STAC3_HUMAN
ID STAC3_HUMAN Reviewed; 364 AA.
AC Q96MF2; B4DUK9; Q96HU5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=SH3 and cysteine-rich domain-containing protein 3;
GN Name=STAC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [5]
RP FUNCTION, VARIANT MYPBB SER-284, AND INVOLVEMENT IN MYPBB.
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).
RN [6]
RP STRUCTURE BY NMR OF 80-142.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-051, a C1 domain of STAC3 from human
RT cDNA.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [7] {ECO:0007744|PDB:6B29}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 309-364, FUNCTION, INTERACTION
RP WITH CACNA1S, AND CHARACTERIZATION OF VARIANT MYPBB SER-284.
RX PubMed=29078335; DOI=10.1073/pnas.1708852114;
RA Wong King Yuen S.M., Campiglio M., Tung C.C., Flucher B.E., Van Petegem F.;
RT "Structural insights into binding of STAC proteins to voltage-gated calcium
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E9520-E9528(2017).
RN [8]
RP VARIANT MYPBB SER-284, AND INVOLVEMENT IN MYPBB.
RX PubMed=28777491; DOI=10.1002/ajmg.a.38375;
RG Moebius Syndrome Research Consortium;
RA Telegrafi A., Webb B.D., Robbins S.M., Speck-Martins C.E., FitzPatrick D.,
RA Fleming L., Redett R., Dufke A., Houge G., van Harssel J.J.T., Verloes A.,
RA Robles A., Manoli I., Engle E.C., Jabs E.W., Valle D., Carey J.,
RA Hoover-Fong J.E., Sobreira N.L.M.;
RT "Identification of STAC3 variants in non-Native American families with
RT overlapping features of Carey-Fineman-Ziter syndrome and Moebius
RT syndrome.";
RL Am. J. Med. Genet. A 173:2763-2771(2017).
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 (PubMed:23736855, PubMed:29078335). Increases CACNA1S channel activity,
CC in addition to its role in enhancing the expression of CACNA1S at the
CC cell membrane. Has a redundant role in promoting the expression of the
CC calcium channel CACNA1S at the cell membrane (By similarity). Slows
CC down the inactivation rate of the calcium channel CACNA1C
CC (PubMed:29078335). {ECO:0000250|UniProtKB:Q8BZ71,
CC ECO:0000269|PubMed:23736855, ECO:0000269|PubMed:29078335}.
CC -!- SUBUNIT: Interacts (via SH3 domains) with the calcium channels CACNA1S
CC and CACNA1C (PubMed:29078335). Component of a calcium channel complex
CC with CACNA1S and CACNB1. Component of a calcium channel complex with
CC CACNA1C and CACNB1 (By similarity). {ECO:0000250|UniProtKB:Q8BZ71,
CC ECO:0000269|PubMed:29078335}.
CC -!- INTERACTION:
CC Q96MF2; A1A5B0: ANKRD36; NbExp=3; IntAct=EBI-745680, EBI-14100900;
CC Q96MF2; Q9UIF8-2: BAZ2B; NbExp=3; IntAct=EBI-745680, EBI-10321972;
CC Q96MF2; P68400: CSNK2A1; NbExp=7; IntAct=EBI-745680, EBI-347804;
CC Q96MF2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-745680, EBI-742054;
CC Q96MF2; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-745680, EBI-10233719;
CC Q96MF2; Q96JC9: EAF1; NbExp=5; IntAct=EBI-745680, EBI-769261;
CC Q96MF2; Q9H0I2: ENKD1; NbExp=4; IntAct=EBI-745680, EBI-744099;
CC Q96MF2; Q86V42: FAM124A; NbExp=3; IntAct=EBI-745680, EBI-744506;
CC Q96MF2; Q8N9E0: FAM133A; NbExp=6; IntAct=EBI-745680, EBI-10268158;
CC Q96MF2; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-745680, EBI-6658203;
CC Q96MF2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-745680, EBI-8468186;
CC Q96MF2; Q92914: FGF11; NbExp=3; IntAct=EBI-745680, EBI-11987787;
CC Q96MF2; P61328-2: FGF12; NbExp=3; IntAct=EBI-745680, EBI-10699759;
CC Q96MF2; O95995: GAS8; NbExp=3; IntAct=EBI-745680, EBI-1052570;
CC Q96MF2; O75420: GIGYF1; NbExp=3; IntAct=EBI-745680, EBI-947774;
CC Q96MF2; Q14451-3: GRB7; NbExp=3; IntAct=EBI-745680, EBI-11991632;
