STAC_HUMAN
ID STAC_HUMAN Reviewed; 402 AA.
AC Q99469; B2R8S8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
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; Synonyms=STAC1 {ECO:0000303|PubMed:29078335};
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 [MRNA].
RC 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 STRUCTURE BY NMR OF 288-342.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first SH3 domain of STAC protein.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [5] {ECO:0007744|PDB:6B25}
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 288-402, AND INTERACTION WITH
RP CACNA1S.
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).
CC -!- FUNCTION: Promotes expression of the ion channel CACNA1H at the cell
CC membrane, and thereby contributes to the regulation of channel
CC activity. Plays a minor and redundant role in promoting the expression
CC of calcium channel CACNA1S at the cell membrane, and thereby
CC contributes to increased channel activity. Slows down the inactivation
CC rate of the calcium channel CACNA1C. {ECO:0000250|UniProtKB:P97306}.
CC -!- SUBUNIT: Interacts (via SH3 domains) with CACNA1S (PubMed:29078335).
CC Interacts with CACNA1H. Interacts with CACNA1C (By similarity).
CC {ECO:0000250|UniProtKB:P97306, ECO:0000269|PubMed:29078335}.
CC -!- INTERACTION:
CC Q99469; Q86V38: ATN1; NbExp=3; IntAct=EBI-2652799, EBI-11954292;
CC Q99469; P22607: FGFR3; NbExp=3; IntAct=EBI-2652799, EBI-348399;
CC Q99469; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2652799, EBI-618309;
CC Q99469; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2652799, EBI-2556193;
CC Q99469; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-2652799, EBI-10181113;
CC Q99469; Q92876: KLK6; NbExp=3; IntAct=EBI-2652799, EBI-2432309;
CC Q99469; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2652799, EBI-741037;
CC Q99469; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2652799, EBI-16439278;
CC Q99469; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-2652799, EBI-10963850;
CC Q99469; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2652799, EBI-22310682;
CC Q99469; Q9UGN5: PARP2; NbExp=2; IntAct=EBI-2652799, EBI-2795348;
CC Q99469; Q02548: PAX5; NbExp=3; IntAct=EBI-2652799, EBI-296331;
CC Q99469; P26367: PAX6; NbExp=3; IntAct=EBI-2652799, EBI-747278;
CC Q99469; P78424: POU6F2; NbExp=3; IntAct=EBI-2652799, EBI-12029004;
CC Q99469; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-2652799, EBI-751555;
CC Q99469; P51692: STAT5B; NbExp=3; IntAct=EBI-2652799, EBI-1186119;
CC Q99469; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2652799, EBI-741480;
CC Q99469; P62258: YWHAE; NbExp=3; IntAct=EBI-2652799, EBI-356498;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P97306}. Cell membrane
CC {ECO:0000250|UniProtKB:P97306}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P97306}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P97306}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P97306}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P97306}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P97306}.
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DR EMBL; D86640; BAA13152.1; -; mRNA.
DR EMBL; AK313493; BAG36275.1; -; mRNA.
DR EMBL; CH471055; EAW64474.1; -; Genomic_DNA.
DR CCDS; CCDS2662.1; -.
DR PIR; JC5270; JC5270.
DR RefSeq; NP_003140.1; NM_003149.2.
DR PDB; 2DL4; NMR; -; A=288-342.
DR PDB; 6B25; X-ray; 2.39 A; A=288-402.
DR PDBsum; 2DL4; -.
DR PDBsum; 6B25; -.
DR AlphaFoldDB; Q99469; -.
DR BMRB; Q99469; -.
DR SMR; Q99469; -.
DR BioGRID; 112646; 30.
DR IntAct; Q99469; 26.
DR MINT; Q99469; -.
DR STRING; 9606.ENSP00000273183; -.
DR TCDB; 8.A.34.1.2; the endophilin (endophilin) family.
DR iPTMnet; Q99469; -.
DR PhosphoSitePlus; Q99469; -.
DR BioMuta; STAC; -.
DR DMDM; 12229989; -.
DR MassIVE; Q99469; -.
DR PaxDb; Q99469; -.
DR PeptideAtlas; Q99469; -.
DR PRIDE; Q99469; -.
DR ProteomicsDB; 78285; -.
DR Antibodypedia; 28130; 170 antibodies from 25 providers.
DR DNASU; 6769; -.
DR Ensembl; ENST00000273183.8; ENSP00000273183.3; ENSG00000144681.11.
DR GeneID; 6769; -.
DR KEGG; hsa:6769; -.
DR MANE-Select; ENST00000273183.8; ENSP00000273183.3; NM_003149.3; NP_003140.1.
DR UCSC; uc003cgh.2; human.
DR CTD; 6769; -.
DR DisGeNET; 6769; -.
DR GeneCards; STAC; -.
DR HGNC; HGNC:11353; STAC.
DR HPA; ENSG00000144681; Tissue enhanced (prostate).
DR MIM; 602317; gene.
DR neXtProt; NX_Q99469; -.
DR OpenTargets; ENSG00000144681; -.
DR PharmGKB; PA36175; -.
DR VEuPathDB; HostDB:ENSG00000144681; -.
DR eggNOG; ENOG502QW0M; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_2_0_1; -.
DR InParanoid; Q99469; -.
DR OMA; HHKCADG; -.
DR OrthoDB; 584382at2759; -.
DR PhylomeDB; Q99469; -.
DR TreeFam; TF332878; -.
DR PathwayCommons; Q99469; -.
DR SignaLink; Q99469; -.
DR BioGRID-ORCS; 6769; 7 hits in 1058 CRISPR screens.
DR ChiTaRS; STAC; human.
DR EvolutionaryTrace; Q99469; -.
DR GenomeRNAi; 6769; -.
DR Pharos; Q99469; Tbio.
DR PRO; PR:Q99469; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q99469; protein.
DR Bgee; ENSG00000144681; Expressed in dorsal root ganglion and 143 other tissues.
DR ExpressionAtlas; Q99469; baseline and differential.
DR Genevisible; Q99469; HS.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:2001259; P:positive regulation of cation channel activity; 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:0007165; P:signal transduction; NAS:UniProtKB.
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 3D-structure; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Reference proteome; Repeat; SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="SH3 and cysteine-rich domain-containing protein"
FT /id="PRO_0000072235"
FT DOMAIN 285..344
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 347..402
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 107..159
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 262
FT /note="N -> S (in dbSNP:rs7634545)"
FT /id="VAR_034505"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:6B25"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:6B25"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:6B25"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:6B25"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6B25"
SQ SEQUENCE 402 AA; 44554 MW; 211688D178E4F905 CRC64;
MIPPSSPRED GVDGLPKEAV GAEQPPSPAS TSSQESKLQK LKRSLSFKTK SLRSKSADNF
FQRTNSEDMK LQAHMVAEIS PSSSPLPAPG SLTSTPARAG LHPGGKAHAF QEYIFKKPTF
CDVCNHMIVG TNAKHGLRCK ACKMSIHHKC TDGLAPQRCM GKLPKGFRRY YSSPLLIHEQ
FGCIKEVMPI ACGNKVDPVY ETLRFGTSLA QRTKKGSSGS GSDSPHRTST SDLVEVPEEA
NGPGGGYDLR KRSNSVFTYP ENGTDDFRDP AKNINHQGSL SKDPLQMNTY VALYKFVPQE
NEDLEMRPGD IITLLEDSNE DWWKGKIQDR IGFFPANFVQ RLQQNEKIFR CVRTFIGCKE
QGQITLKENQ ICVSSEEEQD GFIRVLSGKK KGLIPLDVLE NI
