ID SHANK_CAEEL Reviewed; 1140 AA.
AC B7WN72; Q09493; Q7JMK1;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Protein shank {ECO:0000303|PubMed:15013747};
GN Name=shn-1 {ECO:0000303|PubMed:15013747, ECO:0000312|WormBase:C33B4.3c};
GN ORFNames=C33B4.3 {ECO:0000312|WormBase:C33B4.3c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15013747; DOI=10.1016/s0014-5793(04)00107-3;
RA Jee C., Lee J., Lee J.I., Lee W.H., Park B.J., Yu J.R., Park E., Kim E.,
RA Ahnn J.;
RT "SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the
RT inositol-1,4,5-trisphosphate receptor.";
RL FEBS Lett. 561:29-36(2004).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21191812; DOI=10.1007/s10059-011-0007-9;
RA Oh W.C., Song H.O., Cho J.H., Park B.J.;
RT "ANK repeat-domain of SHN-1 is indispensable for in vivo SHN-1 function in
RT C. elegans.";
RL Mol. Cells 31:79-84(2011).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EGL-19, AND DISRUPTION PHENOTYPE.
RX PubMed=28477407; DOI=10.7554/elife.18931;
RA Pym E., Sasidharan N., Thompson-Peer K.L., Simon D.J., Anselmo A.,
RA Sadreyev R., Hall Q., Nurrish S., Kaplan J.M.;
RT "Shank is a dose-dependent regulator of Cav1 calcium current and CREB
RT target expression.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Scaffold protein that most likely acts in the postsynaptic
CC density (PSD) of excitatory synapses which orchestrates synapse
CC formation and maintenance at neuromuscular junctions (PubMed:28477407).
CC Associates with and trafficks the L-type calcium channel egl-19 to the
CC cell surface of body wall muscles to ensure the function of the calcium
CC channel and therefore maintain the Ca(2+) current density
CC (PubMed:28477407). The maintenance of Ca(2+) also allows for the
CC downstream regulation of Ca(2+)-induced expression of genes such as
CC gem-4 (PubMed:28477407). Plays a role in the regulation of the
CC defecation cycle, and this may be in association with the inositol
CC trisphosphate (IP3) receptor itr-1, which in turn mediates periodic
CC calcium release and muscle contractions (PubMed:15013747,
CC PubMed:21191812). Required for normal fertility and pharyngeal pumping
CC (PubMed:21191812). {ECO:0000269|PubMed:15013747,
CC ECO:0000269|PubMed:21191812, ECO:0000269|PubMed:28477407}.
CC -!- SUBUNIT: Interacts (via PDZ domain) with egl-19 (via C-terminus).
CC {ECO:0000269|PubMed:28477407}.
CC -!- INTERACTION:
CC B7WN72; Q8MXV3: ccep-135; NbExp=2; IntAct=EBI-2914750, EBI-2422468;
CC -!- SUBCELLULAR LOCATION: Cell projection, pseudopodium
CC {ECO:0000269|PubMed:15013747}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15013747}. Postsynaptic density
CC {ECO:0000305|PubMed:28477407}. Note=Localizes to sperm pseudopodium.
CC {ECO:0000269|PubMed:15013747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:C33B4.3c};
CC IsoId=B7WN72-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C33B4.3a};
CC IsoId=B7WN72-2; Sequence=VSP_059097;
CC Name=b {ECO:0000312|WormBase:C33B4.3b};
CC IsoId=B7WN72-3; Sequence=VSP_059097, VSP_059098, VSP_059099;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, pharyngeal-intestinal
CC valve, intestine, rectal epithelial cells, tail neurons, nerve cord and
CC sperm. {ECO:0000269|PubMed:15013747}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryos to
CC adults. Highly expressed in the nerve cord of embryos. Expressed in
CC vulval epithelial cells of L4 stage hermaphrodites.
CC {ECO:0000269|PubMed:15013747}.
CC -!- DISRUPTION PHENOTYPE: Animals are viable, but produce a reduced brood
CC size, have a prolonged defecation cycle and a reduced pharyngeal
CC pumping rate as compared to wild-type (PubMed:21191812). Reduced male
CC fertility which may be due to irregular male mating behavior and
CC defective sperm function (PubMed:21191812). Reduced cell surface
CC abundance of the L-type egl-19 calcium channel in body wall muscles,
CC which results in a 20% decrease in Ca(2+) current density
CC (PubMed:28477407). In response to the nicotinic acetylcholine agonist
CC levamisole, there is reduced expression of genes such as gem-4
CC (PubMed:28477407). Irregular postsynaptic transmission at neuromuscular
CC junctions characterized by larger stimulus-evoked excitatory
CC postsynaptic currents as compared to wild-type (PubMed:28477407). RNAi-
CC mediated knockdown results in viable animals with no visible phenotype
CC (PubMed:15013747). However, there is a slight reduction in brood size,
CC but there are no visible defects in terms of embryonic viability,
CC growth or morphology in their resulting progeny (PubMed:15013747).
CC RNAi-mediated knockdown in an itr-1(sa73) loss of function mutant
CC background results in a longer defecation cycle as compared to the itr-
CC 1 single mutant (PubMed:15013747). {ECO:0000269|PubMed:15013747,
CC ECO:0000269|PubMed:21191812, ECO:0000269|PubMed:28477407}.
CC -!- MISCELLANEOUS: In contrast to the mammalian Shank proteins, does not
CC contain a SH3 domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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DR EMBL; BX284602; CAA88324.1; -; Genomic_DNA.
DR EMBL; BX284602; CAE54886.1; -; Genomic_DNA.
