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SH3 and cysteine-rich domain-containing protein 3

 STAC3_MOUSE             Reviewed;         360 AA.
Q8BZ71;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
18-JUL-2018, entry version 111.
RecName: Full=SH3 and cysteine-rich domain-containing protein 3;
Name=Stac3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Jaw, and Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=23626854; DOI=10.1371/journal.pone.0062760;
Reinholt B.M., Ge X., Cong X., Gerrard D.E., Jiang H.;
"Stac3 is a novel regulator of skeletal muscle development in mice.";
PLoS ONE 8:E62760-E62760(2013).
[4]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
STAGE, AND TISSUE SPECIFICITY.
PubMed=23818578; DOI=10.1073/pnas.1310571110;
Nelson B.R., Wu F., Liu Y., Anderson D.M., McAnally J., Lin W.,
Cannon S.C., Bassel-Duby R., Olson E.N.;
"Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-
induced Ca2+ release and contractility.";
Proc. Natl. Acad. Sci. U.S.A. 110:11881-11886(2013).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25548159; DOI=10.1073/pnas.1423113112;
Polster A., Perni S., Bichraoui H., Beam K.G.;
"Stac adaptor proteins regulate trafficking and function of muscle and
neuronal L-type Ca2+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 112:602-606(2015).
[6]
FUNCTION, AND MUTAGENESIS OF TRP-280.
PubMed=27621462; DOI=10.1073/pnas.1612441113;
Polster A., Nelson B.R., Olson E.N., Beam K.G.;
"Stac3 has a direct role in skeletal muscle-type excitation-
contraction coupling that is disrupted by a myopathy-causing
mutation.";
Proc. Natl. Acad. Sci. U.S.A. 113:10986-10991(2016).
[7]
SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH
CACNA1S AND CACNA1C, AND MUTAGENESIS OF VAL-104 AND TYR-133.
PubMed=28112192; DOI=10.1038/srep41003;
Campiglio M., Flucher B.E.;
"STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal
muscle triads.";
Sci. Rep. 7:41003-41003(2017).
[8]
FUNCTION, INTERACTION WITH CACNA1S, AND SUBCELLULAR LOCATION.
PubMed=29467163; DOI=10.1085/jgp.201711917;
Polster A., Nelson B.R., Papadopoulos S., Olson E.N., Beam K.G.;
"STAC proteins associate with the critical domain for excitation-
contraction coupling in the II-III loop of CaV1.1.";
J. Gen. Physiol. 150:613-624(2018).
[9]
FUNCTION, INTERACTION WITH CACNA1C, AND SUBCELLULAR LOCATION.
PubMed=29363593; DOI=10.1073/pnas.1715997115;
Campiglio M., Coste de Bagneaux P., Ortner N.J., Tuluc P.,
Van Petegem F., Flucher B.E.;
"STAC proteins associate to the IQ domain of CaV1.2 and inhibit
calcium-dependent inactivation.";
Proc. Natl. Acad. Sci. U.S.A. 115:1376-1381(2018).
-!- FUNCTION: Required for normal excitation-contraction coupling in
skeletal muscle and for normal muscle contraction in response to
membrane depolarization (PubMed:23818578, PubMed:27621462,
PubMed:29467163). Required for normal Ca(2+) release from the
sarcplasmic reticulum, which ultimately leads to muscle
contraction (PubMed:23818578). Probably functions via its effects
on muscle calcium channels. Increases CACNA1S channel activity, in
addition to its role in enhancing the expression of CACNA1S at the
cell membrane (PubMed:27621462). Has a redundant role in promoting
the expression of the calcium channel CACNA1S at the cell membrane
(PubMed:25548159, PubMed:27621462, PubMed:29467163). Slows down
the inactivation rate of the calcium channel CACNA1C
(PubMed:25548159, PubMed:29363593). {ECO:0000269|PubMed:23818578,
ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:27621462,
ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}.
-!- SUBUNIT: Interacts (via SH3 domains) with the calcium channels
CACNA1S and CACNA1C (PubMed:28112192, PubMed:29467163,
PubMed:29363593). Component of a calcium channel complex with
CACNA1S and CACNB1 (PubMed:28112192). Component of a calcium
channel complex with CACNA1C and CACNB1 (PubMed:28112192).
{ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29363593,
ECO:0000269|PubMed:29467163}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28112192,
ECO:0000269|PubMed:29467163}. Cell membrane, sarcolemma
{ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:28112192,
ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163,
ECO:0000305|PubMed:25548159}; Peripheral membrane protein
{ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163,
ECO:0000305|PubMed:25548159}; Cytoplasmic side
{ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163,
ECO:0000305|PubMed:25548159}. Note=Co-localizes with CACNA1S and
CACNA1C on T-tubules (extensions of the sarcolemma).
{ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:28112192,
ECO:0000269|PubMed:29363593}.
-!- TISSUE SPECIFICITY: Dected in skeletal muscle, including soleus,
extensor digitorum longus, tibialis anterior, quadriceps and
gastronemicus. Detected in tongue. {ECO:0000269|PubMed:23626854,
ECO:0000269|PubMed:23818578}.
-!- DEVELOPMENTAL STAGE: Detected in somites and limb buds at 9.5 and
13 dpc, in embryonic limb muscle and tongue (PubMed:23626854,
PubMed:23818578). Detected in tongue and diaphragm at 14.5 dpc
(PubMed:23818578). {ECO:0000269|PubMed:23626854,
ECO:0000269|PubMed:23818578}.
