SH3B4_XENTR
ID SH3B4_XENTR Reviewed; 957 AA.
AC Q5U228;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=SH3 domain-binding protein 4;
GN Name=sh3bp4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible role in regulating endocytosis of the transferrin
CC receptor at the plasma membrane. Alternatively, may function as a
CC negative regulator of the amino acid-induced TOR signaling by
CC inhibiting the formation of active Rag GTPase complexes. Preferentially
CC binds inactive Rag GTPase complexes and prevents their interaction with
CC the mTORC1 complex inhibiting its relocalization to lysosomes and its
CC activation. Thereby, may indirectly regulate cell growth, proliferation
CC and autophagy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or homooligomer. {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. {ECO:0000250}.
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DR EMBL; BC086304; AAH86304.1; -; mRNA.
DR RefSeq; NP_001011179.1; NM_001011179.1.
DR AlphaFoldDB; Q5U228; -.
DR SMR; Q5U228; -.
DR STRING; 8364.ENSXETP00000023846; -.
DR PaxDb; Q5U228; -.
DR DNASU; 496599; -.
DR GeneID; 496599; -.
DR KEGG; xtr:496599; -.
DR CTD; 23677; -.
DR Xenbase; XB-GENE-970857; sh3bp4.
DR eggNOG; ENOG502QTUW; Eukaryota.
DR HOGENOM; CLU_013080_2_0_1; -.
DR InParanoid; Q5U228; -.
DR OMA; NISSWCS; -.
DR OrthoDB; 140316at2759; -.
DR PhylomeDB; Q5U228; -.
DR TreeFam; TF105572; -.
DR Reactome; R-XTR-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; 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:0031267; F:small GTPase binding; IEA:InterPro.
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; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 2: Evidence at transcript level;
KW Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Nucleus;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..957
FT /note="SH3 domain-binding protein 4"
FT /id="PRO_0000274581"
FT DOMAIN 54..113
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 312..449
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 649..719
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 957 AA; 106584 MW; 6880E1ED043445D7 CRC64;
MAAQKIRSAN TNGLPRCKSE GALIDFSGVP DPNLSDVKVL SPSSLRVDNP ASLDNVKEVV
AIKDYCPNNF TTLKFSKGEH LYVLDTSGGE WWYAHNTTEM GYIPSSYVQP LNYRDSCLSD
SGMIDGLLES VDEGVKELDL LGDWTETISQ DPIKKCHNNP FLRPSVSNPF LNGPLMPQIH
ALETGNSVDL LLFDPLAPSH AFSSETSTDV LLDLLPNNTQ NEVAVPVKRD NPFFRSKRSY
SLSELSVLQA KSENPTTGSF FAGLKSPAPE QFQSREDFRT AWLNHRKLAR SCHDLDLLGQ
NPGWGQTQPV ETSIVCRLDS SGGAVQLPDT NISIHVPEKH VASGETQQIS LKALLDPPLE
LNNDKCTTVS PVLEIKLSNM DVQSPLTLEL RISVALGGNA SALNMVGIKC LRSDAKEGPY
NPVTQIYIYG DTVQVKLDNL EPVMYVVMVA QGQGIVSPSS VWEYINKKVT VGLYGPKHIH
PSFKAVLAIF GHDCAPKTLL VNEVGQQANN SAPVTLQLWG KQQFVLPKPQ DLQLCLFSNM
TNYRVDAGDQ GKMVRGFQLK LGKVSRLIFP IICQEPAQLS DFTLRVQVRD EVGGVLSQYC
VQTPRPPPKT GNKSTGPRRF LKKKEVGKIV LSPLAVTCKY PTFQDRPVTS LKYGKLLKTV
VRQSKNPYLL EYKKGDVIGL LSEEKIRLKG QLWNKEWYIG YYQGKLGLVH AKNVLVVGKV
KPSFFSGPEL TTGLLLEQML RPCKFLTYIY ASVRTLLMEN IGSWRCFADA LGYGNLPLSY
FCRVELESET ERVASVLEKL KEECNSEGKE KKSFQKELIM ALLKIDCQGL VVRLIQDFVL
LTTAVEVASR WRELAEKLAR VSKQQMDGYE APHRDRNGAL DSEAMWKPAY DFLLTWSAQI
GESYRDVIQE LHTGLDKMRS PITKRWKHLT GTLILVNSLD ILRAAAFSTQ EPEDCII
