STAM2_RAT
ID STAM2_RAT Reviewed; 523 AA.
AC Q5XHY7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Signal transducing adapter molecule 2;
DE Short=STAM-2;
GN Name=Stam2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION.
RX PubMed=11062024; DOI=10.1006/bbrc.2000.3749;
RA Murai S., Kitamura N.;
RT "Involvement of hrs binding protein in IgE receptor-triggered exocytosis in
RT RBL-2H3 mast cells.";
RL Biochem. Biophys. Res. Commun. 277:752-756(2000).
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 sorting machinery that recognizes ubiquitinated
CC receptors and transfers them to further sequential lysosomal
CC sorting/trafficking processes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11062024}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and
CC HGS. Part of a complex at least composed of HSG, STAM2 and EPS15.
CC Interacts with JAK2 and JAK3. Interacts with ubiquitinated proteins and
CC the deubiquitinating enzyme USP8/UBPY. Interacts (via the via the PxVxL
CC motif) with CBX5; the interaction is direct. Interacts with VPS37C.
CC Interacts with ubiquitin; the interaction is direct. Interacts (via UIM
CC domain) with UBQLN1 (via ubiquitin-like domain) (By similarity).
CC {ECO:0000250|UniProtKB:O75886, ECO:0000250|UniProtKB:O88811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; BC083912; AAH83912.1; -; mRNA.
DR RefSeq; NP_001012085.1; NM_001012085.1.
DR AlphaFoldDB; Q5XHY7; -.
DR BMRB; Q5XHY7; -.
DR SMR; Q5XHY7; -.
DR STRING; 10116.ENSRNOP00000033318; -.
DR jPOST; Q5XHY7; -.
DR PaxDb; Q5XHY7; -.
DR PRIDE; Q5XHY7; -.
DR Ensembl; ENSRNOT00000115523; ENSRNOP00000080484; ENSRNOG00000027447.
DR GeneID; 311030; -.
DR KEGG; rno:311030; -.
DR UCSC; RGD:1311497; rat.
DR CTD; 10254; -.
DR RGD; 1311497; Stam2.
DR eggNOG; KOG2199; Eukaryota.
DR GeneTree; ENSGT00940000157055; -.
DR HOGENOM; CLU_010104_0_0_1; -.
DR InParanoid; Q5XHY7; -.
DR OMA; FASEVRV; -.
DR OrthoDB; 906159at2759; -.
DR PhylomeDB; Q5XHY7; -.
DR TreeFam; TF315007; -.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:Q5XHY7; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000027447; Expressed in testis and 18 other tissues.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd11963; SH3_STAM2; 1.
DR Gene3D; 1.25.40.90; -; 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 Pfam; PF00018; SH3_1; 1.
DR Pfam; PF02809; UIM; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00726; UIM; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transport.
FT CHAIN 1..523
FT /note="Signal transducing adapter molecule 2"
FT /id="PRO_0000190149"
FT DOMAIN 16..144
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 165..184
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 202..261
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 360..377
FT /note="ITAM"
FT REGION 219..220
FT /note="Interaction with USP8"
FT /evidence="ECO:0000250"
FT REGION 334..368
FT /note="Interaction with HGS"
FT /evidence="ECO:0000250"
FT MOTIF 54..67
FT /note="PxVxL motif"
SQ SEQUENCE 523 AA; 57159 MW; 60D6910505391C74 CRC64;
MPLFTANPFE QDVEKATNEY NTTEDWSLIM DICDRVGSTP NGAKDCLKAI MKRVNHKVPH
VALQALTLLG ACVANCGKIF HLEVCSRDFA TEVRAVIKNK AHPKVCEKLK SLMVEWSEEF
QKDPQFSLIS ATIKAMKEEG VTFPSAGSQT VSAAAKNGAS LNKNKEDEDI AKAIELSLQE
QKQQYPETKA LCPPAESQLS NKVARRVRAL YDFEAVEDNE LTFKHGEIIT VLDDSDANWW
EGENHRGAGL FPSSFVTTDL STEVEAATVD KSNVIDDDVE EIKKSEPEPV YIDEGKMDRA
LQILQSIDPK DPKPDSQDLL DLEDICQQMG PMIDEKLEEI DRRHSELSEL NVKVLEALEL
YNKLVNEAPM YSVYSKLHPA PYSATAAGVP VQTYPVQSHG GNYLGHGIHQ VPVAQSYNLG
PDPMGSSRSL PPNMNSVTAH TIQPPYLSTG QDAVSNPSYM TQSSHLQAAA GTAAYTPAMG
VSADLSSFQS TASGLPQLAG FPVAVPVPPA PQPQASYHQQ PLL
