ID   SH34A_XENLA             Reviewed;         957 AA.
AC   Q6NU22;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=SH3 domain-binding protein 4-A;
GN   Name=sh3bp4-a;
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; BC068780; AAH68780.1; -; mRNA.
DR   RefSeq; NP_001084672.1; NM_001091203.1.
DR   AlphaFoldDB; Q6NU22; -.
DR   SMR; Q6NU22; -.
DR   DNASU; 414632; -.
DR   GeneID; 414632; -.
DR   KEGG; xla:414632; -.
DR   CTD; 414632; -.
DR   Xenbase; XB-GENE-6252292; sh3bp4.S.
DR   OMA; HRIRANN; -.
DR   OrthoDB; 140316at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 414632; Expressed in gastrula 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   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035455; SH3BP4.
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-A"
FT                   /id="PRO_0000274579"
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;  106581 MW;  3AFA683E721981FC CRC64;
     MAAQKIRSAN INGLPRCKSE GTLIDFSGVP DPSLSEVKVL SPSSLRIDNP ASLENVKEVV
     AIKDYCPNNF TTLKFSKGEH LYVLDASGGD WWYAHNSTEM GYIPSSYVQP LNYRDSCLSD
     SGMIDGLLEN VDEGVKELDL LGDWTDSFNQ DSVKKSHNNP FLRPSVSNPF LNGPLVSQTH
     AADTENSVDL LLFDPLAPSH VIASETSTDM LVNLLPNTTP NKVAVAVKRD NSFFRSKRSY
     SLSELSVLQA KSEGPTTGSF FAGLKSPAPE QFQSREDFRT AWLNHRKLAR SCHDLDLLGQ
     NPGWGQTQPV ETSIVCRLDS SGGAVQLPDT NISIHVPEKH VASGETQQIS LKALLDPPLE
     LNNDKCTTVS PVLEIKLSNM DVHCPLTLEL RISVALGGNA SALNMVGIKC LRSDAREGPY
     NPVTQIYMYG DTVQVKLDNL EPVMYVVMVA QGQGIVSPSS VWEYINKKVT VGLYGPKHIH
     PSFKAVLAIF GHDCAPKSLL VNEVGQQANN PAPVTLQLWG KQQFVLPKPQ DVQLCLFSNM
     TNYRVDAGDQ GKIVRGFQLK LGKVSRLIFP IICQDPDQLS DFTLRVQVRD EFGGVLSQYC
     VQTPRPLPKT GTKSTGPRRF LKKKELGKIV LSPLAITCKY PTFQDRPVTS LKYGKLLKTV
     VRQSKNPYLL EYKKGDVIGL LSEEKIRLKG QLWNKEWYIG YYQGKLGLVH AKNVLVVGKV
     KPSFFSGPEL TTGLLLEQIL RPCKFLTYIY ASVRTLLMEN IGSWRCFADA LGYGNLPLSY
     FCRVELESET ERVASVLEKL KEECNSEGKE KKSFQKELIM ALLKIDCQGL VVRLIQDFVL
     LTTAVEVAAR WRELSEKLAR VSKQQMDGYE APHRDRNGML DSEAMWKPAY DFLLTWSAQI
     GESYRDVIQE LHTGLDKMRS PITKRWKHLT GTLILVNSLD ILRATAFSTE APEDCII