ID W5M3N3_LEPOC Unreviewed; 515 AA.
AC W5M3N3;
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=Signal transducing adaptor molecule 2 {ECO:0000313|Ensembl:ENSLOCP00000002991.1};
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:ENSLOCP00000002991.1, 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:ENSLOCP00000002991.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the STAM family.
CC {ECO:0000256|ARBA:ARBA00009666}.
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DR EMBL; AHAT01011602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01011604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M3N3; -.
DR STRING; 7918.ENSLOCP00000002991; -.
DR Ensembl; ENSLOCT00000002997.1; ENSLOCP00000002991.1; ENSLOCG00000002547.1.
DR eggNOG; KOG2199; Eukaryota.
DR GeneTree; ENSGT00940000157055; -.
DR HOGENOM; CLU_010104_0_0_1; -.
DR InParanoid; W5M3N3; -.
DR OMA; VPMQAYL; -.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000002547; Expressed in bone element and 13 other cell types or tissues.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd21390; GAT_STAM2; 1.
DR CDD; cd11820; SH3_STAM; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR PANTHER; PTHR45929:SF1; SIGNAL TRANSDUCING ADAPTER MOLECULE 2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 16..143
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 207..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..372
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 56772 MW; F881C1E8CC3E4F42 CRC64;
MPLFSQNPFD QDVEKATNEH NTADDWGLIM DICDRVGTTP NGAKECLRSI VKRINHKVPH
VAMQALTLLS ACVSNSGKIF HLEICSRDFA NDVRGILSKA HPKVCEKFKA LLVEWADEFQ
KDPQLSLLGA TIKSLKEEGV TFTSSGSQQS HKKCARKPFF FLSKPLAGAK YDTGLITIEL
SLQEQRQQQT ETRPLTVVAD PPFNNNRESR KVRALYDFEA AEDNELTFKA GELIIVQDDS
DPNWWKGENH RGVGLFPSNF VTTNLNADPE PAAFVEKTAL PEDTSLESKM EPEPVFIDEE
KMDRTLHLLR NTDPADSEPD SSELLHLEEV CRQMNPMIDE KLEEIDRKHS ELSELNVKVL
EALELYNKLM NEAPMYSVYS KMQPQAHFPQ TSAGVPVQAY PGQPQSGAYM ASGVPGQGYS
LGPDQAGPLR SLPPAVSAPV TSQPGQAPYL SAGVNAGYMN QSSGGPAPYP HQVGVAMDMS
AYQNTSMAQA SAYPLAAPSH PGPQQQANYY QQPLL
//
