SH3B4_RAT
ID SH3B4_RAT Reviewed; 961 AA.
AC Q9JJS5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=SH3 domain-binding protein 4;
GN Name=Sh3bp4;
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 [MRNA].
RC TISSUE=Brain;
RA Sharma K.D., Schmidt H., Rathjen F.G.;
RT "Cloning and characterization of a novel gene from rat brain.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function in transferrin receptor internalization at the
CC plasma membrane through a cargo-specific control of clathrin-mediated
CC endocytosis. Alternatively, may act as a negative regulator of the
CC amino acid-induced TOR signaling by inhibiting the formation of active
CC Rag GTPase complexes. Preferentially binds inactive Rag GTPase
CC complexes and prevents their interaction with the mTORC1 complex
CC inhibiting its relocalization to lysosomes and its activation. Thereby,
CC may indirectly regulate cell growth, proliferation and autophagy (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or homooligomer. Interacts with DNM2, EPS15,
CC clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with
CC the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most
CC probably direct, preferentially occurs with their inactive GDP-bound
CC form and is negatively regulated by amino acids (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}.
CC Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Specifically associated with transferrin receptor-
CC containing clathrin-coated pits and clathrin-coated vesicles. May also
CC localize to the nucleus (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain mediates localization to the clathrin-coated
CC pits and vesicles. The SH3 domain mediates interaction with DNM2 and
CC the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also
CC mediates interaction with RRAGB, RRAGC and is required for the negative
CC regulation of mTORC1 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon EGF stimulation. Phosphorylation prevents
CC interaction with DNM2 (By similarity). {ECO:0000250}.
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DR EMBL; AJ278266; CAB93353.2; -; mRNA.
DR AlphaFoldDB; Q9JJS5; -.
DR SMR; Q9JJS5; -.
DR STRING; 10116.ENSRNOP00000026312; -.
DR iPTMnet; Q9JJS5; -.
DR PhosphoSitePlus; Q9JJS5; -.
DR PaxDb; Q9JJS5; -.
DR PRIDE; Q9JJS5; -.
DR UCSC; RGD:620219; rat.
DR RGD; 620219; Sh3bp4.
DR eggNOG; ENOG502QTUW; Eukaryota.
DR InParanoid; Q9JJS5; -.
DR PhylomeDB; Q9JJS5; -.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q9JJS5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
DR CDD; cd11757; SH3_SH3BP4; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035455; SH3BP4.
DR InterPro; IPR035456; SH3BP4_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR15603:SF3; PTHR15603:SF3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..961
FT /note="SH3 domain-binding protein 4"
FT /id="PRO_0000274576"
FT DOMAIN 55..114
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 315..452
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 652..722
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921I6"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0V3"
SQ SEQUENCE 961 AA; 107513 MW; F31DA2AD30B3F35A CRC64;
MAAQRIRAAN SSGLPRCKSE GTLIDLSEGF SETSFNDVKV PSPSALLVDN PTPFGNAKEV
IAIKDYCPNN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE MGYIPSSYVQ PLNYRNSTLS
DSGMIDNLPD SPDEVAKELD LLGGWTDDQK QSGRPYSNNP FWNGVRTNPF LNGNAQPSMD
ELNPKSTVDL LLFDTGTSSF TESSSATTNS TGNIFDELPA TNGIHLEQPV KRDNPFFRSK
RSYSLSELSV LQAKSDAPPT SSFFTGLKSP APEQFQSRED FRTAWLNHRK LARSCHDLDL
LGQSPGWGQT QAVETNIVCK LDSSGGSVQL PDTSISIHVP EGHVAPGETQ QISMKALLDP
PLDLNSDRST SISPVVEVKL SNLEVSTFII LEMKVSAEVK GDIFSKSTVV LQCLRSDSKE
GPYAPIPLAY SYGDTIQVQL DNLEPCMYLA IVAQGSNILY PSTVWDFIHK RVTVGLYGPK
HIHPSFKTVV TIFGHDCAPK TLLVTEVTRQ APSPAPVALQ LWGKHQFILS RPQDLRVCMF
SNMTNYDVKS NEQAKVVRGF QMKLGKVSRL IFSVISQNPN ELSDFTLRVQ VKDDQDTILT
QFCVQTPQPP PKSAIKPSGQ RRFLKKNEVG KIILSPFVVT TKYPTFQDRP VSSLKFGKLL
KTVVRQNKSH YLLEYKKGDV VALLSEERIR LKGQLWTKEW YIGYYQGKVG LVHTKNVLVV
GKARPSLFSG PELSTSVLLE QILRPCKFLT YIYASVRTLL MENISSWRAF ADALGYGNLP
LTFFCRAELD SEPERVASVL EKLKEDCNNP DNKDRKSFQK ELVMALLKMD CQGLVVRLIQ
DFVLLTTAVE VAQRWRELAE KLAKVSKQQM DAYESPHRDR NGVVDSEAMW KPAYDFLLTW
SHQIGDSYRD VIQELHIGLD KMKNPITRRW KHLTGTLILV NSLDILRAAA FSPADHDDFV
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