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BTNL1_MOUSE
ID   BTNL1_MOUSE             Reviewed;         509 AA.
AC   Q7TST0; A6X8K2; G3UZN0; O70356;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Butyrophilin-like protein 1;
DE   Flags: Precursor;
GN   Name=Btnl1; Synonyms=Btnl3, Gm316, Ng10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RA   Rowen L., Qin S., Loretz C., Mix L., Lasky S., Madan A., Hood L.;
RT   "Sequence of the mouse major histocompatibility class II region.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-342.
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC05289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAH52925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH52925.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AF050157; AAC05289.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CR974457; CAO77747.1; -; Genomic_DNA.
DR   EMBL; BC052925; AAH52925.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS50075.1; -.
DR   RefSeq; NP_001104564.1; NM_001111094.1.
DR   AlphaFoldDB; Q7TST0; -.
DR   SMR; Q7TST0; -.
DR   STRING; 10090.ENSMUSP00000079140; -.
DR   iPTMnet; Q7TST0; -.
DR   PhosphoSitePlus; Q7TST0; -.
DR   MaxQB; Q7TST0; -.
DR   PaxDb; Q7TST0; -.
DR   PeptideAtlas; Q7TST0; -.
DR   PRIDE; Q7TST0; -.
DR   ProteomicsDB; 273715; -.
DR   DNASU; 100038862; -.
DR   Ensembl; ENSMUST00000080254; ENSMUSP00000079140; ENSMUSG00000062638.
DR   GeneID; 100038862; -.
DR   KEGG; mmu:100038862; -.
DR   UCSC; uc012apy.1; mouse.
DR   CTD; 100038862; -.
DR   MGI; MGI:1932027; Btnl1.
DR   VEuPathDB; HostDB:ENSMUSG00000062638; -.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   GeneTree; ENSGT00940000162079; -.
DR   HOGENOM; CLU_013137_22_2_1; -.
DR   InParanoid; Q7TST0; -.
DR   OMA; ISYTGWR; -.
DR   OrthoDB; 522383at2759; -.
DR   PhylomeDB; Q7TST0; -.
DR   TreeFam; TF331083; -.
DR   BioGRID-ORCS; 100038862; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q7TST0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q7TST0; protein.
DR   Bgee; ENSMUSG00000062638; Expressed in jejunum and 12 other tissues.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0045062; P:extrathymic T cell selection; IMP:MGI.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Immunoglobulin domain; Membrane; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..509
FT                   /note="Butyrophilin-like protein 1"
FT                   /id="PRO_0000014536"
FT   TOPO_DOM        28..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..509
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..139
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          151..237
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          316..509
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          349..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        53..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        167..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        22
FT                   /note="F -> S (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="M -> T (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="M -> T (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="L -> S (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332..337
FT                   /note="DWRKEL -> AIDLSN (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339..341
FT                   /note="QEA -> CIK (in Ref. 3; AAH52925)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  57726 MW;  8302DFBA7C3C8826 CRC64;
     MMKGSPSVPP AGCLLPLLLL LFTGVSGEVS WFSVKGPAEP ITVLLGTEAT LPCQLSPEQS
     AARMHIRWYR AQPTPAVLVF HNGQEQGEVQ MPEYRGRTQM VRQAIDMGSV ALQIQQVQAS
     DDGLYHCQFT DGFTSQEVSM ELRVIGLGSA PLVHMTGPEN DGIRVLCSSS GWFPKPKVQW
     RDTSGNMLLS SSELQTQDRE GLFQVEVSLL VTDRAIGNVI CSIQNPMYDQ EKSKAILLPE
     PFFPKTCPWK VALVCSVLIL LVLLGGISLG IWKEHQVKRR EIKKWSKEHE EMLLLKKGTK
     SVLKIRDDLQ ADLDRRKALY KEDWKKALLY PDWRKELFQE APVRINYEMP DQDKTDSRTE
     ENRGEETVSS SQVDHNLITL SQEGFMLGRY YWEVDVKDTE EWTLGVYELC TQDASLTDPL
     RKFRVLEKNG DGYRALDFCS QNINSEEPLQ LKTRPLKIAI FLDQEDNDLS FYNMTDETHI
     FSFAQVPFLG SPYPYFTRNS MGLSATAQP
 
 
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