ID   STAC3_XENTR             Reviewed;         337 AA.
AC   Q68F99;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=SH3 and cysteine-rich domain-containing protein 3;
GN   Name=stac3;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for normal excitation-contraction coupling in
CC       skeletal muscle and for normal muscle contraction in response to
CC       membrane depolarization. Required for normal Ca(2+) release from the
CC       sarcplasmic reticulum, which ultimately leads to muscle contraction.
CC       Probably functions via its effects on muscle calcium channels.
CC       Increases CACNA1S channel activity, in addition to its role in
CC       enhancing the expression of CACNA1S at the cell membrane. Has a
CC       redundant role in promoting the expression of the calcium channel
CC       CACNA1S at the cell membrane. {ECO:0000250|UniProtKB:Q8BZ71}.
CC   -!- SUBUNIT: Component of a calcium channel complex with CACNA1S.
CC       {ECO:0000250|UniProtKB:Q8BZ71}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BZ71}. Cell
CC       membrane, sarcolemma {ECO:0000250|UniProtKB:Q8BZ71}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:Q8BZ71}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma, T-tubule
CC       {ECO:0000250|UniProtKB:Q8BZ71}.
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DR   EMBL; BC079943; AAH79943.1; -; mRNA.
DR   RefSeq; NP_001007507.1; NM_001007506.1.
DR   AlphaFoldDB; Q68F99; -.
DR   SMR; Q68F99; -.
DR   STRING; 8364.ENSXETP00000037412; -.
DR   PaxDb; Q68F99; -.
DR   DNASU; 493233; -.
DR   GeneID; 493233; -.
DR   KEGG; xtr:493233; -.
DR   CTD; 246329; -.
DR   Xenbase; XB-GENE-5903818; stac3.
DR   eggNOG; ENOG502QT6I; Eukaryota.
DR   HOGENOM; CLU_048120_1_1_1; -.
DR   InParanoid; Q68F99; -.
DR   OrthoDB; 902304at2759; -.
DR   PhylomeDB; Q68F99; -.
DR   TreeFam; TF332878; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
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:0045202; C:synapse; IEA:GOC.
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:0007274; P:neuromuscular synaptic transmission; ISS:UniProtKB.
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:0003009; P:skeletal muscle contraction; ISS:UniProtKB.
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; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SSF50044; 2.
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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Membrane; Metal-binding; Reference proteome;
KW   Repeat; SH3 domain; Zinc; Zinc-finger.
FT   CHAIN           1..337
FT                   /note="SH3 and cysteine-rich domain-containing protein 3"
FT                   /id="PRO_0000232584"
FT   DOMAIN          220..279
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          280..337
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   ZN_FING         59..110
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  38765 MW;  282411AE732881F5 CRC64;
     MFKKKAKEEK PSPVPDAQQN GELPNSGPII YYIYESEEEE EEEEEEPPPE PPRPVNDKPH
     KFKDHYLKKP KFCDVCARMI VLNNKFGLRC KNCKTNIHHH CQSYVEFQKC FGKIPPGFRR
     AYSSPLYSNQ QNACVKELMP FSASNRTDPV FDTLRVGVIM ANKERKKGQD DKKNPMLEEE
     PEELPPKPEE KQEGDVPDGD KKGEKGGQDA KNKKAQPGFM QSHYFVALYR FKALEKDDLD
     FQAGERITVI DDSNEEWWRG KVGEKAGYFP ANFIIRVRAA ERVYKVTRSF VGNREIGQIT
     LKKDQIVVQK GDEVNGYIKV STGRKVGLFP LDFLQEI