-!- DISRUPTION PHENOTYPE: Complete perinatal lethality, due to
paralysis and inability to breathe (PubMed:23626854,
PubMed:23818578). Embryos have a curved body with abnormal
curvature of the vertebral spine and drooping forelimbs
(PubMed:23626854, PubMed:23818578). They display multiple skeletal
abnormalities involving ribs, sternum and costal cartilage, and
strongly reduced formation of bone ridges at major muscle
attachment sites (PubMed:23818578). They weigh about 15% less than
wild-type at 18.5 dpc (PubMed:23626854). They do not move or
respond to touch, but have a beating heart when dissected out of
the uterus (PubMed:23626854). Their myofibers have altered
morphology with centrally located nuclei, unlike wild-type, where
the nuclei are located in the periphery of the myofibers
(PubMed:23626854, PubMed:23818578). Sarcomeres have streaming Z-
lines (PubMed:23626854). The diaphragm does not contract in
response to membrane depolarization or electric stimulation
(PubMed:23818578). Myotubes from mutant mice lack voltage-induced
calcium release from the sarcoplasmic reticulum (PubMed:23818578).
{ECO:0000269|PubMed:23626854, ECO:0000269|PubMed:23818578}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK036516; BAC29460.1; -; mRNA.
EMBL; BC067208; AAH67208.1; -; mRNA.
CCDS; CCDS24242.1; -.
RefSeq; NP_808375.1; NM_177707.3.
RefSeq; XP_006513703.1; XM_006513640.2.
RefSeq; XP_006513705.1; XM_006513642.2.
UniGene; Mm.32087; -.
ProteinModelPortal; Q8BZ71; -.
SMR; Q8BZ71; -.
STRING; 10090.ENSMUSP00000048148; -.
iPTMnet; Q8BZ71; -.
PhosphoSitePlus; Q8BZ71; -.
MaxQB; Q8BZ71; -.
PaxDb; Q8BZ71; -.
PRIDE; Q8BZ71; -.
Ensembl; ENSMUST00000035839; ENSMUSP00000048148; ENSMUSG00000040287.
Ensembl; ENSMUST00000160019; ENSMUSP00000125124; ENSMUSG00000040287.
GeneID; 237611; -.
KEGG; mmu:237611; -.
UCSC; uc007hjr.1; mouse.
CTD; 246329; -.
MGI; MGI:3606571; Stac3.
eggNOG; ENOG410IFB4; Eukaryota.
eggNOG; ENOG410YWV2; LUCA.
GeneTree; ENSGT00390000008822; -.
HOGENOM; HOG000230980; -.
HOVERGEN; HBG017859; -.
InParanoid; Q8BZ71; -.
OMA; KNSLAAM; -.
OrthoDB; EOG091G085P; -.
PhylomeDB; Q8BZ71; -.
TreeFam; TF332878; -.
PRO; PR:Q8BZ71; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000040287; -.
CleanEx; MM_STAC3; -.
ExpressionAtlas; Q8BZ71; baseline and differential.
Genevisible; Q8BZ71; MM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007274; P:neuromuscular synaptic transmission; ISS:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
GO; GO:0003009; P:skeletal muscle contraction; ISS:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
CDD; cd00029; C1; 1.
CDD; cd11986; SH3_Stac3_1; 1.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035736; Stac3_SH3_1.
Pfam; PF00130; C1_1; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 2.
PROSITE; PS50002; SH3; 2.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Membrane; Metal-binding;
Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
CHAIN 1 360 SH3 and cysteine-rich domain-containing
protein 3.
/FTId=PRO_0000232583.
DOMAIN 243 302 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 303 360 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 88 139 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
COMPBIAS 65 75 Poly-Glu.
MUTAGEN 104 104 V->L: Loss of co-localization with
CACNA1S and strongly decreased co-
localization with CACNA1C; when
associated with E-133.
{ECO:0000269|PubMed:28112192}.
MUTAGEN 133 133 Y->E: Loss of co-localization with
CACNA1S and strongly decreased co-
localization with CACNA1C; when
associated with L-104.
{ECO:0000269|PubMed:28112192}.
MUTAGEN 280 280 W->S: Loss of normal excitation-
contraction coupling. Loss of function in
enhancing calcium channel activity.
{ECO:0000269|PubMed:27621462}.
SEQUENCE 360 AA; 41000 MW; ADA948B421F5B0F8 CRC64;
MTEKEVVESP QPPFPGETPQ SGLQRLKQLF KKGSPETAEM EPPPEPQANG EAVGAGGGPI
YYIYEEEEEE EEEEEPPPEP PKLVNDKPHK FKDHFFKKPK FCDVCARMIV LNNKFGLRCK
NCKTNIHEHC QSYVEMQRCF GKIPPGFRRA YSSPLYSDQQ YAVSAANRND PVFETLRVGV
IMANKERKKG QADKKNPLAA MMEEEPESAR PEEGKSQDGN NAEKDKKAEK KTPDDKNKQP
GFQQSHYFVA LYRFKALEKD DLDFPPGEKI TVIDDSNEEW WRGKIGEKVG FFPPNFIIRV
RAGERVHRVT RSFVGNREIG QITLKKDQIV VQKGDEAGGY VKVYTGRKVG LFPTDFLEEI


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