ID A0A3Q0CQQ6_MESAU Unreviewed; 1845 AA.
AC A0A3Q0CQQ6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=SH3 and multiple ankyrin repeat domains protein 2 isoform X4 {ECO:0000313|RefSeq:XP_021083026.1};
GN Name=Shank2 {ECO:0000313|RefSeq:XP_021083026.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021083026.1};
RN [1] {ECO:0000313|RefSeq:XP_021083026.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000256|ARBA:ARBA00034105}.
CC -!- SIMILARITY: Belongs to the SHANK family.
CC {ECO:0000256|ARBA:ARBA00010508}.
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DR RefSeq; XP_021083026.1; XM_021227367.1.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0050808; P:synapse organization; IEA:UniProt.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd09506; SAM_Shank1_2_3; 1.
DR CDD; cd11983; SH3_Shank2; 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; IPR032425; FERM_f0.
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:SF17; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF16511; FERM_f0; 1.
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; 4.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
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 196..229
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 230..262
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 297..329
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 330..362
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 526..585
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 626..720
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1782..1845
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1845 AA; 200927 MW; 72BD07331E73C4E7 CRC64;
MPRSPTSSED EMAQSFSDYS MGSESDSSKE ETIYDTIRAT TEKPSGVKME ELQGNTLVIR
VLIQDLQQTK CIRFNPDATV WVAKQKILCT LNQGLKDVLN YGLFQPASNG RDGKFLDEER
LLREYPQPVG PGVPSLEFRY KKRVYKQSNL DEKQLARLHT KTNLKKFMDH TQHHSVEKLV
KLLDRGLDPN FHDLETGETP LTLAAQLDDS MEVIKVLRNG GAHLDFRARD GMTALHKAAR
MRNQVALKTL LELGASPDYK DSYGLTPLYH TAIVGGDPYC CELLLHEHAS VCCKDENGWH
EIHQACRYGH VQHLEHLLFY GADMSAQNAS GNTALHICAL YNQDSCARVL LFRGGNKELK
NYNSQTPFQV AIIAGNFELA EYIKNHKETD IVPFREAPAY SNRRRRPPNT LAAPRVLLRS
NSDNNLHAGA PEWAVCAAAT SHRSLSPQLL QQTPNKPDGA TKNLGSYAPG PRSRSPSLNR
LGGTGEDGKR PQPHWHVGSP FTPGANKDSR STFEYPGPRR KLYSAVPGRL FVAIKPYQPQ
VDGEIPLHRG DRVKVLSIGE GGFWEGSARG HIGWFPAECV EEVQCKPRDS QAETRADRSK
KLFRHYTVGS YDSFDAASDC IIEDKTVVLQ KKDNEGFGFV LRGAKADTPI EEFTPTPAFP
ALQYLESVDE GGVAWQAGLR TGDFLIEVNN ENVVKVGHRQ VVNMIRQGGN HLVLKVVTVT
RNLDPDDTAR KKAPPPPKRA PTTALTLRSK SMTAELEELG LSLVDKASVR KKKDKPEEIV
PASKPSRTAE NVAIESRVAT IKQRPTSRCF PAASDVNSVY ERQGIAVMTP TVPGSPKGPF
LGLPRGTMRR QKSIGITEEE RQFLAPPMLK FTRSLSMPDT SEDIPPPPQS VPPSPPPPSP
TTYNCPKSPT PRVYGTIKPA FNQNPVAKVP PATRSDTVAT MMREKGMFYR RELDRFSLDS
EDVYSRSPAP QAAFRTKRGQ MPENPYSEVG KIASKAVYVP AKPARRKGML VKQSNVEDSP
EKTCSIPIPT IIVKEPSTSS SGKSSQGSSM EIDPQATEPG QLRPDDSLTV SSPFAAAIAG
AVRDREKRLE ARRNSPAFLS TDLGDEDVGL GPPAPRMRSS KFPEEGGFGD EDGTEQPLSP
TPGTTPRELE NHFLGGGEVV TQGETGGPLS SISKAKGPES GPAAPLKSGN TASPENYVHP
LTGRLLDPSS PLALALSARD RAMQESQQGH KGEAPKADLN KPLYIDTKMR PSVESSFPPV
TRQNTRGPLR RQETENKYET DLSKDRRADD KKNMLINIVD TAQQKSAGLL MVHTVDIPTA
GPPLEEEEDR EDVDIKPDHS PSTVPEGVPK TEGALQISAA PEPAAAPGRT IVAAGSVEEA
VILPFRIPPP PLASVDLDED FLFTEPLPPP LEFANSFDIP DDRAASVPAL ADLVKQKKND
TPQPPSLNSS QPANSADSKK PTGISNCLPS SFLPPPESFD AVTDSGIEEV DSRSSSDHHL
ETTSTISTVS SISTLSSEGG ESMDTCTVYA DGQAFVVDKP PVPPKPKMKP IVHKSNALYQ
DTLPEEDTDG FVIPPPAPPP PPGSAQASMA KVIQPRTSKL WGDVPEVKSP ILSGPKANVI
SELNSILQQM NRGKSVKPGE GLELPVGAKS ANLAPRSPEV MSTVSGTRST TVTFTVRPGT
SQPITLQSRA PDYESRTSGP RRAPSPVVSP TELNKEILPT PPSAAAASPS PTLSDVFSLP
SQSPAGDLFG LNPAGRSRSP SPSILQQPIS NKPFTTKPVH LWTKPDVADW LESLNLGEHK
ETFMDNEIDG SHLPNLQKED LIDLGVTRVG HRMNIERALK QLLDR
//
