STAM2_CHICK
ID STAM2_CHICK Reviewed; 468 AA.
AC O93436;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Signal transducing adapter molecule 2;
DE Short=STAM-2;
DE AltName: Full=Epidermal growth factor receptor-associated protein with SH3 and TAM domain;
GN Name=STAM2; Synonyms=EAST;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION,
RP INTERACTION WITH EGFR AND EPS15, AND SUBCELLULAR LOCATION.
RX PubMed=9694904; DOI=10.1074/jbc.273.33.21408;
RA Lohi O., Poussu A., Merilaeinen J., Kellokumpu S., Wasenius V.-M.,
RA Lehto V.P.;
RT "EAST, an epidermal growth factor receptor- and Eps15-associated protein
RT with Src homology 3 and tyrosine-based activation motif domains.";
RL J. Biol. Chem. 273:21408-21415(1998).
RN [2]
RP FUNCTION, INTERACTION WITH EPS15, AND SUBCELLULAR LOCATION.
RX PubMed=9801161; DOI=10.1016/s0014-5793(98)01171-5;
RA Lohi O., Lehto V.-P.;
RT "EAST, a novel EGF receptor substrate, associates with focal adhesions and
RT actin fibers.";
RL FEBS Lett. 436:419-423(1998).
RN [3]
RP PHOSPHORYLATION BY SRC.
RX PubMed=9720929; DOI=10.1016/s0014-5793(98)00874-6;
RA Lohi O., Lehto V.-P.;
RT "Src phosphorylates EAST, a novel EGF receptor-associated protein.";
RL FEBS Lett. 432:225-227(1998).
CC -!- FUNCTION: Involved in intracellular signal transduction mediated by
CC EGF. As a protein associated with focal adhesions and actin filaments,
CC it may play a role in EGF receptor-stimulated cytoskeletal
CC reorganization. The ESCRT-0 complex binds ubiquitin and acts as sorting
CC machinery that recognizes ubiquitinated receptors and transfers them to
CC further sequential lysosomal sorting/trafficking processes (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9801161}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM2 and HGS.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9694904,
CC ECO:0000269|PubMed:9801161}. Early endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9694904}.
CC -!- PTM: Phosphorylated in response to EGF and PDGF. Phosphorylated by SRC.
CC {ECO:0000269|PubMed:9694904, ECO:0000269|PubMed:9720929}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ224514; CAA12023.1; -; mRNA.
DR RefSeq; NP_001012940.1; NM_001012922.1.
DR AlphaFoldDB; O93436; -.
DR SMR; O93436; -.
DR STRING; 9031.ENSGALP00000036962; -.
DR PaxDb; O93436; -.
DR GeneID; 424317; -.
DR KEGG; gga:424317; -.
DR CTD; 10254; -.
DR VEuPathDB; HostDB:geneid_424317; -.
DR eggNOG; KOG2199; Eukaryota.
DR InParanoid; O93436; -.
DR OrthoDB; 906159at2759; -.
DR PhylomeDB; O93436; -.
DR PRO; PR:O93436; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IDA:AgBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IDA:AgBase.
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; IDA:AgBase.
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 1: Evidence at protein level;
KW Cytoplasm; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transport.
FT CHAIN 1..468
FT /note="Signal transducing adapter molecule 2"
FT /id="PRO_0000190150"
FT DOMAIN 16..143
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 164..183
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 201..260
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 358..375
FT /note="ITAM"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 52407 MW; FAE790D5BDDC78A7 CRC64;
MPLSASNPFE QDVEKATNEH NNSEDWGLIM DICDKVGSTP NGAKDCLKAI MRRVNHKVPH
VALQALTLLG ACVSNCGRIF HLEVCSRDFA TEARGIINKA HGKVSEKLKT LMVEWSEEFQ
KDPQCSLISA TIKSLKEEGV TFPAAGSQAT TNAAKNGSSL SKNKEDEDIR KAIELSLQEQ
KQQQMETKSL YPSAEIQQTN QNLRKVRALY DFEAVEDNEL TFKSGEIIFV LDDSDTDWWK
GENHRGVGLF PSNFVTSDLN VEPEAATVDN SCVPEDATEE IKKAEPEAVY IDEDKMDKTL
QVLQSIDPTD LNLDTDLLDS EVICQQMGPM IDEKLEEIDR KHSELSELNV KVLEALELYN
KLMNETPMYS AYSKLHHPAQ YPPTSSGVSV QSYPVQPPSG NYMIQGVHQV TVSQGYGLGP
DQMGQLRSLP QNINSSDCNL YTKSNRQRMC HMKAITTWQR FSKHTSER
