ID A0A2K6Q9U6_RHIRO Unreviewed; 540 AA.
AC A0A2K6Q9U6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Signal transducing adaptor molecule {ECO:0000313|Ensembl:ENSRROP00000025549.1};
GN Name=STAM {ECO:0000313|Ensembl:ENSRROP00000025549.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000025549.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000025549.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_010353051.1; XM_010354749.1.
DR AlphaFoldDB; A0A2K6Q9U6; -.
DR STRING; 61622.ENSRROP00000025549; -.
DR Ensembl; ENSRROT00000049766.1; ENSRROP00000025549.1; ENSRROG00000036523.1.
DR GeneID; 104655327; -.
DR KEGG; rro:104655327; -.
DR CTD; 8027; -.
DR GeneTree; ENSGT00940000157171; -.
DR OMA; QVYRDWW; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; IEA:Ensembl.
DR CDD; cd21389; GAT_STAM1; 1.
DR CDD; cd11964; SH3_STAM1; 1.
DR CDD; cd17000; VHS_STAM1; 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; IPR047492; GAT_STAM1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035657; STAM1_SH3.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR047528; VHS_STAM1.
DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR PANTHER; PTHR45929:SF2; SIGNAL TRANSDUCING ADAPTER MOLECULE 1; 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; 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 Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 16..143
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 210..269
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 501..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 59170 MW; C92FB6E41DBD8CF3 CRC64;
MPLFATNPFD QDVEKATSEM NTAEDWGLIL DICDKVGQSR TGPKDCLRSI MRRVNHKDPH
VAMQALTLLG ACVSNCGKIF HLEVCSRDFA SEVSNVLNKG HPKVCEKLKA LMVEWTDEFK
NDPQLSLISA MIKNLKEQGV AFPAIGSQAA EQAKASPALA AKDPGTVANK KEEEDLAKAI
ELSLKEQRQQ STTLSTLYPS TSNLLTNHQH EGRKVRAIYD FEAAEDNELT FKAGEIITVL
DDSDPNWWKG ETHQGIGLFP SNFVTADLTA EPEMIKTEKK TVQFSDDVQV ETIEPEPEPA
FIDEDKMDQL LQMLQSTDPS DDQPDLPELL HLEAMCHQMG PLIDEKLEDI DRKHSELSEL
NVKVMEALSL YTKLMNEDPM YSMYAKLQNQ PYYMQSSGVS GSQVYAGPPP SGAYLVAGNA
QMSHLQSYSL PPEQLSSLSQ AVVPPSANPA LPSQQTQAAY PNTMVSSVQG NTYPSQAPVY
SPPPTATVAA ATADVTLYQN AGPSMSQVPN YNLTSSTLPQ PGGSQQPPQP QQPYSQKALL
//