DR EMBL; BX284602; CAV31765.1; -; Genomic_DNA.
DR PIR; T19673; T19673.
DR RefSeq; NP_001022006.1; NM_001026835.3. [B7WN72-2]
DR RefSeq; NP_001022007.1; NM_001026836.3. [B7WN72-3]
DR RefSeq; NP_001254297.1; NM_001267368.1.
DR AlphaFoldDB; B7WN72; -.
DR SMR; B7WN72; -.
DR IntAct; B7WN72; 18.
DR STRING; 6239.C33B4.3c.1; -.
DR EPD; B7WN72; -.
DR PaxDb; 6239-C33B4-3c; -.
DR PeptideAtlas; B7WN72; -.
DR EnsemblMetazoa; C33B4.3a.1; C33B4.3a.1; WBGene00006444. [B7WN72-2]
DR EnsemblMetazoa; C33B4.3b.1; C33B4.3b.1; WBGene00006444. [B7WN72-3]
DR EnsemblMetazoa; C33B4.3c.1; C33B4.3c.1; WBGene00006444. [B7WN72-1]
DR GeneID; 174739; -.
DR KEGG; cel:CELE_C33B4.3; -.
DR UCSC; C33B4.3a; c. elegans.
DR AGR; WB:WBGene00006444; -.
DR WormBase; C33B4.3a; CE01508; WBGene00006444; shn-1. [B7WN72-2]
DR WormBase; C33B4.3b; CE36107; WBGene00006444; shn-1. [B7WN72-3]
DR WormBase; C33B4.3c; CE43434; WBGene00006444; shn-1. [B7WN72-1]
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4375; Eukaryota.
DR GeneTree; ENSGT00940000153561; -.
DR InParanoid; B7WN72; -.
DR OMA; RCSHDEV; -.
DR OrthoDB; 2247290at2759; -.
DR PhylomeDB; B7WN72; -.
DR Reactome; R-CEL-6794361; Neurexins and neuroligins.
DR PRO; PR:B7WN72; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006444; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IGI:WormBase.
DR GO; GO:0007622; P:rhythmic behavior; IGI:WormBase.
DR CDD; cd17091; FERM_F0_SHANK; 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; 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; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24135:SF28; LD13733P; 1.
DR PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Cytoplasmic vesicle;
KW Reference proteome; Repeat; Synapse.
FT CHAIN 1..1140
FT /note="Protein shank"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441737"
FT REPEAT 144..174
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 178..207
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 211..242
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 246..275
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 279..309
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 312..341
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT DOMAIN 436..529
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1078..1140
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 337..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 546..575
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059097"
FT VAR_SEQ 1014..1023
FT /note="MSVASSSTAS -> VVKYHSNTRR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059098"
FT VAR_SEQ 1024..1140
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059099"
SQ SEQUENCE 1140 AA; 125946 MW; CE17B1F5BC5CC8DF CRC64;
MNQEEDTVNL QIFVPELNVR KFLAVTQNDF IWDVKRKLLA TLPQALPQAF NYGLFLPPCD
GRAGKFLLED RTIRDYPFTD CVPYLELKYK KRVYKMLNLD EKQLKAMHTK GQLKKFMDYV
QQKNNEKVEK MCSQGLDANF HDAQGETPLT LAAGIPNNRA VIVSLIGGGA HVDFRNSEGQ
TAMHKAAFLS SFENVKTLIE LGASPNYRDP IGLTPLYYNM LTADSNDQVA EILLREAADI
GVTDMHGNHE IHQACKNGLT KHVEHLLYFG GQIDAENVNG NSPLHVCAVN NRPECARVLL
FRGADHLAVN KQGQTALHVS HIVGNPGVAD VVQAHNPKSS VPYRGTPQYS TRRRLSSTIT
RRRSMSQSSI CSQDVYRTPQ SVRKGPMSAA PSPSPSRSSR TTITPSEYGT MRRSGMDSMR
GGGMIAAGHE TNIARILVIP RGVKGFGFIL RGAKHVAMPL NFEPTAQVPA LQFFEGVDMS
GMAVRAGLRP GDYLLEIDGI DVRRCSHDEV VEFIQQAGDT ITLKVITVDV ADMSRGGTIV
HRPPTASSRH SLVFTPTPSA IYSSTKASSV YRMRFDTHDA HGVDYYAPNE IRNAYSESRH
ASVRQRPGSG RRISAAELEN LMVRQRVPSV QGSPYQMQYD QESLNGGYSS KKYNSVSDMK
RRKGQRNVVA SSAGLNRSTF EQAAPTTSTF EYNCSSRSTP QLSRMDSFDS FDDEDEMPAP
PPASYISPDL QRDSSMQRSE YSRPFRPTSR PKTPPPPPPM QHQNHQNHQY QQQHPSLPRS
ASTPQPIQQQ QSSIPPPPPP PPPPHCEPTM VHVEFTPPST SSVPPPPPPL PPISSGAPPP
PPPPPPGGLM HVAASAPVLM SNSKGISADA LKSVQLKKAE PRETSAASVS NNNNNNNNST
TDFQMDLKNA LAKRRSKVAH DVDEDEERES RFEGLSLRET VRENVVERGK GIQNIGIVNK
KDSGYTSSRT SLEPSESEEK DHRPHFSLDH SPNVQRVTLI SQHLEDNYGQ KDNMSVASSS
TASSSSTVDL TKPGCFVVPS HVIPPVDYDD DPDSGTGDSD GEIRCSEISF EHKKVDVWSV
DDVIGWLSSL HLSEYTPAFR SQRINGRCLR QCDRSRFTQL GVTRIAHRQI IESALRGLLQ
//