CC Q96MF2; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-745680, EBI-7261162;
CC Q96MF2; Q9C086: INO80B; NbExp=3; IntAct=EBI-745680, EBI-715611;
CC Q96MF2; Q969R5: L3MBTL2; NbExp=6; IntAct=EBI-745680, EBI-739909;
CC Q96MF2; Q8N8X9: MAB21L3; NbExp=7; IntAct=EBI-745680, EBI-10268010;
CC Q96MF2; P55081: MFAP1; NbExp=3; IntAct=EBI-745680, EBI-1048159;
CC Q96MF2; Q9BU76: MMTAG2; NbExp=5; IntAct=EBI-745680, EBI-742459;
CC Q96MF2; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-745680, EBI-3920396;
CC Q96MF2; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-745680, EBI-10180231;
CC Q96MF2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-745680, EBI-25882629;
CC Q96MF2; P35268: RPL22; NbExp=3; IntAct=EBI-745680, EBI-354533;
CC Q96MF2; P32969: RPL9P9; NbExp=3; IntAct=EBI-745680, EBI-358122;
CC Q96MF2; P62851: RPS25; NbExp=3; IntAct=EBI-745680, EBI-353054;
CC Q96MF2; P00441: SOD1; NbExp=3; IntAct=EBI-745680, EBI-990792;
CC Q96MF2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-745680, EBI-12023934;
CC Q96MF2; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-745680, EBI-12037215;
CC Q96MF2; Q8N9Q2: SREK1IP1; NbExp=6; IntAct=EBI-745680, EBI-10268630;
CC Q96MF2; Q96MF2: STAC3; NbExp=6; IntAct=EBI-745680, EBI-745680;
CC Q96MF2; Q15560: TCEA2; NbExp=3; IntAct=EBI-745680, EBI-710310;
CC Q96MF2; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-745680, EBI-752102;
CC Q96MF2; P26368-2: U2AF2; NbExp=3; IntAct=EBI-745680, EBI-11097439;
CC Q96MF2; Q3SXR9: VCX2; NbExp=3; IntAct=EBI-745680, EBI-11983741;
CC Q96MF2; Q8TBK6: ZCCHC10; NbExp=7; IntAct=EBI-745680, EBI-597063;
CC Q96MF2; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-745680, EBI-3439227;
CC Q96MF2; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-745680, EBI-10183064;
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}. Note=Co-localizes with CACNA1S and
CC CACNA1C on T-tubules. {ECO:0000250|UniProtKB:Q8BZ71}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96MF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MF2-2; Sequence=VSP_017914;
CC Name=3;
CC IsoId=Q96MF2-3; Sequence=VSP_055272;
CC -!- DISEASE: Myopathy, congenital, Bailey-Bloch (MYPBB) [MIM:255995]: An
CC autosomal recessive disease characterized by congenital weakness and
CC arthrogryposis, cleft palate, ptosis, short stature, kyphoscoliosis,
CC talipes deformities, and susceptibility to malignant hyperthermia
CC provoked by anesthesia. {ECO:0000269|PubMed:23736855,
CC ECO:0000269|PubMed:28777491, ECO:0000269|PubMed:29078335}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AK057013; BAB71343.1; -; mRNA.
DR EMBL; AK300688; BAG62371.1; -; mRNA.
DR EMBL; AC137834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97005.1; -; Genomic_DNA.
DR EMBL; BC008069; AAH08069.1; -; mRNA.
DR CCDS; CCDS66405.1; -. [Q96MF2-3]
DR CCDS; CCDS66406.1; -. [Q96MF2-2]
DR CCDS; CCDS8936.1; -. [Q96MF2-1]
DR RefSeq; NP_001273185.1; NM_001286256.1. [Q96MF2-2]
DR RefSeq; NP_001273186.1; NM_001286257.1. [Q96MF2-3]
DR RefSeq; NP_659501.1; NM_145064.2. [Q96MF2-1]
DR RefSeq; XP_011536428.1; XM_011538126.2. [Q96MF2-1]
DR PDB; 2DB6; NMR; -; A=80-140.
DR PDB; 6B29; X-ray; 1.30 A; A/B/C/D=309-364.
DR PDB; 6UY7; X-ray; 2.10 A; A=245-364.
DR PDB; 6UY8; X-ray; 1.65 A; A/B=245-364.
DR PDB; 6UY9; X-ray; 1.60 A; A=245-364.
DR PDBsum; 2DB6; -.
DR PDBsum; 6B29; -.
DR PDBsum; 6UY7; -.
DR PDBsum; 6UY8; -.
DR PDBsum; 6UY9; -.
DR AlphaFoldDB; Q96MF2; -.
DR SMR; Q96MF2; -.
DR BioGRID; 128899; 45.
DR IntAct; Q96MF2; 44.
DR MINT; Q96MF2; -.
DR STRING; 9606.ENSP00000329200; -.
DR iPTMnet; Q96MF2; -.
DR PhosphoSitePlus; Q96MF2; -.
DR BioMuta; STAC3; -.
