ID W5MBH4_LEPOC Unreviewed; 409 AA.
AC W5MBH4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=SH3 and cysteine rich domain {ECO:0000313|Ensembl:ENSLOCP00000005733.1};
GN Name=STAC {ECO:0000313|Ensembl:ENSLOCP00000005733.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005733.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005733.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}.
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DR EMBL; AHAT01021981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01021982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01021983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01021984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01021985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015212663.1; XM_015357177.1.
DR AlphaFoldDB; W5MBH4; -.
DR STRING; 7918.ENSLOCP00000005733; -.
DR Ensembl; ENSLOCT00000005741.1; ENSLOCP00000005733.1; ENSLOCG00000004780.1.
DR GeneID; 102686771; -.
DR KEGG; loc:102686771; -.
DR CTD; 6769; -.
DR eggNOG; ENOG502QW0M; Eukaryota.
DR GeneTree; ENSGT00950000183092; -.
DR HOGENOM; CLU_048120_2_0_1; -.
DR InParanoid; W5MBH4; -.
DR OMA; IYRCVRT; -.
DR OrthoDB; 3716527at2759; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000004780; Expressed in heart and 4 other cell types or tissues.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR CDD; cd11833; SH3_Stac_1; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR035508; STAC1_SH3.
DR PANTHER; PTHR15135:SF3; SH3 AND CYSTEINE-RICH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR15135; STAC; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF16664; STAC2_u1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 108..160
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 292..351
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
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"
FT COMPBIAS 233..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 45865 MW; CC13962BEBD40ACA CRC64;
MIPPANMLEE DNIEKEKENE QEHDLPQSPA STVSQQESKL QKLKRSLSFK AKSLRSKSAD
NFFQRTNSDM KLQVDLLTGV STSTGQLTTS DSHISSPTKS LKQPDTTVHS FLEHIFKKPT
FCDVCNHMIV GTNAKHGLRC KACKMSIHHK CADGVGQQRC MGKLPKGFRR YYSSPLLIQE
QFGCIKEVMP IACGSKVDPV YETLRFGTSL AQKTKRSSTG SGSESPHRNS TTDLAEVPEE
SDGHSLPGHT GHTRKLSDSV FTSLENGTEH FHSEEKKPET SPVKIQQRKD ILQLNTYVAL
YKFVPQENED LEMRPGDRII LADDSNDDWW KGVIEDRVGF FPASFAQQVR AGERVYRCTR
TYIGCKEQGQ ITLKEGQICV TNEDENNGFI KVSSGKKKGF VPFDVLENI
//
