CL12B_BOVIN
ID CL12B_BOVIN Reviewed; 276 AA.
AC Q2NL33;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=C-type lectin domain family 12 member B;
GN Name=CLEC12B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitory receptor postulated to negatively regulate immune
CC and non-immune functions (By similarity). Upon phosphorylation,
CC recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its
CC ITIM motif and antagonizes activation signals (By similarity). Although
CC it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known
CC ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart
CC (By similarity). May limit activation of myeloid cell subsets in
CC response to infection or tissue inflammation (By similarity). May
CC protect target cells against natural killer cell-mediated lysis (By
CC similarity). May negatively regulate cell cycle and differentiation of
CC melanocytes via inactivation of STAT3 (By similarity).
CC {ECO:0000250|UniProtKB:Q2HXU8}.
CC -!- SUBUNIT: Homodimer. Interacts (via ITIM motif) with PTPN6. Interacts
CC (via ITIM motif) with PTPN11; this interaction triggers
CC dephosphorylation and activation of PTPN11.
CC {ECO:0000250|UniProtKB:Q2HXU8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2HXU8};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC {ECO:0000250|UniProtKB:Q2HXU8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC111146; AAI11147.1; -; mRNA.
DR RefSeq; NP_001069876.1; NM_001076408.2.
DR AlphaFoldDB; Q2NL33; -.
DR SMR; Q2NL33; -.
DR STRING; 9913.ENSBTAP00000030514; -.
DR PaxDb; Q2NL33; -.
DR GeneID; 616085; -.
DR KEGG; bta:616085; -.
DR CTD; 387837; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q2NL33; -.
DR OrthoDB; 1201127at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR GO; GO:0030545; F:signaling receptor regulator activity; IEA:InterPro.
DR GO; GO:0097325; P:melanocyte proliferation; ISS:UniProtKB.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; ISS:UniProtKB.
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; IPR042916; CLEC12A/B.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR013600; Ly49_N.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47647; PTHR47647; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 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;
KW Phosphoprotein; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..276
FT /note="C-type lectin domain family 12 member B"
FT /id="PRO_0000313580"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 150..264
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT /evidence="ECO:0000250|UniProtKB:Q2HXU8"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q2HXU8"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 172..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 242..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 276 AA; 31835 MW; 9CC30570DF558405 CRC64;
MSEDMTYATL TFQDSVAAGN NQDRNNLRKR GYPAPSSIWR QAALGLLTLC VMLLIGLVTL
GIMFLQMSSE INSDSDKLTQ LQKIIHQQQD NISQQLSKYR NFPVEEEFLK SQISSLLKRQ
GQMAIKLCQE LIIHTSDHKC NPCPKTWKWY QTSCYYFAVN EEKTWPNSRK NCMDKNSTLV
KIDSLEEKDF LRSQPLPKFP FFWLGLSWDP SGRSWLWEDS SRPSPSLFSA YEYAQINESK
GCAYFQNGNI YISRCSAEIS WICEKTAALV KIEDLD