DR DMDM; 74732360; -.
DR jPOST; Q96MF2; -.
DR MassIVE; Q96MF2; -.
DR PaxDb; Q96MF2; -.
DR PeptideAtlas; Q96MF2; -.
DR PRIDE; Q96MF2; -.
DR ProteomicsDB; 5195; -.
DR ProteomicsDB; 77345; -. [Q96MF2-1]
DR ProteomicsDB; 77346; -. [Q96MF2-2]
DR Antibodypedia; 28547; 91 antibodies from 24 providers.
DR DNASU; 246329; -.
DR Ensembl; ENST00000332782.7; ENSP00000329200.2; ENSG00000185482.8. [Q96MF2-1]
DR Ensembl; ENST00000546246.2; ENSP00000441515.2; ENSG00000185482.8. [Q96MF2-3]
DR Ensembl; ENST00000554578.5; ENSP00000452068.1; ENSG00000185482.8. [Q96MF2-2]
DR GeneID; 246329; -.
DR KEGG; hsa:246329; -.
DR MANE-Select; ENST00000332782.7; ENSP00000329200.2; NM_145064.3; NP_659501.1.
DR UCSC; uc001snp.4; human. [Q96MF2-1]
DR CTD; 246329; -.
DR DisGeNET; 246329; -.
DR GeneCards; STAC3; -.
DR GeneReviews; STAC3; -.
DR HGNC; HGNC:28423; STAC3.
DR HPA; ENSG00000185482; Group enriched (skeletal muscle, tongue).
DR MalaCards; STAC3; -.
DR MIM; 255995; phenotype.
DR MIM; 615521; gene.
DR neXtProt; NX_Q96MF2; -.
DR OpenTargets; ENSG00000185482; -.
DR Orphanet; 168572; Native American myopathy.
DR PharmGKB; PA134877600; -.
DR VEuPathDB; HostDB:ENSG00000185482; -.
DR eggNOG; ENOG502QT6I; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_1_1_1; -.
DR InParanoid; Q96MF2; -.
DR OMA; DQQYACV; -.
DR PhylomeDB; Q96MF2; -.
DR TreeFam; TF332878; -.
DR PathwayCommons; Q96MF2; -.
DR SignaLink; Q96MF2; -.
DR BioGRID-ORCS; 246329; 17 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; Q96MF2; -.
DR GenomeRNAi; 246329; -.
DR Pharos; Q96MF2; Tbio.
DR PRO; PR:Q96MF2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96MF2; protein.
DR Bgee; ENSG00000185482; Expressed in gastrocnemius and 113 other tissues.
DR ExpressionAtlas; Q96MF2; baseline and differential.
DR Genevisible; Q96MF2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP: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; IMP:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR CDD; cd00029; C1; 1.
DR CDD; cd11986; SH3_Stac3_1; 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; IPR035736; Stac3_SH3_1.
DR PANTHER; PTHR15135; PTHR15135; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Disease variant; Membrane; Metal-binding; Reference proteome; Repeat;
KW SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="SH3 and cysteine-rich domain-containing protein 3"
FT /id="PRO_0000232582"
FT DOMAIN 247..306
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 307..364
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 89..140
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..186
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055272"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017914"
FT VARIANT 284
FT /note="W -> S (in MYPBB; loss of interaction with CACNA1S;
FT dbSNP:rs140291094)"
FT /evidence="ECO:0000269|PubMed:23736855,
FT ECO:0000269|PubMed:28777491, ECO:0000269|PubMed:29078335"
FT /id="VAR_071313"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2DB6"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2DB6"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2DB6"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2DB6"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2DB6"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2DB6"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2DB6"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2DB6"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6UY9"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6UY9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6B29"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6B29"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:6B29"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6B29"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:6B29"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6B29"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6B29"
SQ SEQUENCE 364 AA; 41507 MW; 9464C4F035FEDB98 CRC64;
MTEKEVLESP KPSFPAETRQ SGLQRLKQLL RKGSTGTKEM ELPPEPQANG EAVGAGGGPI
YYIYEEEEEE EEEEEEPPPE PPKLVNDKPH KFKDHFFKKP KFCDVCARMI VLNNKFGLRC
KNCKTNIHEH CQSYVEMQRC FGKIPPGFHR AYSSPLYSNQ QYACVKDLSA ANRNDPVFET
LRTGVIMANK ERKKGQADKK NPVAAMMEEE PESARPEEGK PQDGNPEGDK KAEKKTPDDK
HKQPGFQQSH YFVALYRFKA LEKDDLDFPP GEKITVIDDS NEEWWRGKIG EKVGFFPPNF
IIRVRAGERV HRVTRSFVGN REIGQITLKK DQIVVQKGDE AGGYVKVYTG RKVGLFPTDF
LEEI
