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SHANK_CAEEL
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   03-AUG-2022, entry version 110.
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: CELE_H06I04.1; 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; -.
DR   EPD; B7WN72; -.
DR   PaxDb; B7WN72; -.
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   CTD; 174739; -.
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; 151556at2759; -.
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 tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 2.30.42.10; -; 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   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; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF50156; SSF50156; 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
 
 
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