ID   SH34B_XENLA             Reviewed;         957 AA.
AC   Q6NU51;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=SH3 domain-binding protein 4-B;
GN   Name=sh3bp4-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-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; BC068750; AAH68750.1; -; mRNA.
DR   RefSeq; NP_001084680.1; NM_001091211.1.
DR   AlphaFoldDB; Q6NU51; -.
DR   SMR; Q6NU51; -.
DR   DNASU; 414640; -.
DR   GeneID; 414640; -.
DR   KEGG; xla:414640; -.
DR   CTD; 414640; -.
DR   Xenbase; XB-GENE-970863; sh3bp4.L.
DR   OMA; PQDLHVC; -.
DR   OrthoDB; 140316at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 414640; Expressed in pancreas and 19 other tissues.
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-B"
FT                   /id="PRO_0000274580"
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;  106447 MW;  67D9EC12F6B6DE84 CRC64;
     MAAQKIRSAN TNGLPRCKSE GALIDFSGVP DPSLSEVKVL SPSSLRIDNP ASLENVKEVV
     AIKDYCPNNF TTLKFSKGEH LYVLDASGGD WWYAHNTTEM GYIPSSYVQP LNYRDSCLSD
     SGMIDGLLES VDEGVKELDL LGDWTNSSNQ DSVKKCHNNP FLRPSVSNPF LNGPLVPQTH
     TADTENSVDL LLFDPLAPSH AIASETSTDV LLDLLPNTSQ NEVTVPVKRD NPFFRSKRSY
     SLSELSVLQA KSESPTTGSF FAGLKSPAPE QFQSREDFRT AWLNHRKLAR SCHDLDLLGQ
     NPGWGQTQPV ETSIVCRLDS SGGAVQLPDT SISILVPEKH VASGETQQIS LKALLDPPLE
     LNNDKCTTVS PVLEIKLSNM DVQSPLTLEV RISVALGGNA SALNMVGIKC LRSDAKEGPY
     NSVTQIYMYG DTVQVKLDNL EPVMYVVMVA QGQGIVSPSS VWEYINKKVT VGLYGPKHIH
     PSFKAVIVIF GHDCAPKSLL VNEVGQQANK SAPVTLQLWG KQQFVLPKPQ DLQLCLFSNM
     TNYRVDAGDQ GKMVRGFQLK LGKVSRLIFP ITCQDSAQLS DFTLRVQVRD EAGGVLSQYC
     VQTPQPPPKT GSKSTGPRRF LKKKEVGKIV LSPLALTYKY PTFQDRPVTS LKYGKLIKTV
     VRQSKNPYLL EYKKGDVIGL LSEEKIRLKG QLWNKEWYIG YYQGKLGLVH AKNVLVVGKV
     KPSFFSGPEL TTGLLLEQIL RPCKFLTYIY ASVRTLLMEN IGSWRCFADA LGYGNLPLSY
     FCRVELESET ERVASVLEKL KEECNSEGKE KKSFQKELIM ALLKIDCQGL VVRLIQDFVL
     LTTAVEVASR WRELAEKLAR VSKQQMEGYE APHRDRNGML DSEAMWKPAY DFLLTWSAQI
     GESYRDVIQE LHTGLDKMRS PITKRWKHLT GTLIFVNSLD ILRAAAFSTQ EPEDCII