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CLC2E_MOUSE
ID   CLC2E_MOUSE             Reviewed;         204 AA.
AC   Q80XD9; Q8VI18;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=C-type lectin domain family 2 member E;
DE   AltName: Full=C-type lectin-related protein A;
DE            Short=Clr-a;
GN   Name=Clec2e; Synonyms=Clra;
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 [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=11398965; DOI=10.1007/s002510100319;
RA   Plougastel B., Dubbelde C., Yokoyama W.M.;
RT   "Cloning of Clr, a new family of lectin-like genes localized between mouse
RT   Nkrp1a and Cd69.";
RL   Immunogenetics 53:209-214(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   -!- FUNCTION: Lectin-type cell surface receptor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
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DR   EMBL; AF320600; AAL37200.1; -; Genomic_DNA.
DR   EMBL; BC051091; AAH51091.1; -; mRNA.
DR   AlphaFoldDB; Q80XD9; -.
DR   SMR; Q80XD9; -.
DR   STRING; 10090.ENSMUSP00000032258; -.
DR   GlyGen; Q80XD9; 1 site.
DR   PaxDb; Q80XD9; -.
DR   PRIDE; Q80XD9; -.
DR   ProteomicsDB; 285466; -.
DR   MGI; MGI:3028921; Clec2e.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; Q80XD9; -.
DR   PhylomeDB; Q80XD9; -.
DR   ChiTaRS; Clec2e; mouse.
DR   PRO; PR:Q80XD9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80XD9; protein.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO: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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IBA:GO_Central.
DR   CDD; cd03593; CLECT_NK_receptors_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR033992; NKR-like_CTLD.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..204
FT                   /note="C-type lectin domain family 2 member E"
FT                   /id="PRO_0000315287"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..59
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          84..188
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        105..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        27
FT                   /note="G -> R (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="A -> T (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="V -> S (in Ref. 1; AAL37200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="T -> A (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="S -> P (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="H -> R (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="N -> S (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="R -> C (in Ref. 2; AAH51091)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  22754 MW;  4BA3229004C1C2BC CRC64;
     MLKTDLTAPD CLQEGEMGKK LQAKCLGIIS AASCVKLYCC YGVIMVLTVA VVALSVTLSV
     RKKKPVMESC EPCYAVCSSG WIGFGNKCFY FSEDMGNWTF SQSSCIALDA HLALFDSLEE
     LNFLKRYKGA SDHWIGLHRE SSEHPWIWTD NTEYNNLVLT RGGGECAYLS NRGIYNSSGD
     IHKKWICNKP NNYTLQRPLI VNPG
 
 
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