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LIRA6_PANTR
ID   LIRA6_PANTR             Reviewed;         481 AA.
AC   Q8MJZ2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Leukocyte immunoglobulin-like receptor subfamily A member 6;
DE            Short=Leukocyte immunoglobulin-like receptor E;
DE   Flags: Precursor;
GN   Name=LILRA6; Synonyms=LIRE;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11698452; DOI=10.4049/jimmunol.167.10.5786;
RA   Canavez F.C., Young N.T., Guethlein L.A., Rajalingam R., Khakoo S.I.,
RA   Shum B.P., Parham P.;
RT   "Comparison of chimpanzee and human leukocyte Ig-like receptor genes
RT   reveals framework and rapidly evolving genes.";
RL   J. Immunol. 167:5786-5794(2001).
CC   -!- FUNCTION: May act as receptor for class I MHC antigens. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AF383169; AAL31878.1; -; mRNA.
DR   RefSeq; NP_001009056.1; NM_001009056.1.
DR   AlphaFoldDB; Q8MJZ2; -.
DR   SMR; Q8MJZ2; -.
DR   STRING; 9598.ENSPTRP00000054294; -.
DR   PaxDb; Q8MJZ2; -.
DR   Ensembl; ENSPTRT00000061751; ENSPTRP00000054294; ENSPTRG00000028888.
DR   GeneID; 450148; -.
DR   KEGG; ptr:450148; -.
DR   CTD; 79168; -.
DR   eggNOG; ENOG502RYEX; Eukaryota.
DR   GeneTree; ENSGT01000000214458; -.
DR   HOGENOM; CLU_021100_2_3_1; -.
DR   InParanoid; Q8MJZ2; -.
DR   OrthoDB; 1000446at2759; -.
DR   TreeFam; TF336644; -.
DR   Proteomes; UP000002277; Chromosome 19.
DR   Bgee; ENSPTRG00000028888; Expressed in bone marrow and 9 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032396; F:inhibitory MHC class I receptor activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
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; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Pfam; PF00047; ig; 2.
DR   Pfam; PF13895; Ig_2; 1.
DR   PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..481
FT                   /note="Leukocyte immunoglobulin-like receptor subfamily A
FT                   member 6"
FT                   /id="PRO_0000294368"
FT   TOPO_DOM        24..447
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        469..481
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..118
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          225..314
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          323..408
FT                   /note="Ig-like C2-type 3"
FT   REGION          418..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        144..196
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT   DISULFID        245..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        345..396
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   481 AA;  52438 MW;  3FBFC7E8724BF0FC CRC64;
     MTPALTALLC LGLSLGPRTH VQAGPLPKPT LWAEPGSVIS WRSPVTIWCQ GSLEAQEYRL
     YKEGSREPRD TQNPMEPKNK ARFSIPSMTE HHAGRYRCYY RSPAGWSEPS DPLELVVTGF
     YSTPTLSALP SPVVASGGNV TLRCGSQKGY DHFVLMKEGE HQLPQTLDSQ HLHSGGFQAL
     FPVGPVTPSH RWTFTCYGSY RNTPQVWSHP SDPLEILPSG VSRKPSLLTL QGPVLAPGES
     LTLQCGSDVG YDRFTLYKEG ERDFLQLPGP QPQAGLSQAN FTLGPVSRSH GGQYRCYGAH
     NLSSEWSAPS DPLNILIAGQ FYDRVSLSLQ PDPTVASGEN VTLLCQSQGQ FDTFLLTKEG
     AAHPPLRLRS KYQSQKYQAE FPMNPVTSAH AGTYRCYGSY SSNPHLLSFP SDPLKLMVSG
     PSGGPSLPPT GPPSTPASHA KDYTVENLIR MGMAGLVLVV LGILLFEAQH SQRSPQDAAR
     R
 
 
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