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CLC2L_MOUSE
ID   CLC2L_MOUSE             Reviewed;         211 AA.
AC   P0C7M9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=C-type lectin domain family 2 member L;
GN   Name=Clec2l;
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=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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AC161147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS57419.1; -.
DR   RefSeq; NP_001094977.1; NM_001101507.1.
DR   AlphaFoldDB; P0C7M9; -.
DR   SMR; P0C7M9; -.
DR   STRING; 10090.ENSMUSP00000110524; -.
DR   iPTMnet; P0C7M9; -.
DR   PhosphoSitePlus; P0C7M9; -.
DR   PaxDb; P0C7M9; -.
DR   PeptideAtlas; P0C7M9; -.
DR   PRIDE; P0C7M9; -.
DR   ProteomicsDB; 279103; -.
DR   Antibodypedia; 52522; 61 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000114874; ENSMUSP00000110524; ENSMUSG00000079598.
DR   GeneID; 665180; -.
DR   KEGG; mmu:665180; -.
DR   UCSC; uc029vuf.1; mouse.
DR   CTD; 154790; -.
DR   MGI; MGI:2141402; Clec2l.
DR   VEuPathDB; HostDB:ENSMUSG00000079598; -.
DR   eggNOG; KOG1766; Eukaryota.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000162503; -.
DR   HOGENOM; CLU_1528662_0_0_1; -.
DR   InParanoid; P0C7M9; -.
DR   OMA; DCLMTRP; -.
DR   OrthoDB; 1201127at2759; -.
DR   PhylomeDB; P0C7M9; -.
DR   TreeFam; TF351467; -.
DR   BioGRID-ORCS; 665180; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Clec2l; mouse.
DR   PRO; PR:P0C7M9; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P0C7M9; protein.
DR   Bgee; ENSMUSG00000079598; Expressed in lumbar dorsal root ganglion and 87 other tissues.
DR   Genevisible; P0C7M9; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Lectin; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..211
FT                   /note="C-type lectin domain family 2 member L"
FT                   /id="PRO_0000339386"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..206
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0ZCA7"
FT   DISULFID        125..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        184..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   211 AA;  23653 MW;  147B5192E87612DA CRC64;
     MEPAREPPAR ARPPPPAARP APAAPRPRSP AEAEARGPEG LLRRSGSGYE GSTSWKAALE
     DTTTRLLLGA IAVLLFAILV VMSILASKGC IKCETPCPED WLLYGRKCYY FSEEPRDWNT
     GRQYCHTHEA ALAVIQSQKE LEFMFKFTRR EPWIGLRRVG DDFHWVNGDP FDPDTFTISG
     MGECVFVEPT RLVSTECLTT RPWVCSKMAY T
 
 
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