ID   SHAN2_XENLA             Reviewed;        1292 AA.
AC   Q52KW0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
DE            Short=Shank2;
GN   Name=shank2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to be an adapter protein in the postsynaptic density
CC       (PSD) of excitatory synapses that interconnects receptors of the
CC       postsynaptic membrane including NMDA-type and metabotropic glutamate
CC       receptors, and the actin-based cytoskeleton. May play a role in the
CC       structural and functional organization of the dendritic spine and
CC       synaptic junction (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC       Postsynaptic density {ECO:0000250}. Note=Cytoplasm, postsynaptic
CC       density of neuronal cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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DR   EMBL; BC094169; AAH94169.1; -; mRNA.
DR   RefSeq; NP_001089408.1; NM_001095939.1.
DR   AlphaFoldDB; Q52KW0; -.
DR   SMR; Q52KW0; -.
DR   BioGRID; 592239; 1.
DR   IntAct; Q52KW0; 1.
DR   DNASU; 734458; -.
DR   GeneID; 734458; -.
DR   KEGG; xla:734458; -.
DR   CTD; 734458; -.
DR   Xenbase; XB-GENE-984539; shank2.L.
DR   OrthoDB; 36120at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 734458; Expressed in brain and 15 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
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   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; SH3-binding; Synapse.
FT   CHAIN           1..1292
FT                   /note="SH3 and multiple ankyrin repeat domains protein 2"
FT                   /id="PRO_0000247761"
FT   DOMAIN          56..150
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1229..1292
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          155..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           991..997
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        335..359
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..970
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1292 AA;  141180 MW;  05C63F768DE5979F CRC64;
     MVTPRLQTMA ESSKFKKKVH FGETRSDRTK KLFRHYTVGS YDSFDASSDC IIEEKTVVLQ
     KKDNEGFGFV LRGAKADTPI EEFNPTPAFP ALQYLESVDE DGVAWQAGLR TGDFLTEVNN
     ENVVKVGHRQ VVNMIRHGGN HLVLKVVTVT RNLDPDDTAR KKAPPPPKRA PTTALSLRSK
     SMTSELEELA VDIASVRRRK DVQVSDVECL KRRIVIRVAL NKSEESGPIS KPLRPLDNTP
     VNSRVATVKQ RPTSRCFPAA SDTNSMYDRQ GIAVIPPTTP GSHQGPFLGI PRGTMRRQKS
     IDSRIPLSGI TEEERQFLAP PMLKFTRSLS MPDASEDIPP PPATLPPSPP PPSPSSFNSP
     KSPAPRGYGT IKPAFTQNSG TKSPSPAVRS DNVGTIARDK SMYFRHEANR FSLDSEELYN
     SNMSTQQNFI NKRSKMPENP YSEVGRLGNK GVYVPAKPVR RKGMLVKQSN VEDSPEKTCS
     IPIPTIIIKE PSTSSSGKSS QGSSMETDLQ ISEQVGQLRP DESLNVSGPF AAAIAGAVRD
     REKRLEARRN SPAFLSTDLG DECVGPKPSP RLQHSKSIDD GMFCSEEKAK HFMAPSSLII
     NRGSSNAFTN NDSSHQGDVS NARMSKIKGP ENNAAPAKST NASGNYMHPV TGKLLDPNSP
     LALALAARDR ALKEQNQPSP SPTDPEKADL NKPLFIDTKL RSGMETINAN RPNMRGMLKR
     QETESKHEPD SSKEEKRQGE KKNMLINIMD TSQQKTAGLL MVHTVDTTKA DNVLTESEEA
     EKDPPPENSN SPVSEPREEL ENSIPKASEC GTPAAPHIKA IVSVCSVEEP VILPFRIPPP
     PFASVDVDED FVFTEPLPPP LEFANSFDIP EDASQIPPAS LADLLIQRKN RAFPPPSFNP
     NIASNSIESK RLAALSNCLP TSFMQHPESF DNVTDSGIEE VDSRSGSDHH LETTSTISTV
     SSISTLSSEG GENLDTCTVY ADGQAFLVDK PPVPPKPKVK PIINKSNALY KDAVLEENLD
     NFAVPLPAPP PLPLSIQPSM TKAGQQRTSK LWGDNTEVKS LVMPSPKANV ISELNSILQQ
     MNREKATKTG EGLDSPTGMK TASLSTRGTD ALSTVSGNRN AAVTFTIRPG ANQPISLQNR
     TPEFDSRVTG MRRAPSPVVV SPAEIIRDIK PGPLSAPPAS MSDVFILPSQ PPSGDMFGMS
     MGRSRSPSPS ILQQPISNKP FSAKPIHMWT KQDVAEWLES LHLGEHREMF MDNEIDGTHL
     PNLQKEDLID LGVTRVGHRM NIERALKQLL DR