STAC_MOUSE
ID STAC_MOUSE Reviewed; 403 AA.
AC P97306;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=SH3 and cysteine-rich domain-containing protein;
DE AltName: Full=Src homology 3 and cysteine-rich domain-containing protein;
GN Name=Stac {ECO:0000303|PubMed:8954993};
GN Synonyms=Stac1 {ECO:0000303|PubMed:27149520, ECO:0000303|PubMed:29467163};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C3H/HeJ; TISSUE=Brain;
RX PubMed=8954993; DOI=10.1006/bbrc.1996.1900;
RA Suzuki H., Kawai J., Taga C., Yaoi T., Hara A., Hirose K., Hayashizaki Y.,
RA Watanabe S.;
RT "Stac, a novel neuron-specific protein with cysteine-rich and SH3
RT domains.";
RL Biochem. Biophys. Res. Commun. 229:902-909(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=23818578; DOI=10.1073/pnas.1310571110;
RA Nelson B.R., Wu F., Liu Y., Anderson D.M., McAnally J., Lin W.,
RA Cannon S.C., Bassel-Duby R., Olson E.N.;
RT "Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced
RT Ca2+ release and contractility.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11881-11886(2013).
RN [3]
RP INTERACTION WITH CACNA1H, AND FUNCTION.
RX PubMed=27149520; DOI=10.1080/19336950.2016.1186318;
RA Rzhepetskyy Y., Lazniewska J., Proft J., Campiglio M., Flucher B.E.,
RA Weiss N.;
RT "A Cav3.2/Stac1 molecular complex controls T-type channel expression at the
RT plasma membrane.";
RL Channels 10:346-354(2016).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CACNA1C.
RX PubMed=28112192; DOI=10.1038/srep41003;
RA Campiglio M., Flucher B.E.;
RT "STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal
RT muscle triads.";
RL Sci. Rep. 7:41003-41003(2017).
RN [5]
RP FUNCTION, INTERACTION WITH CACNA1S, AND SUBCELLULAR LOCATION.
RX PubMed=29467163; DOI=10.1085/jgp.201711917;
RA Polster A., Nelson B.R., Papadopoulos S., Olson E.N., Beam K.G.;
RT "STAC proteins associate with the critical domain for excitation-
RT contraction coupling in the II-III loop of CaV1.1.";
RL J. Gen. Physiol. 150:613-624(2018).
RN [6]
RP FUNCTION, INTERACTION WITH CACNA1C, AND SUBCELLULAR LOCATION.
RX PubMed=29363593; DOI=10.1073/pnas.1715997115;
RA Campiglio M., Coste de Bagneaux P., Ortner N.J., Tuluc P., Van Petegem F.,
RA Flucher B.E.;
RT "STAC proteins associate to the IQ domain of CaV1.2 and inhibit calcium-
RT dependent inactivation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1376-1381(2018).
CC -!- FUNCTION: Promotes expression of the ion channel CACNA1H at the cell
CC membrane, and thereby contributes to the regulation of channel activity
CC (PubMed:27149520). Plays a minor and redundant role in promoting the
CC expression of calcium channel CACNA1S at the cell membrane, and thereby
CC contributes to increased channel activity (PubMed:29467163). Slows the
CC rate of calcium-mediated inactivation of CACNA1C calcium channel
CC activity (PubMed:29363593). {ECO:0000269|PubMed:27149520,
CC ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}.
CC -!- SUBUNIT: Interacts (via SH3 domains) with CACNA1S (PubMed:29467163).
