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Database: UniProt
Entry: A0A2U4AC19_TURTR
LinkDB: A0A2U4AC19_TURTR
Original site: A0A2U4AC19_TURTR 
ID   A0A2U4AC19_TURTR        Unreviewed;       604 AA.
AC   A0A2U4AC19;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Signal transducing adapter molecule 2 isoform X1 {ECO:0000313|RefSeq:XP_019778553.1};
GN   Name=STAM2 {ECO:0000313|RefSeq:XP_019778553.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019778553.1};
RN   [1] {ECO:0000313|RefSeq:XP_019778553.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019778553.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in intracellular signal transduction mediated by
CC       cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it
CC       plays a role in signaling leading to DNA synthesis and MYC induction.
CC       May also play a role in T-cell development. Involved in down-regulation
CC       of receptor tyrosine kinase via multivesicular body (MVBs) when
CC       complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds
CC       ubiquitin and acts as a sorting machinery that recognizes ubiquitinated
CC       receptors and transfers them to further sequential lysosomal
CC       sorting/trafficking processes. {ECO:0000256|ARBA:ARBA00043869}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004469}.
CC   -!- SIMILARITY: Belongs to the STAM family.
CC       {ECO:0000256|ARBA:ARBA00009666}.
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DR   RefSeq; XP_019778553.1; XM_019922994.2.
DR   AlphaFoldDB; A0A2U4AC19; -.
DR   STRING; 9739.ENSTTRP00000014767; -.
DR   GeneID; 101319805; -.
DR   InParanoid; A0A2U4AC19; -.
DR   OrthoDB; 620063at2759; -.
DR   Proteomes; UP000245320; Chromosome 7.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd21390; GAT_STAM2; 1.
DR   CDD; cd11963; SH3_STAM2; 1.
DR   CDD; cd16999; VHS_STAM2; 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; IPR035675; STAM2_SH3.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
DR   InterPro; IPR047493; VHS_STAM2.
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; PF02809; UIM; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00726; UIM; 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; PS50330; UIM; 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   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          94..222
FT                   /note="VHS"
FT                   /evidence="ECO:0000259|PROSITE:PS50179"
FT   DOMAIN          280..339
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          411..445
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        587..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  65747 MW;  419619D4676DE856 CRC64;
     MPAAGGTSYR EERSGRSARA ERGPGAGPSG RSGAGAVAEV PDATGAEPSR KPGPWVPQPG
     AAAEPPPDRS NLGSGAGEMP LFTANHFEQD VEKATNEYNT TEDWSLIMDI CDKVGSTPNG
     AKDCLKAIMK RVNHKVPHVA LQALTLLGAC VANCGKIFHL EVCSRDFATE VRAVIKNKAH
     PKVCEKLKSL MVEWSEEFQK DPQFSLISAT IKSMKEEGIT FPSAGSQTVS VAAKNGTSLN
     KNKEDEDIAK AIELSLQEQK QQHTETKSLY PSAEIPSNNK VARKVRALYD FEAVEDNELT
     FKHGEIIIVL DDSDANWWKG ENHRGIGLFP SNFVTTNLNI EPEAAAVDKL NVIDDEEEEI
     KKSEPEPVYI DEDKMDRALQ VLQSIDPTDS KPDSQDLLDL EDICQRMGPM IDEKLEEIDR
     KHSELSELNV KVLEALELYN KLMNEAPVYS VYSKIHHPAH YPPSSAGVPM QTYPVQPHGA
     NYMGQSIHQV TVAQSYSLGP DQIGPLRSLP PNVNSSVTTQ PAPTPYLSAG QDTVSNPTYM
     NQNSHLQSAT GAAAYTQQMG MSVDLSSHQS TTSSLPRSAG FAVAAPAHSV SQQQTDYPQQ
     QPLL
//
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