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SPAR_HUMAN
ID   SPAR_HUMAN              Reviewed;          90 AA.
AC   A0A1B0GVQ0;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 2.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Small regulatory polypeptide of amino acid response {ECO:0000303|PubMed:28024296};
GN   Name=SPAAR {ECO:0000312|HGNC:HGNC:27244};
GN   Synonyms=LINC00961 {ECO:0000312|HGNC:HGNC:27244},
GN   SPAR {ECO:0000303|PubMed:28024296};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [2]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH ATP6V0A1 AND ATP6V0A2.
RX   PubMed=28024296; DOI=10.1038/nature21034;
RA   Matsumoto A., Pasut A., Matsumoto M., Yamashita R., Fung J., Monteleone E.,
RA   Saghatelian A., Nakayama K.I., Clohessy J.G., Pandolfi P.P.;
RT   "mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR
RT   polypeptide.";
RL   Nature 541:228-232(2017).
CC   -!- FUNCTION: [Isoform 2]: Negative regulator of amino acid sensing and
CC       mTORC1, a signaling complex promoting cell growth in response to growth
CC       factors, energy levels and amino acids (PubMed:28024296). Negatively
CC       regulates mTORC1 activation by inhibiting recruitment of mTORC1 to
CC       lysosomes upon stimulation with amino acids: acts by promoting the
CC       formation of a tightly bound supercomplex composed of the lysosomal V-
CC       ATPase, Ragulator and Rag GTPases, preventing recruitment of mTORC1
CC       (PubMed:28024296). Acts as a regulator of muscle regeneration following
CC       injury by regulating mTORC1 activation (By similarity).
CC       {ECO:0000250|UniProtKB:A0A1B0GSZ0, ECO:0000269|PubMed:28024296}.
CC   -!- SUBUNIT: Interacts with components of the lysosomal V-ATPase complex
CC       (PubMed:28024296). Interacts with ATP6V0A1 (PubMed:28024296). Interacts
CC       with ATP6V0A2 (PubMed:28024296). {ECO:0000269|PubMed:28024296}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000269|PubMed:28024296}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:28024296}. Lysosome membrane
CC       {ECO:0000269|PubMed:28024296}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:28024296}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1 {ECO:0000305|PubMed:28024296};
CC         IsoId=A0A1B0GVQ0-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305|PubMed:28024296};
CC         IsoId=A0A1B0GVQ0-2; Sequence=VSP_058780;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung, heart and skeletal
CC       muscle. {ECO:0000269|PubMed:28024296}.
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DR   EMBL; AL135841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001335036.1; NM_001348107.1. [A0A1B0GVQ0-2]
DR   AlphaFoldDB; A0A1B0GVQ0; -.
DR   SMR; A0A1B0GVQ0; -.
DR   BioMuta; SPAAR; -.
DR   MassIVE; A0A1B0GVQ0; -.
DR   PeptideAtlas; A0A1B0GVQ0; -.
DR   Antibodypedia; 79062; 2 antibodies from 2 providers.
DR   DNASU; 158376; -.
DR   Ensembl; ENST00000443779.3; ENSP00000490187.1; ENSG00000235387.5. [A0A1B0GVQ0-2]
DR   Ensembl; ENST00000636776.1; ENSP00000490606.1; ENSG00000235387.5. [A0A1B0GVQ0-2]
DR   Ensembl; ENST00000638062.1; ENSP00000489755.1; ENSG00000235387.5. [A0A1B0GVQ0-2]
DR   GeneID; 158376; -.
DR   KEGG; hsa:158376; -.
DR   MANE-Select; ENST00000443779.3; ENSP00000490187.1; NM_001348107.3; NP_001335036.2. [A0A1B0GVQ0-2]
DR   CTD; 158376; -.
DR   DisGeNET; 158376; -.
DR   GeneCards; SPAAR; -.
DR   HGNC; HGNC:27244; SPAAR.
DR   HPA; ENSG00000235387; Tissue enhanced (adipose tissue, breast).
DR   MIM; 617627; gene.
DR   neXtProt; NX_A0A1B0GVQ0; -.
DR   OpenTargets; ENSG00000235387; -.
DR   VEuPathDB; HostDB:ENSG00000235387; -.
DR   GeneTree; ENSGT00850000133592; -.
DR   OMA; ILCCFSC; -.
DR   OrthoDB; 1584628at2759; -.
DR   PathwayCommons; A0A1B0GVQ0; -.
DR   SignaLink; A0A1B0GVQ0; -.
DR   GenomeRNAi; 158376; -.
DR   Pharos; A0A1B0GVQ0; Tbio.
DR   PRO; PR:A0A1B0GVQ0; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; A0A1B0GVQ0; protein.
DR   Bgee; ENSG00000235387; Expressed in apex of heart and 126 other tissues.
DR   GO; GO:1905103; C:integral component of lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
DR   GO; GO:0043416; P:regulation of skeletal muscle tissue regeneration; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative initiation; Endosome; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..90
FT                   /note="Small regulatory polypeptide of amino acid response"
FT                   /id="PRO_0000439038"
FT   TOPO_DOM        1..18
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:28024296"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:28024296"
FT   VAR_SEQ         1..15
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305|PubMed:28024296"
FT                   /id="VSP_058780"
SQ   SEQUENCE   90 AA;  9632 MW;  74327A62C468FF5B CRC64;
     MGAKAPRGPK VAQWAMETAV IGVVVVLFVV TVAITCVLCC FSCDSRAQDP QGGPGRSFTV
     ATFRQEASLF TGPVRHAQPV PSAQDFWTFM
 
 
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