A7C9F982B09E99D CRC64;
     MVQKFGCRKT WIQQCQCDIQ PELYGSSLSK GLAIQSLTQC LQFDQDCTVW SAKQQIVCSL
     GESLWDVYNY GLFQPAGEGR DAKFLEEERP LRDYARTFEK GVPYLEFRYK TRVYKQTNLD
     EKALAKLTTK ASQKKFIEYV QTGAMEKMAK VLDKGLDPNF HDPDSGETPL SVAVQSGLSV
     EGIRLLVLGG AHMDFRSRDG MTALHKAVRA HNHAGLLALL SLGASPDYKD RCGLTPLYHT
     VLTGGETSCC ETLLYYRAKL GTRDENGWDE SHQACQNGFA QHLEHLLFYG ADTASQNASG
     NTALHISALY NKESCVRVLL YRGANKEAKN KHGQTPFQVA VMSGHFELGE IIKNHKDTDI
     VPFLESPKFV PRRKDSVHTL PLPSLQSHPL LRANSDNTMT QSDPLSLPNK AATNPNPGQV
     LKGLGMCASV DLCDNMHSLC DLHAWSSVCL CRASAGAPSA GSGGGQMKRM YSAVPGRMYV
     AIRSHSASGD RELSLNKGDK VKVLSVGEGG YWEGTARGRT GWFPSDCVQE VAPPSKEKET
     RSEKAKRKLF RNVTVGAYDG TDGPSDYIIK EKTVLLQKKD NEGFGFVLRG AKAQTPIEEF
     TPTPAFPALQ YLESVDEGGV AWRAGLRMGD FLIEVNGQNV VKVGHRQVVN MIRQGGNSLM
     VKVVMVARNP ELEDTARKKA PQQTKRLTPP AIALRSKSMT SELEDMVCFT IKDSYKNVLH
     NIWFKYQIVP FHYIQTYIYV VLFAFLFEMC SNTLKQPYEQ QSSVSMMQTG QGFGYNQAHF
     QPGHGPQHAV MMRQKSIGVT EEERQHLHPP AMKLARSLSV PGPEDIPPPP NTSAPEPPLS
     AGPYPGRGPA MPIPPISQPH YQLHSQSAHP AQPVWEMGGP GVINQQVMVP TLRRQSDGLC
     IREPEAPRRG GGKMGGLRRG YSIGRDGRGV ARRGGRGALI KQSKVEDGLR QHRGKGGATK
     EKSSIPIPTI IVKAPSTSSS GRSSQGSSME ADVAPTVSSQ QNLENQDGQP KSAPSVYGNQ
     PTTTFIHPLT GKVLDPSSPL GLALAARERA LKDDRRTRRD DRHFGRQLST VGSFPTPIQT
     PTPSLFATPT QSAYTSPVSL HLGSPSVTTS PSSLSRPQSP RILRLGGGGE RVEREREGGP
     KEGLRVRFSE DKNSQFPTQY YPQSSREKEK EMYEREHAQP VQPPPPPAQP APRRPSYLHM
     ENIPNTSYIP QYTVPTAPSQ TNDTVGEARA GAGGLGLMVL PPPAPSIDVD EEFVFADPLP
     PPLQFANGKN ERALEFSQHH SHHISSVAPP PPPPPPSPKP QNPPQQSSQA SSDYTMAGVK
     VSISTGNKET DPTHSSAVIP KSGDWQDTVV DSGIEELDSH SSSDHHLEML GLSGLRGEKI
     GHGGNAQGRE GEKVSDHQDT CITYRGGQTF ELHTSKLANP VFPKMTHYKE HKQSRPRIED
     GFSSALAQVG VQHGGMVMEG RRLHSPFSGV KANIINELSS KLQQMSSMRS MDDWSHAPKS
     PNIHRLMPTS PVHSHPPHSP TYCPYPTSPK HRSKLRRQTF DFQCSPSKEM RSSVSRRRAP
     SPLIYSTEQP NPTPPRPSSL PILPSTPIYS NPFDFPASSP LHLPPSPSCL NYPHLSPAPP
     AKPFAIKPLP YWTKYDVADW LTYLNLGEHR ERFIDNEIDG SHLPSLTKDD FLDLGVTRVG
     HRMNIERALK KLTDR
//
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