SH34A_DANRE
ID SH34A_DANRE Reviewed; 965 AA.
AC Q1LVQ2; Q4V977; Q76JU7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=SH3 domain-binding protein 4-A;
GN Name=sh3bp4a; Synonyms=sh3bp4; ORFNames=si:dkey-110p14.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-681.
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
RA Abe S.;
RT "Danio rerio SH3BP4 mRNA, partial CDS.";
RL Submitted (NOV-2002) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH97028.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BX649510; CAK05098.1; -; Genomic_DNA.
DR EMBL; BC097028; AAH97028.1; ALT_SEQ; mRNA.
DR EMBL; AB095747; BAD01557.1; -; mRNA.
DR RefSeq; NP_001303259.1; NM_001316330.1.
DR RefSeq; XP_005161754.1; XM_005161697.3.
DR AlphaFoldDB; Q1LVQ2; -.
DR SMR; Q1LVQ2; -.
DR STRING; 7955.ENSDARP00000110108; -.
DR PaxDb; Q1LVQ2; -.
DR Ensembl; ENSDART00000022654; ENSDARP00000007868; ENSDARG00000020000.
DR Ensembl; ENSDART00000105711; ENSDARP00000096489; ENSDARG00000020000.
DR Ensembl; ENSDART00000130585; ENSDARP00000110108; ENSDARG00000020000.
DR GeneID; 403082; -.
DR KEGG; dre:403082; -.
DR CTD; 403082; -.
DR ZFIN; ZDB-GENE-040303-3; sh3bp4a.
DR eggNOG; ENOG502QTUW; Eukaryota.
DR GeneTree; ENSGT00390000013151; -.
DR InParanoid; Q1LVQ2; -.
DR OMA; HRIRANN; -.
DR OrthoDB; 140316at2759; -.
DR PhylomeDB; Q1LVQ2; -.
DR TreeFam; TF105572; -.
DR Reactome; R-DRE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q1LVQ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000020000; Expressed in Kupffer's vesicle and 32 other tissues.
DR ExpressionAtlas; Q1LVQ2; baseline.
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; 1.
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..965
FT /note="SH3 domain-binding protein 4-A"
FT /id="PRO_0000274577"
FT DOMAIN 56..115
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 322..456
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 656..726
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT CONFLICT 38
FT /note="D -> F (in Ref. 3; BAD01557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 965 AA; 108453 MW; 2E9C5AC8853751F5 CRC64;
MAAHRIRVTN NNNVLPRCKS EGTLIDIDEG VTEASLVDVK VPSPSALRLA PSTSFGTARE
VVAIKDYCPS SFTTLKFSKG DHLYVLDTSG GEWWYAHNNR EMGYIPSTYV QPINYRNSSL
SDSGMIDNLG DCSEEGAKEL DLLGEWTGVC LKPSLPYDNN NPFSMLSSTN PFLNGSMDDV
LDQNSNEKPN QCNSMDLLFF DLPSAPISTT SNTKGYSISG FDGTSTSADL EALQMLRKDN
PFFRSKRSYS LSELSTLQAQ SNPPLPSSGF FTGLKAPSPE QFQNREDFRT AWLNHRKLAR
SCHDLESLGQ NPGWGQTQPV ETNIVCKLDS CGGAVQLPDT NISIHVPEGH VAVGDTQQIS
MKALLDPPLE LNNDRCSTVS PVVEIKLSNM EIKSFITLEM KVSVMTRTES PMAEIVCVRS
DCKEGPYSPV PQAYIYGDTI QVQLDNLEPC MYVAVVVQAK HVSFSSNVWN HMVKKVTLGL
YGPKHIHPSF KTVVAIFGHD CAPKTLLVSE VGKQAKSAPP VSLQLWGKHQ FVLSRPQDLQ
IGMYSNMSNY EVKANDQARV VRGFQIKLGK VSRLIYMISS RKADEISDFT LRVQVKDDQD
CILAQFCVQT PQPPPKTGMR NNGQRRFLKK KEVDKIILSP LAITTKYPQF QERCITNLKF
GKLIKTVIRQ TKNQYLLEYK KGDIIALLSE EKIKLKGQLW TKEWYIGYYQ GKIGLVHVKN
VLVLGKVKPI YFCGPDLTTT MLMEQILKPC KFLTYIYASV RTILMENLGN WRAFADALSY
VNLPLTYFCR AELDSEPERV ASVLEKLKED CLNMETKEKK SFQKELMMAL LKMDCQGLVA
RLIMDFVLLT TAVEVAPRWR DLAEKLAHVS KQQMEAYEAP HRDKTGMVDS EAMWKPAYDF
LLTWAAQIGD SYRDVIHELH MGLDRMKNPI TKRWKHLTGT LILVNCLDLL RSSAFSPAPQ
DDFAI
