ID   STAC_BOVIN              Reviewed;         403 AA.
AC   A0JNJ1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. Interacts with
CC       CACNA1H. Interacts with CACNA1C. {ECO:0000250|UniProtKB:P97306}.
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; BC126707; AAI26708.1; -; mRNA.
DR   RefSeq; NP_001071430.1; NM_001077962.2.
DR   AlphaFoldDB; A0JNJ1; -.
DR   SMR; A0JNJ1; -.
DR   STRING; 9913.ENSBTAP00000008854; -.
DR   PaxDb; A0JNJ1; -.
DR   Ensembl; ENSBTAT00000008854; ENSBTAP00000008854; ENSBTAG00000006735.
DR   GeneID; 524215; -.
DR   KEGG; bta:524215; -.
DR   CTD; 6769; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006735; -.
DR   VGNC; VGNC:35350; STAC.
DR   eggNOG; ENOG502QW0M; Eukaryota.
DR   GeneTree; ENSGT00950000183092; -.
DR   InParanoid; A0JNJ1; -.
DR   OMA; HHKCADG; -.
DR   OrthoDB; 584382at2759; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000006735; Expressed in urethra and 98 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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: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: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; 2.
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   2: Evidence at transcript 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_0000274412"
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..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..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;  44487 MW;  EA90A0E47DCBD9FB CRC64;
     MIPPSGARED GVDGLPKETA SAEQPPSPAS TGSQESKLQK LKRSLSFKTK SLRSKSADNF
     FQRTNSDVKL QADVLAGVSP GSSPLPAPGS LTCTPTRAGL YPGGGGKAHA FQEHIFKKPT
     FCDVCNHMIV GTNAKHGLRC KACKMSIHHK CMDGLAPQRC MGKLPKGFRR YYSSPLLIHE
     QFGCIKEVMP IACGNKVDPV YETLRFGTSL AQRTKKSSSG SGSDSPHRTS TSDLVEVPEE
     ADGPGDGYDL RKRSNSVFTY PENGTDDFRD QAKNINHQGP LSKDPLQMNT YVALYKFVPQ
     ENEDLEMRPG DMITLLEDSN EDWWKGKIQD RIGFFPANFV QRVHQNEKIF RCVRTFSGCK
     EQGQITLKEN QICVASEEEQ DGFIRVLSGK KRGLVPLDVL ENI