STAC2_MOUSE
ID STAC2_MOUSE Reviewed; 408 AA.
AC Q8R1B0; Q8BV93; Q8K2U4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=SH3 and cysteine-rich domain-containing protein 2;
DE AltName: Full=24b2/STAC2 {ECO:0000303|Ref.1};
DE AltName: Full=Src homology 3 and cysteine-rich domain-containing protein 2;
GN Name=Stac2;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Rossner M., Faucheron N., Wuerz R., von Ahsen O., Kammandel B.,
RA Schwaninger M., Schneider A.;
RT "Cloning of 24b2/STAC2, a novel STAC-homologous gene up-regulated in
RT cerebral ischemia in mice.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25548159; DOI=10.1073/pnas.1423113112;
RA Polster A., Perni S., Bichraoui H., Beam K.G.;
RT "Stac adaptor proteins regulate trafficking and function of muscle and
RT neuronal L-type Ca2+ channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:602-606(2015).
RN [7]
RP SUBCELLULAR LOCATION.
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH CACNA1C.
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: Plays a redundant role in promoting the expression of calcium
CC channel CACNA1S at the cell membrane, and thereby contributes to
CC increased channel activity (PubMed:29467163). Slows down the
CC inactivation rate of the calcium channel CACNA1C (PubMed:25548159,
CC PubMed:29363593). {ECO:0000269|PubMed:25548159,
CC ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}.
CC -!- SUBUNIT: Interacts (via SH3 domains) with CACNA1S (PubMed:29467163).
CC Interacts (via SH3 domains) with CACNA1C (PubMed:29363593). Has much
CC lower affinity for CACNA1C than for CACNA1S (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZMT1, ECO:0000269|PubMed:29363593,
CC ECO:0000269|PubMed:29467163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192,
CC ECO:0000269|PubMed:29467163}. Cell membrane
CC {ECO:0000269|PubMed:25548159}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25548159}; Cytoplasmic side
CC {ECO:0000305|PubMed:25548159}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:29467163}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29467163}; Cytoplasmic side
CC {ECO:0000269|PubMed:29467163}. Note=Colocalizes with CACNA1C at the
CC plasma membrane of transfected cells. {ECO:0000269|PubMed:25548159}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum, forebrain and midbrain, and
CC in the eye. {ECO:0000269|PubMed:23818578}.
CC -!- MISCELLANEOUS: Up-regulated in cerebral ischemia.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ608761; CAE75538.1; -; mRNA.
DR EMBL; AK078132; BAC37142.1; -; mRNA.
DR EMBL; AK079357; BAC37621.1; -; mRNA.
DR EMBL; AK144433; BAE25886.1; -; mRNA.
DR EMBL; BC024864; AAH24864.1; -; mRNA.
DR EMBL; BC029794; AAH29794.1; -; mRNA.
DR CCDS; CCDS25338.1; -.
DR RefSeq; NP_666140.1; NM_146028.4.
DR AlphaFoldDB; Q8R1B0; -.
DR SMR; Q8R1B0; -.
DR STRING; 10090.ENSMUSP00000017544; -.
DR iPTMnet; Q8R1B0; -.
DR PhosphoSitePlus; Q8R1B0; -.
DR PaxDb; Q8R1B0; -.
DR PeptideAtlas; Q8R1B0; -.
DR PRIDE; Q8R1B0; -.
DR ProteomicsDB; 254577; -.
DR Antibodypedia; 2798; 162 antibodies from 25 providers.
DR DNASU; 217154; -.
DR Ensembl; ENSMUST00000017544; ENSMUSP00000017544; ENSMUSG00000017400.
DR GeneID; 217154; -.
DR KEGG; mmu:217154; -.
DR UCSC; uc007lfl.1; mouse.
DR CTD; 342667; -.
DR MGI; MGI:2144518; Stac2.
DR VEuPathDB; HostDB:ENSMUSG00000017400; -.
DR eggNOG; ENOG502QW9G; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_0_0_1; -.
DR InParanoid; Q8R1B0; -.
DR OMA; ICVGVGK; -.
DR OrthoDB; 584382at2759; -.
DR PhylomeDB; Q8R1B0; -.
DR TreeFam; TF332878; -.
DR BioGRID-ORCS; 217154; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Stac2; mouse.
DR PRO; PR:Q8R1B0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R1B0; protein.
DR Bgee; ENSMUSG00000017400; Expressed in superior frontal gyrus and 95 other tissues.
DR ExpressionAtlas; Q8R1B0; baseline and differential.
DR Genevisible; Q8R1B0; 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:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR CDD; cd11985; SH3_Stac2_C; 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 InterPro; IPR035509; Stac2_SH3.
DR PANTHER; PTHR15135; PTHR15135; 1.
DR Pfam; PF00130; C1_1; 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; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..408
FT /note="SH3 and cysteine-rich domain-containing protein 2"
FT /id="PRO_0000274414"
FT DOMAIN 289..348
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 351..408
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 110..161
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 93
FT /note="P -> S (in Ref. 1; BAC37621)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> E (in Ref. 2; AAH29794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44793 MW; 58D275A654EE4CCA CRC64;
MTEMSEKENE PDDAATHTPP GTVSTLQETK LQRFKRSLSL KTILRSKSVE NFFLRSGSEL
KCPTEVLLTP PTPLPPPSPP PASTDRGLPT PTPSPCPVPR PLAPLKPVRL HSFQEHVFKR
ASPCELCHQL IVGNSKQGLR CKTCKVSVHL WCSEEISHQQ CPGKTSTSFR RNFSSPLLVH
APPPACAMNK ESPPTGTSGK VDPVYETLRY GTSLALMNRS SFSSTSESPT RSLSERDELT
EDGEGSIRSS EEGPGDSVFT APAESEGSGP EEKSPGQQPP KLPLRKDVGP MYSYVALYKF
LPQENNDLAL QPGDRIMLVD DSNEDWWKGK IGDRVGFFPA NFVQRVRPGE NVWRCCQPFS
GNKEQGYMSL KENQICVGVS RSKDSDGFIR VSSGKKRGLV PADSLAEI
