STAC3_DANRE
ID STAC3_DANRE Reviewed; 334 AA.
AC Q6DBR6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=SH3 and cysteine-rich domain-containing protein 3;
GN Name=stac3 {ECO:0000312|ZFIN:ZDB-GENE-040801-248};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAH78395.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH CACNA1S, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23736855; DOI=10.1038/ncomms2952;
RA Horstick E.J., Linsley J.W., Dowling J.J., Hauser M.A., McDonald K.K.,
RA Ashley-Koch A., Saint-Amant L., Satish A., Cui W.W., Zhou W., Sprague S.M.,
RA Stamm D.S., Powell C.M., Speer M.C., Franzini-Armstrong C., Hirata H.,
RA Kuwada J.Y.;
RT "Stac3 is a component of the excitation-contraction coupling machinery and
RT mutated in Native American myopathy.";
RL Nat. Commun. 4:1952-1952(2013).
CC -!- FUNCTION: Required for normal excitation-contraction coupling in
CC skeletal muscle and for normal muscle contraction in response to
CC membrane depolarization (PubMed:23736855). Required for normal Ca(2+)
CC release from the sarcplasmic reticulum, which ultimately leads to
CC muscle contraction. Probably functions via its effects on muscle
CC calcium channels. Increases CACNA1S channel activity, in addition to
CC its role in enhancing the expression of CACNA1S at the cell membrane.
CC Has a redundant role in promoting the expression of the calcium channel
CC CACNA1S at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q8BZ71, ECO:0000269|PubMed:23736855}.
CC -!- SUBUNIT: Component of a calcium channel complex with CACNA1S.
CC {ECO:0000303|PubMed:23736855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BZ71}. Cell
CC membrane, sarcolemma {ECO:0000269|PubMed:23736855}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8BZ71}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000269|PubMed:23736855}.
CC -!- TISSUE SPECIFICITY: Expressed in muscles at the muscle triad.
CC {ECO:0000269|PubMed:23736855}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein level).
CC {ECO:0000269|PubMed:23736855}.
CC -!- DISRUPTION PHENOTYPE: The mutants mi34 that do not express the protein
CC exhibit altered motor behavior most probably due to a defect in the
CC coupling between the electrophysiological activation and the muscular
CC response. The nervous system, the neuromuscular junction or the
CC skeletal muscles seem normal. {ECO:0000269|PubMed:23736855}.
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DR EMBL; CR753874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078395; AAH78395.1; -; mRNA.
DR RefSeq; NP_001003505.1; NM_001003505.1.
DR AlphaFoldDB; Q6DBR6; -.
DR SMR; Q6DBR6; -.
DR STRING; 7955.ENSDARP00000100517; -.
DR PaxDb; Q6DBR6; -.
DR PRIDE; Q6DBR6; -.
DR Ensembl; ENSDART00000163474; ENSDARP00000133228; ENSDARG00000098883.
DR Ensembl; ENSDART00000193970; ENSDARP00000151899; ENSDARG00000098883.
DR GeneID; 445111; -.
DR KEGG; dre:445111; -.
DR CTD; 246329; -.
DR ZFIN; ZDB-GENE-040801-248; stac3.
DR eggNOG; ENOG502QT6I; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_1_1_1; -.
DR InParanoid; Q6DBR6; -.
DR OMA; DQQYACV; -.
DR OrthoDB; 902304at2759; -.
DR PhylomeDB; Q6DBR6; -.
DR TreeFam; TF332878; -.
DR PRO; PR:Q6DBR6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000098883; Expressed in muscle tissue and 18 other tissues.
DR ExpressionAtlas; Q6DBR6; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:ZFIN.
DR GO; GO:0003009; P:skeletal muscle contraction; IMP:ZFIN.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
DR GO; GO:0033292; P:T-tubule organization; IMP:ZFIN.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR039688; STAC1/2/3.
DR PANTHER; PTHR15135; PTHR15135; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Metal-binding; Reference proteome;
KW Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..334
FT /note="SH3 and cysteine-rich domain-containing protein 3"
FT /id="PRO_0000430689"
FT DOMAIN 217..276
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 277..334
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 62..113
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 38826 MW; 951F1BB0D84026B2 CRC64;
MAQYDQLEDK DSLDIHDNPP APENVVKEDD NTVYFVYDEE VEEEEAPPPP TPEPIVQVND
KPHKFKDHYC KKPKFCDVCA RMIVLNNKFA LRCKNCKTNI HHSCQSYVQF QRCFGKIPPG
FRRAYSSPLY DQEINNPGQQ NRTDPVFDTL RVGVIMANKE RKKGSEDKKN MMMMMMEEEE
AQQPKEDEEG AEGKQDGDKK DKTATDDKNK KQQQTFSQSH YYMALYRFKA IEKDDLDFHP
GDRITVLDDS NEEWWRGKIG EKTGYLPMTY IIRVRAGERV YKVTRSFVGN REMGQITLKK
DQIVVKKGEE VNGYLKVSTG RKLGFFPADL LHEL