CC Interacts with CACNA1H (PubMed:27149520). Interacts with CACNA1C
CC (Probable) (PubMed:29363593). {ECO:0000269|PubMed:27149520,
CC ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163,
CC ECO:0000305|PubMed:28112192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192,
CC ECO:0000269|PubMed:29467163}. Cell membrane
CC {ECO:0000269|PubMed:29467163}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29467163}; Cytoplasmic side
CC {ECO:0000269|PubMed:29467163}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:29363593}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29363593}; Cytoplasmic side
CC {ECO:0000269|PubMed:29363593}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain (PubMed:8954993,
CC PubMed:23818578) Detected in brain neurons, more specifically in
CC hippocampus, cerebellum and inferior olive (PubMed:8954993). Highly
CC expressed in urinary bladder, and detected at lower levels in adrenal
CC gland (PubMed:23818578). Detected at very low levels in heart, liver,
CC lung and kidney (PubMed:8954993). {ECO:0000269|PubMed:23818578,
CC ECO:0000269|PubMed:8954993}.
CC -!- DEVELOPMENTAL STAGE: Expression in brain started at late 13.5 dpc and
CC continued to adult (8W) with a peak around P10.
CC {ECO:0000269|PubMed:8954993}.
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DR EMBL; D86639; BAA13151.1; -; mRNA.
DR CCDS; CCDS23586.1; -.
DR PIR; JC5269; JC5269.
DR RefSeq; NP_058549.1; NM_016853.3.
DR AlphaFoldDB; P97306; -.
DR SMR; P97306; -.
DR STRING; 10090.ENSMUSP00000035083; -.
DR iPTMnet; P97306; -.
DR PhosphoSitePlus; P97306; -.
DR PaxDb; P97306; -.
DR PRIDE; P97306; -.
DR ProteomicsDB; 258653; -.
DR Antibodypedia; 28130; 170 antibodies from 25 providers.
DR DNASU; 20840; -.
DR Ensembl; ENSMUST00000035083; ENSMUSP00000035083; ENSMUSG00000032502.
DR GeneID; 20840; -.
DR KEGG; mmu:20840; -.
DR UCSC; uc009rvw.1; mouse.
DR CTD; 6769; -.
DR MGI; MGI:1201400; Stac.
DR VEuPathDB; HostDB:ENSMUSG00000032502; -.
DR eggNOG; ENOG502QW0M; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_2_0_1; -.
DR InParanoid; P97306; -.
DR OMA; HHKCADG; -.
DR OrthoDB; 584382at2759; -.
DR PhylomeDB; P97306; -.
DR TreeFam; TF332878; -.
DR BioGRID-ORCS; 20840; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Stac; mouse.
DR PRO; PR:P97306; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P97306; protein.
DR Bgee; ENSMUSG00000032502; Expressed in lumbar dorsal root ganglion and 85 other tissues.
DR ExpressionAtlas; P97306; baseline and differential.
DR Genevisible; P97306; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
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; IPR035508; STAC1.
DR InterPro; IPR039688; STAC1/2/3.
DR PANTHER; PTHR15135; PTHR15135; 1.
DR PANTHER; PTHR15135:SF3; PTHR15135:SF3; 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; 1.
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..403
FT /note="SH3 and cysteine-rich domain-containing protein"
FT /id="PRO_0000072236"
FT DOMAIN 286..345
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 348..403
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 108..160
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 44319 MW; 2B6CAEBFBCFF9982 CRC64;
MIPPSGARED SGDGLTGEAT GTEQPPSPAS TSSLESKLQK LKRSLSFKTK SLRSKSADNF
FPRTNSDVKP QADLLAKASP GPSPIAIPGS PASMPTKAGL HPGSNSKLHA FQEHVFKKPT
FCDVCNHMIV GTHAKHGLRC GACKMSIHHK CADGLAPQRC MGKLPKGFRR YYSSPLLIHE
QFGCIKEVMP IACGNKVDPV YEALRFGTSL AQRTKKGGSG SGSDSPPRTS TSELVDVPEE
ADGPGDGSDM RTRSNSVFTY PENGMDDFRD QMKTTNHQGP LSKDPLQMNT YVALYRFIPQ
ENEDLEMRPG DMITLLEDSN EDWWKGKIQD RVGFFPANFV QRVEEHEKIY RCVRTFIGCK
DQGQITLKEN QICVTSEEEQ DGFIRVLSGK KRGLVPLDVL VDV
